Professor Nazlin Howell

Emeritis Professor of Food Biochemistry

Qualifications: BSc PhD CChem FRSA FIFST FRSA

Email:
Phone: Work: 01483 68 6448
Room no: 35 AY 03

Further information

Research Interests

Effect of bioactive peptides and proteins on nutritional and functional protperties of food; biochemical changes in frozen fish; processing of and related biochemical studies on the underutilised fish species in Africa and Asia; effect of UV-A mediated skin cell damage and its prevention by metal chelative properties of flavonoids; protein-protein, protein-polysaccharide and protein-lipid interactions; effect of high pressure processing on the structure and physical-chemical properties of proteins; protein-lipid interactions in food gels and emulsions; structural studies and utilisation of Chinese plant products to improve food quality; structure-function relationships of proteins by chemical modification.

Current Research Priorities

Improving the nutritional quality and safety of under-utilised food

I have coordinated major research projects on under-utilised fish species and other staple products in association with developing countries that have been funded by four EC grants (listed individually under the grants section, totalling 3 million euros) involving ten partners in Europe, Africa and Asia. In the last EU project we investigated the nutritional quality of low-value fish and fish oils including the safety of oxidised oils using Caco-2 cells; the effect of natural antioxidants; the presence of pollutants including PCBs, DDT and dioxins in marine fish in collaboration with Unilever Research; production of collagen and gelatin from fish waste skin and innovative extrusion of products including infant weaning foods using staple plant products; this project will reduce waste, pollution and help alleviate food shortages in Africa and Asia in collaboration with FAO and UNICEF as well as industrial partners (SMEs and industrial companies, Masterfoods, Croda, Unilever).

In addition, the Commonwealth Universities Association funded a studentship to study the ‘Biochemical and nutritional properties of sweet potato and its processing into infant weaning foods’ to improve the food processing capability and alleviate food shortages in Uganda.

Further research arising from this project is being undertaken as highlighted below.

Protein-lipid interactions

Elucidation of the mechanisms of protein-lipid interaction is being undertaken (funding by BBSRC, industry, The Royal Society and PhD studentships from Malaysia, Libya and Saudi Arabia,) to improve the quality of products containing polyunsaturated fatty acids, which can minimise cardiovascular and other diseases but are prone to lipid oxidation that can result in toxic products.

Structure and activities of natural antioxidants

The structure and antioxidant properties of natural plant products including vitamin C, vitamin E, rosemary, tea and cocoa polyphenols (BBSRC; EC funding); thyme, thymbra and pimpinella (collaborative student at King Suleimani University, Kurdistan, Iraq), Chinese herbs and green tea ( BBSRC UK-China Partnering award and visits by Chinese Government scholars) are being investigated.

Antioxidant and metal chelative properties of flavonoids in relation to the prevention of UV-A mediated skin cell damage. This collaborative studentship was funded by the King AbdulAziz University, Jeddah, Saudi Arabia (Postgraduate School for Women). The project allows the expertise gained in the protein denaturation and lipid oxidation studies above, to be applied to the investigation of cultured human skin cells subjected to UV damage and the protection offered by the use of flavonoids and other natural antioxidants.

Bioactive peptides from food proteins

Novel and innovative research on peptides derived from food proteins that have health enhancing properties is being undertaken. Hypertension, cholesterol and reactive oxygen species are risk factors associated with cardiovascular disease which is a major cause of death. Research on the antioxidant and antihypertensive effect of fish bioactive peptides is being undertaken by a PhD student from Zambia, funded by the Commonwealth Association of Universities. Novel studies on the isolation of peptides by chromatography and ultrafiltration from chicken flesh and skin (Malaysian Government funding) to study antioxidant and cholesterol lowering activity as well as cholesterol lowering activity of peptides from egg albumen (studentship, Saudi Arabia) and soya proteins are also being investigated.

Effect of high pressure processing on the physico-chemical properties of proteins investigates structural and functional changes in food proteins (egg albumen and whey proteins) and antinutrients (soya proteins), using emerging technologies such as high pressure processing have been undertaken.

Publications

Journal articles

  • Yousr M, Howell N. (2015) 'Antioxidant and ACE Inhibitory Bioactive Peptides Purified from Egg Yolk Proteins'. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 16 (12), pp. 29161-29178.
  • Sarbon, NM, Howell NK, Badii F. (2014) 'THE EFFECT OF CHICKEN SKIN GELATIN AND WHEY PROTEIN INTERACTIONS ON RHEOLOGICAL AND THERMAL PROPERTIES'. Food Hydrocolloids,
    [ Status: Accepted ]

    Abstract

    Physical, thermal and microstructural properties of whey protein isolate (WPI) and chicken skin gelatin mixtures were investigated. This is a first study on the compatibility of an unutilised gelatin source from chicken skin with a well-characterised food protein. The physical-chemical and rheological properties of chicken skin gelatin alone, were reported in our previous paper Sarbon, Badii & Howell, (2013). Preparation and characterisation of chicken skin gelatin as an alternative to mammalian gelatin. Food Hydrocolloids 30, 143-151. In the present study, small deformation rheology indicated that combinations of gelatin (3, 5 and 10 %) and 10 % whey protein (WPI) in distilled water resulted in high elastic modulus (G') values of 1860, 23914 and 20145 Pa, respectively, compared with 120 Pa for 10% WPI alone, due to synergistic interaction. Frequency sweeps showed increased strength of networks in gels containing higher concentrations of gelatin in WPI/gelatin mixtures. Gelatin gels were more stable and stronger than 10 % (w/w)whey protein gels and did not exhibit frequency dependence for G' and G", giving low tan δ (G"/G') values of <0.1. Large deformation gel strength values of all samples increased significantly (p<0.05) with increasing gelatin concentration and were greater at each concentration compared to gelatin alone. Differential scanning calorimetry transition temperature (Tm) and enthalpy change (ΔH) of gelatin and whey protein mixed in the ratios 3:10, 5:10 and 10:10 (w/w) confirmed the reversibility of the gelatin transition on heating to 90 oC and cooling to 10 oC and irreversible denaturation of WPI on heating. The addition of 3, 5 or 10% gelatin to whey protein increased the Tm of whey protein and decreased the Tm of gelatin. However, the presence of 10 % (w/w) WPI significantly increased the ΔH values to 0.62, 1.34 and 2.20 J/g for 3, 5 and 10 % (w/w) gelatin solutions respectively, indicating whey-gelatin interaction. Chicken skin gelatin gels exhibited a fine network of uniform particles whereas whey protein gels comprised aggregates. Differences in structure and molecular size led to phase separation of the mixed gels. The above properties of an underutilized non-mammalian source of gelatin may lead to novel applications in the food industry.

  • Sarbon NM, Cheow CS, Kyaw ZW, Howell NK. (2014) 'Effects of different types and concentration of salts on the rheological and thermal properties of sin croaker and shortfin scad skin gelatin'. International Food Research Journal, 21 (1), pp. 317-324.

    Abstract

    The aims of this study were to examine the effect of salts (CaCl2, CaSO4 and MgSO4) on the rheological and thermal properties of gelatin extracted from the skins of tropical fishes, sin croaker (Johnius dussumeiri) and shortfin scad (Decapterus macrosoma). It was found that the melting temperatures of fish skin gelatins were increased by 1.5 times as compared to bovine gelatin which was only increased by 0.5 times after holding for 2 h at 5°C. The storage (G') and loss (G") modulus of fish skin gelatins were improved with the addition of calcium sulphate (CaSO4) and magnesium sulphate (MgSO4), respectively. However, the storage (G') and loss (G") modulus of gelatin solutions were decreased with the addition of calcium chloride (CaCl2). Magnesium sulphate (MgSO4) was found to be an effective salt to improve the bloom value, elastic and viscous moduli of the fish skin gelatin. This study showed that shortfin scad skin gelatin with salt addition possessed better thermal and rheological properties than sin croaker gelatin ©All Rights Reserved.

  • Dileep AO, Shamasundar BA, Binsi PK, Badii F, Howell NK. (2012) 'Composition, physicochemical and rheological properties of fresh bigeye snapper fish (priacanthus hamrur) mince'. Journal of Food Biochemistry, 36 (5), pp. 577-586.

    Abstract

    Composition and properties of fresh bigeye snapper fish (Priacanthus hamrur) mince has been investigated. The protein content of fish mince was 16.71g/100g mince. Amino acid analysis revealed high proportion of glutamic acid, alanine, lysine and leucine. Fatty acid profile indicated high proportion of eicosa pentaenoic acid and decosa hexaenoic acid content. Gel filtration profile of total proteins from fresh bigeye fish mince revealed a major peak (high molecular weight component) and a few minor peaks, which was further confirmed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis pattern. The differential scanning calorimetry profile of fresh bigeye fish mince revealed transitions at 38.35, 47.72 and 63.02C indicating denaturation temperature of different protein fractions. The gel-forming ability of fresh bigeye fish mince was evaluated by both small strain and large strain tests. The flow behavior of total protein solution from fresh bigeye fish mince as a function of protein concentration and temperature showed pseudoplastic behavior. © 2011 Wiley Periodicals, Inc.

  • Mhd Sarbon N, Badii F, Howell NK. (2012) 'Preparation and characterisation of chicken skin gelatin as an alternative to mammalian gelatin'. Food Hydrocolloids, 30 (1), pp. 143-151.

    Abstract

    The aims of this study were to report for the first time, the extraction and physico-chemical properties of chicken skin gelatin compared to bovine gelatin. Extracted chicken skin gelatin 6.67% (w/v) had a higher bloom value (355 ± 1.48 g) than bovine gelatin (259 ± 0.71 g). The dynamic viscoelastic profile of chicken gelatin exhibited higher viscous and elastic modulus values compared to bovine gelatin for a range of concentrations and frequencies. Thermal properties studied by differential scanning calorimetry (DSC) showed that the melting temperature of 6.67%, chicken skin gelatin was significantly greater (p < 0.05) than that of bovine gelatin, indicating lower stability of bovine gelatin compared to chicken skin gelatin. Results obtained in this study showed that Gly (33.70%), Pro (13.42%), H.Pro (12.13%) and Ala (10.08%) were the most dominant amino acids in chicken skin gelatin which contributed to the higher gel strength and stability. Raman spectra of chicken skin and bovine gelatin were similar and displayed typical protein spectra. Chicken gelatin showed strong hydrogen bonding compared to bovine gelatin as the tyrosine doublet ratio (I 855/I 830) of chicken gelatin was significantly lower than that of bovine gelatin. Significantly, the alpha helix and β-sheet type structures were higher for chicken skin gelatin compared with bovine gelatin. The average molecular weight of chicken gelatin was 285,000 Da. These findings, obtained for the first time for chicken skin gelatin, show that it has high potential for application as an alternative to commercial gelatin. © 2012 Elsevier Ltd.

  • Leelapongwattana K, Benjakul S, Visessanguan W, Howell NK. (2010) 'EFFECTS OF TRIMETHYLAMINE-N-OXIDE DEMETHYLASE (TMAOase) INHIBITORS AND ANTIOXIDANTS ON PHYSICOCHEMICAL AND BIOCHEMICAL CHANGES OF HADDOCK MUSCLE INDUCED BY LIZARDFISH TMAOase DURING FROZEN STORAGE'. JOURNAL OF FOOD BIOCHEMISTRY, 34 (5), pp. 1032-1048.
  • Howell NK, Kasase C. (2010) 'Bioactive Peptides and Proteins from Fish Muscle and Collagen'. , pp. 203-223.
  • Dileep AO, Shamasundar BA, Binsi PK, Howell NK. (2010) 'COMPOSITION AND QUALITY OF RICE FLOUR-FISH MINCE BASED EXTRUDED PRODUCTS WITH EMPHASIS ON THERMAL PROPERTIES OF RICE FLOUR'. J TEXTURE STUD, 41 (2), pp. 190-207.
  • Howell NK, Kasase C. (2009) 'Angiotensin I converting enzyme (ACE) inhibitory activity and antioxidant behavior of Atlantic mackerel peptides'. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 237, pp. 93-93.
  • Binsi PK, Shamasundar BA, Dileep AO, Badii F, Howell NK. (2009) 'Rheological and functional properties of gelatin from the skin of Bigeye snapper (Priacanthus hamrur) fish: Influence of gelatin on the gel-forming ability of fish mince'. Food Hydrocolloids, 23 (1), pp. 132-145.

    Abstract

    The rheological and functional properties of gelatin from the skin of bigeye snapper (Priacanthus hamrur) fish were assessed. The protein content of dried gelatin was 94.6% and moisture content was 4.2%. The amino acid profile of gelatin revealed high proportion of glycine and imino acids. The bloom strength of solidified gelatin was 108 g. The average molecular weight of fish skin gelatin was 282 kDa as determined by gel filtration technique. The emulsion capacity (EC) of gelatin at a concentration of 0.05% (w/v) was 1.91 ml oil/mg protein and with increase in concentration, the EC values decreased. The gelling and melting temperatures of gelatin were 10 and 16.8 °C, respectively as obtained by small deformation measurements. The flow behavior of gelatin solution as a function of concentration and temperature revealed non-Newtonian behavior with pseudoplastic phenomenon. The Casson and Herschel-Bulkley models were suitable to study the flow behavior. The yield stress was maximum at 10 °C with the concentration of 30 mg/ml. Thermal gelation behavior of threadfin bream (Nemipterus japonicus) mince in presence of different concentration of gelatin was assessed. Gelatin at a concentration of 0.5% yielded higher storage modulus (G′) value than control. Frequency sweep of heat set gel with gelatin revealed strong network formation. © 2007 Elsevier Ltd. All rights reserved.

  • Alghazeer R, Gao H, Howell NK. (2008) 'Cytotoxicity of oxidised lipids in cultured colonal human intestinal cancer cells (caco-2 cells)'. TOXICOLOGY LETTERS, 180 (3), pp. 202-211.
  • Alghazeer R, Saeed S, Howell NK. (2008) 'Aldehyde formation in frozen mackerel (Scomber scombrus) in the presence and absence of instant green tea'. FOOD CHEMISTRY, 108 (3), pp. 801-810.
  • Alghazeer R, Howell NK. (2008) 'Formation of 4-hydroxynonenal (4-HNE) in frozen mackerel (Scomber scombrus) in the presence and absence of green tea'. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 88 (7), pp. 1128-1134.
  • Leelapongwattana K, Benjakul S, Visessanguan W, Howell NK. (2008) 'Effect of some additives on the inhibition of lizardfish trimethylamine-N-oxide demethylase and frozen storage stability of minced flesh'. INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY, 43 (3), pp. 448-455.
  • Leelapongwattana K, Benjakul S, Visessanguan W, Howell NK. (2008) 'Effect of trimethylamine-N-oxide demethylase from lizardfish kidney on biochemical changes of haddock natural actomyosin stored at 4 and -10 degrees C'. EUROPEAN FOOD RESEARCH AND TECHNOLOGY, 226 (4), pp. 833-841.
  • Sarkardei S, Howell NK. (2008) 'Effect of natural antioxidants on stored freeze-dried food product formulated using horse mackerel (Trachurus trachurus)'. INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY, 43 (2), pp. 309-315.
  • Leelapongwattana K, Benjakul S, Visessanguan W, Howell NK. (2008) 'Raman spectroscopic analysis and rheological measurements on natural actomyosin from haddock (Melanogrammus aeglefinus) during refrigerated (4 degrees C) and frozen (-10 degrees C) storage in the presence of trimethylamine-N-oxide demethylase from kidney of lizardfish (Saurida tumbil)'. FOOD CHEMISTRY, 106 (3), pp. 1253-1263.
  • Kasase C, Ganeshalingam A, Howell NK. (2008) 'Antioxidant activity of soy protein hydrolysate and peptides'. Gums and Stabilisers for the Food Industry 14, , pp. 402-406.
  • Davila E, Pares D, Howell NK. (2007) 'Studies on plasma protein interactions in heat-induced gels by differential scanning calorimetry and FT-Raman spectroscopy'. FOOD HYDROCOLLOIDS, 21 (7), pp. 1144-1152.
  • Wu W, Clifford M, Howell NK. (2007) 'The effect of instant green tea on the foaming and rheological properties of egg albumen proteins'. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 87 (10), pp. 1810-1819.
  • Rahimuddin SA, Khoja SM, Zuhair MM, Howell NK, Brown JE. (2007) 'Inhibition of lipid peroxidation in UVA-treated skin fibroblasts by luteolin and its glucosides'. EUROPEAN JOURNAL OF LIPID SCIENCE AND TECHNOLOGY, 109 (7), pp. 647-655.
  • Intarasirisawat R, Benjakul S, Visessanguan W, Prodpran T, Tanaka M, Howell NK. (2007) 'Autolysis study of bigeye snapper (Priacanthus macracanthus) skin and its effect on gelatin'. FOOD HYDROCOLLOIDS, 21 (4), pp. 537-544.
  • Sarkardei S, Howell NK. (2007) 'The effects of freeze-drying and storage on the FT-Raman spectra of Atlantic mackerel (Scomber scombrus) and horse mackerel (Trachurus trachurus)'. FOOD CHEMISTRY, 103 (1), pp. 62-70.
  • Cheow CS, Norizah MS, Kyaw ZY, Howell NK. (2007) 'Preparation and characterisation of gelatins from the skins of sin croaker (Johnius dussumieri) and shortfin scad (Decapterus macrosoma)'. FOOD CHEMISTRY, 101 (1), pp. 386-391.
  • Davila E, Pares D, Howell NK. (2006) 'Fourier transform Raman spectroscopy study of heat-induced gelation of plasma proteins as influenced by pH'. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 54 (20), pp. 7890-7897.
  • Saeed S, Gillies D, Wagner G, Howell NK. (2006) 'ESR and NMR spectroscopy studies on protein oxidation and formation of dityrosine in emulsions containing oxidised methyl linoleate'. FOOD AND CHEMICAL TOXICOLOGY, 44 (8), pp. 1385-1392.
  • Badii F, Howell NK. (2006) 'Fish gelatin: Structure, gelling properties and interaction with egg albumen proteins'. FOOD HYDROCOLLOIDS, 20 (5), pp. 630-640.
  • Dileep AO, Shamasundar BA, Binsi PK, Badii E, Howell NK. (2005) 'Effect of ice storage on the physicochemical and dynamic viscoelastic properties of ribbonfish (Trichiurus spp) meat'. JOURNAL OF FOOD SCIENCE, 70 (9), pp. E537-E545.
  • Leelapongwattana K, Benjakul S, Visessanguan W, Howell NK. (2005) 'Physicochemical and biochemical changes in whole lizardfish (saurida micropectoralis) muscles and fillets during frozen storage'. Journal of Food Biochemistry, 29 (5), pp. 547-569.

    Abstract

    The physicochemical and biochemical changes in whole lizardfish (Saurida micropectoralis) muscles and its fillets kept in air and under vacuum during frozen storage at -20C for 24 weeks were investigated. The formaldehyde (FA) and dimethylamine contents increased with a concomitant decrease in trimethylamine-N-oxide (TMAO) content as the storage time increased (P < 0.05). The Ca2+-adenosine 5′-triphosphatase activity continuously decreased with a coincidental decrease in salt-soluble fraction. The disulfide bonds were increasingly formed throughout the storage (P < 0.05). The surface hydrophobicity increased and reached the maximum at week 12 with a subsequent decrease up to the end of storage. In general, the higher changes were observed in samples kept under vacuum than those kept in air. With the same atmosphere used, the whole fish showed slightly higher changes than the fillets. A marked increase in TMAO demethylase (TMAOase) activities was observed up to 12 weeks, followed by the continuous decrease up to 24 weeks © Copyright 2005, Blackwell Publishing.

  • Leelapongwattana K, Benjakul S, Visessanguan W, Howell NK. (2005) 'Physicochemical and biochemical changes during frozen storage of minced flesh of lizardfish (Saurida micropectoralis)'. Food Chemistry, 90 (1-2), pp. 141-150.

    Abstract

    Physicochemical and biochemical changes of minced flesh of lizardfish (Saurida micropectoralis) kept in air and vacuum during frozen storage at -20°C for 24 weeks were investigated. Formaldehyde and dimethylamine (DMA) contents increased with a concomitant decrease in trimethylamine oxide (TMAO) content as the storage time increased (P<0.05). Ca2+-ATPase activity decreased continuously with a coincidental decrease in the salt-soluble fraction. Disulfide bonds were increasingly formed throughout the storage (P<0.05). Nevertheless, surface hydrophobicity increased and reached a maximum at week 4 with a subsequent decrease up to the end of storage. In general, greater changes were observed in lizardfish mince kept under vacuum than in air. A marked increase in trimethylamine-N-oxide demethylase (TMAOase) activities was observed up to 6 weeks, followed by continuous decrease up to 24 weeks of storage. TMAOase activity, as well as formaldehyde formation, could be reduced to some extent with packaging containing oxygen. © 2004 Elsevier Ltd. All rights reserved.

  • Badii F, Zhdan P, Howell NK. (2004) 'Elucidation of protein aggregation in frozen cod and haddock by transmission electron microscopy/immunocytochemistry, light microscopy and atomic force microscopy'. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 84 (14), pp. 1919-1928.
  • Saeed S, Howell NK. (2004) 'Rheological and differential scanning calorimetry studies on structural and textural changes in frozen Atlantic mackerel (Scomber scombrus)'. Journal of the Science of Food and Agriculture, 84 (10), pp. 1216-1222.

    Abstract

    The viscoelastic behaviour and thermal stability of Atlantic mackerel fillets stored at -20 and -30°C for up to 2 years were investigated. An increase in elastic (G′) and viscous (G″) modulus values, reflecting protein aggregation, was observed in samples stored at -20°C compared with those stored at -30′C, as well as with storage time. The results indicate that toughening on frozen storage is not just limited to lean gadoid fish but also occurs in fatty fish, leading to texture deterioration. Differential scanning calorimetry of fillets stored at -20°C showed a shift to a lower transition temperature (T m) and a decrease in enthalpy (ΔH) compared with control fillets stored at -30°C; this change was enhanced when fillets were stored for a longer period of time, confirming protein denaturation and the formation of aggregates reported previously by the authors (J Sci Food Agric 82: 579-586 (2002)). The contribution of lipid oxidation to protein aggregation was shown by storing minced mackerel with or without the antioxidant vitamin E at -10°C. The G′ and G″ values were higher in samples stored without vitamin E than in samples stored with vitamin E; thus antioxidants may be used to minimise protein aggregation in fatty fish. The role of lipid oxidation in promoting protein aggregation and deterioration in the texture of fatty fish has not been reported hitherto. Antioxidants such as vitamin E may be used not only to prevent lipid oxidation but also to minimise protein damage in order to prolong the shelf-life of fatty fish. © 2004 Society of Chemical Industry.

  • Cheow CS, Kyaw ZY, Howell NK, Dzulkifly MH. (2004) 'Relationship between physicochemical properties of starches and expansion of fish cracker 'keropok''. Journal of Food Quality, 27 (1), pp. 1-12.

    Abstract

    The influence of physicochemical properties of starches on expansion of 'keropok' was studied. Swelling power, solubility, and amylose leaching of a starch were dependent on the lipid and protein contents of the starch. The morphology of different starch granules used in 'keropok' gel was observed using scanning electron microscopy. The sizes of swollen starch granules in the gel were quantitatively measured by image analysis. The average length and width of swollen gelatinized sago and tapioca starch granules were significantly higher than that of wheat starch, and consequently, the linear expansion of 'keropok' with wheat starch was lower than those of 'keropok' made with tapioca or sago starches. Linear expansion was positively correlated to swelling power and solubility of the starch. Textural properties of 'keropok' gels with different starches were also measured and found to have correlation with linear expansion of the final products.

  • Howell NK. (2004) 'The chemistry of quality enhancement in low-value fish.'. Adv Exp Med Biol, United States: 542, pp. 135-145.
  • Ngarize S, Adams A, Howell NK. (2004) 'Studies on egg albumen and whey protein interactions by FT-Raman spectroscopy and rheology'. Food Hydrocolloids, 18 (1), pp. 49-59.

    Abstract

    Large deformation rheological studies of either egg albumen or whey protein isolate (15% protein w/w) gels made by heating at 90 °C for 30 min indicated a higher gel strength and Young's modulus values for egg albumen compared to whey protein isolate. The proteins mixed in the ratio 10:5 whey/egg albumen indicated synergistic interactions producing greater than expected gel strength values. Small deformation rheological studies of egg albumen 15% (w/w) and whey protein isolate 15% (w/w) showed very low values of the storage modulus (G′) at 20 °C suggesting that both proteins do not easily aggregate at room temperature. Whey proteins gelled at 80 °C, whereas egg albumen proteins were already cross-linked at 20 °C (G′ > G″. A mixture of 7.5% whey/7.5% egg albumen showed the highest G′ value at the end of both heating and cooling cycles but this value was lower than that of the individual proteins. Changes in the conformation, molecular structure and protein-protein interactions in whey and egg albumen (15% w/w in D 2O pD7.2) and their mixtures (7.5:7.5 protein w/w) were investigated by FT-Raman spectroscopy. Upon heating to 90 °C for 30 min, individual whey and egg albumen proteins showed changes in the CH (1350 cm-1), CH2 (1450 cm-1) bending vibrations and Trp residues at 760 cm-1, reflecting involvement of hydrophobic interactions. Changes in the disulphide stretching vibrations were also observed. Peak intensity increased for β-sheet structures in the Amide 111′ region 980-990 cm-1 and decreased for helix structures (900-960 cm -1) for both egg albumen and whey proteins. Differences in the experimental and theoretical average spectra indicated changes in β-sheet structures, CH2 bending, carboxyl and hydrophobic groups in heated binary mixtures of egg albumen and whey proteins, providing evidence of protein-protein interactions, observed by large deformation rheology. © 2003 Elsevier Ltd. All rights reserved.

  • Comfort S, Howell NK. (2003) 'Gelation properties of salt soluble meat protein and soluble wheat protein mixtures'. Food Hydrocolloids, 17 (2), pp. 149-159.

    Abstract

    Salt soluble meat proteins (SSMP) and commercially available soluble wheat proteins (SWP) were characterised by SDS-polyacrylamide gel electrophoresis, differential scanning calorimetry (DSC) and small and large deformation testing. DSC scans indicated transitions similar to those of native actomyosin for the salt soluble meat extract whereas SWP did not indicate any transitions between 20 and 120 °C. Small deformation tests on SWP indicated a G′/G″ crossover gelation temperature of 90 °C and weak gels as judged by frequency sweeps. In contrast, SSMP gelled at 40 °C and formed strong gels on heating to 90 °C. However, on autoclaving at 120 °C, 20% SWP in distilled water produced strong elastic gels with little syneresis, compared with the more brittle gels produced with 20% (w/w) SSMP as indicated by large deformation testing. Mixtures of the two proteins in the ratio SSMP/SWP (15:5) gave strong elastic gels similar to the SWP gels. Even the presence of very small amounts of SWP in the mixture, e.g. SSMP/SWP 20:1 trebled the elastic modulus compared with a SSMP gel and reduced syneresis. This was probably due to the close association of SWP with actomyosin strands as viewed by transmission electron microscopy. However, increased levels of SWP in the mixture, for example SSMP/SWP 10:10 ratio, resulted in the separation of the two protein phases as shown by phase contrast microscopy, and consequently led to lower G′ values in the mixed gels. The addition of 20 mM chloride salts showed that potassium reduced the shear modulus, sodium had no effect and calcium enhanced the shear modulus for SWP gels formed at 120 °C. In contrast, SSMP gels were stronger in the presence of potassium, followed by sodium and calcium. © 2002 Elsevier Science Ltd. All rights reserved.

  • Badii F, Howell NK. (2003) 'Elucidation of the effect of formaldehyde and lipids on frozen stored cod collagen by FT-Raman spectroscopy and differential scanning calorimetry'. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 51 (5), pp. 1440-1446.
  • Comfort S, Howell NK. (2002) 'Gelation properties of soya and whey protein isolate mixtures'. Food Hydrocolloids, 16 (6), pp. 661-672.

    Abstract

    Gelation properties of commercially available soya and whey protein isolates (15-18% w/w) were tested in isolation and when mixed in ratios ranging from 17:1 to 1:17 soya/whey to give a final protein concentration of 18% protein (w/w) in distilled water. The isolates and mixtures were investigated by both small and large deformation rheological analysis, which indicated phase separation of the two proteins systems. Phase inversion occurred at 5:1 ratio (soya/whey) where the lowest shear modulus value, by large deformation testing, was 3.5 compared to 5.5 for 18% (w/w) soya and 10.7 for 18% (w/w) whey proteins in distilled water. The G′ value obtained by small deformation testing, also showed the lowest value at the 5:1 ratio (soya/whey proteins). In addition, gels exhibited maximum syneresis at this ratio indicating instability at the point of inversion. Electron microscopy in combination with immunocytochemistry using anti-soya or anti-whey antibodies also indicated phase separation of the two types of proteins. Phase separation was considered to occur due to differences in the molecular sizes of the proteins and physical-chemical differences including hydrophobicity as verified by the cis-parinaric fluorescent probe technique. © 2002 Elsevier Science Ltd. All rights reserved.

  • Badii F, Howell NK. (2002) 'Changes in the texture and structure of cod and haddock fillets during frozen storage'. FOOD HYDROCOLLOIDS, 16 (4) Article number PII S0268-005X(01)00104-7 , pp. 313-319.
  • Badii F, Howell NK. (2002) 'Effect of antioxidants, citrate, and cryoprotectants on protein denaturation and texture of frozen cod (Gadus morhua)'. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 50 (7), pp. 2053-2061.
  • Saeed S, Howell NK. (2002) 'Effect of lipid oxidation and frozen storage on muscle proteins of Atlantic mackerel (Scomber scombrus)'. Journal of the Science of Food and Agriculture, 82 (5), pp. 579-586.

    Abstract

    The effect of storage on the lipids and proteins in Atlantic mackerel stored for up to 24 months at -20 and -30°C was studied. Traditional methods including the peroxide value, thiobarbituric acid-reactive substances (TBARS) and a reverse phase HPLC method were used to determine the primary and secondary lipid oxidation products. All tests showed an increase in lipid oxidation products with storage time and at a higher storage temperature of -20°C compared with samples stored at -30°C. Antioxidants had a significant effect (P < 0.01) on the inhibition of lipid oxidation, as shown by the reduction in peroxide value and hydroxides, and malondialdehyde formation. Similarly, deterioration of protein structure and functionality in mackerel stored for 3, 6, 12 and 24 months was greater at -20 than -30°C. ATPase activity in the myosin extract of Atlantic mackerel showed a significant decrease (P < 0.01) with progressive frozen storage. Protein solubility in high salt concentration (0.6M NaCl) decreased (P < 0.01) during storage at both -20 and -30°C but was greater at -20°C. Interestingly, antioxidants BHT, vitamin C and vitamin E protected the proteins against complete loss of ATPase activity and protein solubility to a significant level (P < 0.01) for up to 1 year at -20°C compared with samples stored without antioxidants. This study confirms the deleterious effect of lipid oxidation products on protein structure and function in frozen fatty fish. © 2002 Society of Chemical Industry.

  • Badii F, Howell NK. (2002) 'A comparison of biochemical changes in cod (Gadus morhua) and haddock (Melanogrammus aeglefinus) fillets during frozen storage'. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 82 (1), pp. 87-97.
  • Saeed S, Howell NK. (2001) '12-Lipoxygenase activity in the muscle tissue of Atlantic mackerel (Scomber scombrus) and its prevention by antioxidants'. Journal of the Science of Food and Agriculture, 81 (8), pp. 745-750.

    Abstract

    Lipoxygenase was prepared from Atlantic mackerel muscle using differential centrifugation, ammonium sulphate precipitation and gel permeation (phenyl Sephadex G-50) column chromatography. The crude lipoxygenase enzyme preparation was characterised by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), which showed two prominent bands with molecular weights of 119 and 125kDa. Fractions collected from the chromatography column were tested for enzyme activity by reacting with arachidonic acid and determining the production of hydroxyeicosatetraenoic acid (12-HETE) using reverse phase HPLC and GC-MS. The 12-HETE peak was absent from the fresh arachidonic acid control sample and from arachidonic acid treated with heat-inactivated lipoxygenase. Esculetin, a known inhibitor of lipoxygenase, inhibited the production of 12-HETE from the reaction of lipoxygenase with arachidonic acid, thus confirming that the enzyme was lipoxygenase. The HETE peak was partially reduced in the presence of antioxidants, namely synthetic butylated hydroxytoluene (BHT) and natural antioxidants vitamins C and E. The presence of lipoxygenase in Atlantic mackerel muscle indicates the possibility that the lipid oxidation mechanism is initiated enzymatically in chilled and frozen stored fillets of mackerel and that this oxidative deterioration could be inhibited by antioxidants (BHT, vitamins C and E) which are used widely in the food industry. © 2001 Society of Chemical Industry.

  • Howell NK, Herman H, Li-Chan EC. (2001) 'Elucidation of protein-lipid interactions in a lysozyme-corn oil system by Fourier transform Raman spectroscopy.'. J Agric Food Chem, United States: 49 (3), pp. 1529-1533.

    Abstract

    Lysozyme (25% in D2O, corn oil, and their emulsions (10% w/w oil/D2O solution) were examined by Fourier transform Raman spectroscopy. Emulsions showed three layers, namely, top oil, middle cream, and bottom aqueous layers. Raman spectral analysis revealed hydrophobic interactions involving both protein and lipid components. Compared to lysozyme in D2O, the difference spectrum obtained after subtraction of oil from the cream layer spectrum showed reduced intensity of tryptophan bands at 760, 1013, 1340, and 1360 cm(-)(1), reduced intensity ratio of the tyrosine doublet at 850 and 830 cm(-)(1), and increased intensity of the C-H bending band at 1455 cm(-)(1). Compared to corn oil, the difference spectrum after subtraction of lysozyme from the cream layer spectrum indicated decreased intensity at 2855 cm(-)(1) (lipid CH(2) symmetric stretch) and 3011 cm(-)(1) (unsaturated fatty acid hydrocarbon chain =C-H stretch) and a higher intensity ratio of the C-H stretching band at 2900 cm(-)(1) to bands at 2885 and 2933 cm(-)(1). Spectra of the top and bottom layers resembled corn oil and lysozyme, respectively, except for changes in the D2O band. Raman spectroscopy can be used to detect structural changes in proteins, lipids, and D2O due to protein-lipid interactions.

  • Kyaw ZY, Yu SY, Cheow CS, Dzulkifly MH, Howell NK. (2001) 'Effect of fish to starch ratio on viscoelastic properties and microstructure of fish cracker ('keropok') dough'. International Journal of Food Science and Technology, 36 (7), pp. 741-747.

    Abstract

    Starch granules found at the centre of fish crackers ('keropok') which contained from 0 to 10% fish did not gelatinize after 2 h steaming. This was because of water movement from the centre to the periphery during steaming. A fish protein network started to develop in dough with a 15% fish content and this entrapped water molecules. These water molecules helped to complete gelatinization. The viscoelastic properties of 'keropok' dough increased with an increasing fish to starch ratio and also because of the formation of a fish-protein network in the dough.

  • Cheow CS, Yu SY, Howell NK, Man YC, Muhammad K. (1999) 'Effect of fish, starch and salt contents on the microstructure and expansion of fish crackers ('keropok')'. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 79 (6), pp. 879-885.
  • Cheow CS, Yu SY, Howell NK. (1999) 'Effect of salt, sugar and monosodium glutamate on the viscoelastic properties of fish cracker ("keropok") gel'. Journal of Food Processing and Preservation, 23 (1), pp. 21-37.

    Abstract

    Rheological and microscopic studies were carried out on the fish cracker ('keropok') gels. A hard gel is very important for the production of uniform, round, and thin slices of dried 'keropok' and easier for mechanical slicing. The addition of 2% salt in the 'keropok' gel increased the storage modulus (G′), and reduced loss tangent (tan δ = G″/G′). An increase in the fish content in 'keropok' also increased the G′ and reduced tan δ. Gels having higher values of storage modulus G′ and lower tan δ values, indicative of a strong elastic network, showed well crosslinked fish muscle bundles in the microscopy studies. In the absence of salt, the fish protein appeared to be in lumps and this has resulted in low storage modulus G′ and higher tan δ values. Lower the temperature of the gel to 5C will result in 5-6 fold increase in the G′ value.

  • Howell NK, Arteaga G, Nakai S, Li-Chan EC. (1999) 'Raman spectral analysis in the C-H stretching region of proteins and amino acids for investigation of hydrophobic interactions.'. J Agric Food Chem, UNITED STATES: 47 (3), pp. 924-933.

    Abstract

    Raman spectra of amino acids showed complexity in the C-H stretching region (2800-3100 cm(-)(1)) attributed to diversity of CH, CH(2), and CH(3) groups in the side chains, ionization state, and microenvironment. The involvement of specific amino acids in the C-H stretching region of selected proteins, namely, lysozyme, alpha-lactalbumin, beta-lactoglobulin, and their binary mixtures, was investigated by deconvolution using maximum likelihood techniques. The main protein band near 2940 cm(-)(1) was attributed not only to aromatic and aliphatic amino acids but also to many other amino acids. A band near 3065 cm(-)(1) was assigned to aromatic residues, whereas bands near 2880 and 2900 cm(-)(1) corresponded primarily to aliphatic amino acids. Heating at 90 degrees C increased relative intensity near 2940 cm(-)(1) and decreased relative intensity at 2895-2902 cm(-)(1) for lysozyme and its mixtures with alpha-lactalbumin or beta-lactoglobulin. Additional bands at 2812 or 2838 and 3003 cm(-)(1) were observed after heating or in 8 M deuterated urea, reflecting changes upon denaturation.

  • Saeed S, Howell NK. (1999) 'High-performance liquid chromatography and spectroscopic studies on fish oil oxidation products extracted from frozen Atlantic mackerel'. JAOCS, Journal of the American Oil Chemists' Society, 76 (3), pp. 391-397.

    Abstract

    The formation of stable hydroxy derivatives from hydroperoxides produced during the oxidation of linoleic acid methyl ester and fish oil were studied by reverse-phase high-performance liquid chromatography (HPLC), gas chromatography-mass spectrometry (GC-MS) and 13C nuclear magnetic resonance (NMR) spectroscopy. The oxidation products identified were mixtures of four isomeric hydroxy derivatives: 13-hydroxy-9-cis, 11-trans-octadecadienoic, 13-hydroxy-9-trans, 11-trans-octadecadienoic, 9-hydroxy-10-trans, 12-cis-octadecadienoic, and 9-hydroxy-10-trans, 12-trans-octadecadienoic acids. The presence of hydroxy compounds was confirmed by 13C NMR, which gave rise to a hydroxy carbon peak at 87 ppm, and by GC-MS, which showed three peaks corresponding to isomeric mixtures of trimethylsilyl ethers of the oxidized linoleic acid methyl ester. The mass spectra scans of the three peaks showed that they represent isomers of molecular weight 382 and are consistent with the molecular formula C 22H 42O 3Si. In oil extracted from stored frozen mackerel, 13-hydroxy-9-cis, 11-trans-octadecadienoic acid was more prominent compared to the model lipid systems. HPLC offered a sensitive means of detection of hydroxy compounds produced both in the initiation and latter stages of oxidation. The effect of antioxidants added to the fish mince prior to storage can also be monitored by HPLC. Thus, the monitoring of lipid oxidation hydroxy derivatives by HPLC is of practical value in the efficient processing and quality control of fish, fish oils, and other fatty foodstuffs in order to enhance the acceptability, nutritional, and safety aspects.

  • Saeed S, Fawthrop SA, Howell NK. (1999) 'Electron spin resonance (ESR) study on free radical transfer in fish lipid-protein interaction'. Journal of the Science of Food and Agriculture, 79 (13), pp. 1809-1816.

    Abstract

    Oxidised lipids interact with proteins causing undesirable changes in the nutritional and functional properties, including a loss of amino acids, cross-linking and damage to proteins and DNA. Proteins including egg lysozyme, egg ovalbumin, fish myosin and amino acids arginine, lysine and histidine were exposed to oxidised lipids methyl linoleate and oil extracted from Atlantic mackerel (Scomber scombrus). A strong central singlet signal was induced in the proteins and amino acids which was detected by ESR spectroscopy and assigned to the carbon radical (g value range 2.0021-2.0049); with ovalbumin and fish myosin a downfield shoulders, attributed to the sulphydryl group (g value 2.014-2.017), was also observed. The above changes in the proteins were accompanied by an increase in fluorescence indicating the formation of cross-links. Synthetic antioxidants such as butyl hydroxytoluene (BHT) and butyl hydroxyanisole (BHA) as well as natural antioxidants ascorbic acid and α-tocopherol inhibited the development of both the free radical signal and fluorescence when added to the proteins prior to incubation with oxidised lipids; the central singlet signal attributed to the carbon radical was reduced by 10-50%. This paper clearly indicates direct free radical transfer from oxidised lipids to amino acids and proteins which results in protein denaturation and the formation of insoluble aggregates in fish flesh on storage.

  • Cheow CS, Yu SY, Howell NK, Che Man Y, Muhammad K. (1999) 'Effect of fish, starch and salt contents on the microstructure and expansion of fish crackers ('keropok')'. Journal of the Science of Food and Agriculture, 79 (6), pp. 879-885.

    Abstract

    Light microscopy studies on the fish cracker gel and expanded product ('keropok') emphasised the role of fish proteins in the starch expansion process. The addition of salt (20 g kg-1) in the 'keropok' helped to distribute evenly the starch in the fish protein. Formation of thin fish muscle bundles assisted the expansion of 'keropok'. At 700-900 g kg-1 fish content, the fish muscle bundles formed a continuous network that caused a drop in the 'keropok' expansion. From the scanning electron microscopy study, ridges were found in samples (containing 600-900 g kg-1 fish content) with 20 g kg-1 salt at high magnification.

  • Howell NK, Yeboah NA, Lewis DFV. (1995) 'Studies on the electrostatic interactions of lysozyme with alpha-lactalbumin and beta-lactoglobulin'. INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY, 30 (6), pp. 813-824.
  • HOWELL NK, TAYLOR C. (1995) 'EFFECT OF ASCORBIC-ACID ON THE FOAMING AND GELLING OF GLOBULAR-PROTEINS'. INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY, 30 (3), pp. 321-334.
  • HOWELL NK, TAYLOR C. (1991) 'EFFECT OF AMIDATION ON THE FOAMING AND PHYSICOCHEMICAL PROPERTIES OF BOVINE SERUM-ALBUMIN'. INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY, 26 (4), pp. 385-395.
  • MURPHY MC, HOWELL NK. (1991) 'EFFECT OF THE ATTACHMENT OF VALINE RESIDUES ON THE PHYSICOCHEMICAL AND FUNCTIONAL-PROPERTIES OF BOVINE SERUM-ALBUMIN'. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 54 (2), pp. 245-253.
  • MURPHY MC, HOWELL NK. (1991) 'FUNCTIONAL-PROPERTIES OF NATIVE AND POSITIVELY AND NEGATIVELY CHARGED MODIFIED BOVINE SERUM-ALBUMIN'. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 55 (3), pp. 489-492.
  • MURPHY MC, HOWELL NK. (1991) 'EFFECTS OF THE ATTACHMENT OF SMALL MOLECULES BY CARBODIIMIDE-MEDIATED CONDENSATION ON THE PHYSICOCHEMICAL AND FUNCTIONAL-PROPERTIES OF BOVINE SERUM-ALBUMIN'. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 55 (1), pp. 117-140.
  • MURPHY MC, HOWELL NK. (1990) 'EFFECT OF SUCCINYLATION ON THE FUNCTIONAL AND PHYSICOCHEMICAL PROPERTIES OF BOVINE SERUM-ALBUMIN'. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 51 (1), pp. 109-123.
  • MURPHY MC, HOWELL NK. (1990) 'EFFECT OF THIOLATION ON THE PHYSICOCHEMICAL AND FUNCTIONAL-PROPERTIES OF BOVINE SERUM-ALBUMIN'. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 53 (4), pp. 549-558.
  • HOWELL NK, LAWRIE RA. (1987) 'FUNCTIONAL-ASPECTS OF BLOOD-PLASMA PROTEINS .5. VISCOSITY'. INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY, 22 (2), pp. 145-151.
  • HOWELL NK, LAWRIE RA. (1985) 'FUNCTIONAL-ASPECTS OF BLOOD-PLASMA PROTEINS .4. ELUCIDATION OF THE MECHANISM OF GELATION OF PLASMA AND EGG-ALBUMIN PROTEINS'. JOURNAL OF FOOD TECHNOLOGY, 20 (4), pp. 489-504.
  • HOWELL NK, LAWRIE RA. (1984) 'FUNCTIONAL-ASPECTS OF BLOOD-PLASMA PROTEINS .2. GELLING PROPERTIES'. JOURNAL OF FOOD TECHNOLOGY, 19 (3), pp. 289-295.
  • HOWELL NK, LAWRIE RA. (1984) 'FUNCTIONAL-ASPECTS OF BLOOD-PLASMA PROTEINS .3. INTERACTION WITH OTHER PROTEINS AND STABILIZERS'. JOURNAL OF FOOD TECHNOLOGY, 19 (3), pp. 297-313.

Conference papers

  • Tan S-T, Rai B, Boustead L, Badii F, Howell N, Frost G, Scott J, Elliott P, Chambers JC, Koner JS. (2013) 'Assessing the Contribution of Dietary Factors to the Increased Prevalence of Insulin Resistance Amongst Uk Indian Asians Compared to Europeans'. LIPPINCOTT WILLIAMS & WILKINS CIRCULATION, Dallas, TX: Scientific Sessions and Resuscitation Science Symposium of the American-Heart-Association 128 (22)
  • Howell NK, Saeed S, Gillies D. (2005) 'ESR and NMR spectroscopy studies on emulsions containing lactoglobulin and oxidised methyl linoleate'. ROYAL SOC CHEMISTRY Magnetic Resonance in Food Science: The Multivariate Challenge, Royal Vet & Agr Univ, Copenhagen, DENMARK: 7th International Conference on Applications of Magnetic Resonance in Food Science, pp. 104-112.
  • Howell NK, Badii F. (2004) 'Fish gelatin: Structure, gelling properties and interactions with other food proteins'. ROYAL SOC CHEMISTRY GUMS AND STABILIZERS FOR THE FOOD INDUSTRY 12, N E Wales Inst, Wrexham, WALES: 12th Conference on Gums and Stabilisers for the Food Industry (294), pp. 167-178.
  • Howell NK. (2002) 'Elucidation of protein-lipid interactions'. ROYAL SOC CHEMISTRY GUMS AND STABILISERS FOR THE FOOD INDUSTRY 11, NE WALES INST, WREXHAM, WALES: 11th Conference on Gums and Stabilisers for Food Industry (278), pp. 73-81.
  • Howell NK. (2000) 'Gelation properties and interactions of fish proteins'. ELSEVIER SCIENCE BV HYDROCOLLOIDS, PT 1, OSAKA, JAPAN: Osaka-City-University International Symposium 98/4th International Conference on Hydrocolloids, pp. 399-406.
  • Howell NK. (2000) 'Recent advances in protein interactions'. ROYAL SOC CHEMISTRY GUMS AND STABILISERS FOR THE FOOD INDUSTRY 10, NE WALES INST, WREXHAM, WALES: 10th Gums and Stabilisers for the Food Industry Conference (251), pp. 317-327.
  • Howell NK, Saeed S. (1999) 'The application of electron spin resonance spectroscopy to the detection and transfer of free radicals in protein-lipid systems'. ROYAL SOC CHEMISTRY ADVANCES IN MAGNETIC RESONANCE IN FOOD SCIENCE, NORWICH, ENGLAND: 4th International Conference on Applications of Magnetic Resonance in Food Science (231), pp. 135-143.
  • Howell NK. (1995) 'Synergism and interactions in mixed protein systems'. NOTTINGHAM UNIVERSITY PRESS BIOPOLYMER MIXTURES, UNIV NOTTINGHAM, NOTTINGHAM, ENGLAND: 56th Easter School on Biopolymer Mixtures, pp. 329-347.
  • HOWELL NK. (1994) 'ELUCIDATION OF PROTEIN PROTEIN INTERACTIONS IN GELS AND FOAMS'. OXFORD UNIV PRESS GUMS AND STABILIZERS FOR THE FOOD INDUSTRY 7, N E WALES INST, WREXHAM, WALES: 7th International Conference on Gums and Stabilisers for the Food Industry, pp. 77-89.

Book chapters

  • Howell NK. (2010) 'Bioactive Proteins and Peptides as Functional Foods and Nutraceuticals'. in Mine Y (ed.) Bioactive Proteins and Peptides as Functional Foods and Nutraceuticals Wiley-Blackwell Article number 14

    Abstract

    The book considers fundamental concepts and structure-activity relations for the major classes of nutraceutical proteins and peptides.

All Publications

PUBLICATIONS
REFEREED RESEARCH PAPERS

1. Alghazeer, R, Saeed, S and Howell, N. (2008). Aldehyde formation in frozen fish. Food Chemistry 108, 801-810.

2. Alghazeer, R, Saeed, S and Howell, N. (2008). Formation of 4-hydroxynonenal (4-HNE) in frozen mackerel. J. Sci Food Agric. 88. 1128-1134.

3. Alghazeer, R and Howell, N. (2008). Effect of green tea on protein structure of mackerel (Scomber scombrus) during frozen storage by FT-Raman spectrosdopy. Int J. Food Sci. Technol. Accepted.

4. Alghazeer, R and Howell, N. (2008). Cytotoxicity effect of oxidised lipids on cultured colonal human intestinal cancer cells (Caco-2 cells). Toxicology Letters. (Accepted).

5. Alghazeer, R, Herman, H, Gao, H and Howell, N. (2007). Elucidation of cytotoxicity effect of oxidised lipids on cultured caco-2 cells using bioimaging techniques. Submitted.

6. Eduard Dàvila, Dolors Parés, Nazlin K. Howell (2007). Studies on plasma proteins interactions in heat-induced gels by differential scanning calorimetry and FT-Raman spectroscopy. Food Hydrocolloids 21, 1144-1152.

7. Eduard Dàvila, Dolors Parés, Nazlin K. Howell (2006). FT Raman spectroscopy study of heat-induced gelation of plasma proteins as influenced by pH. J. Agric and Food Chem. 54, 7890-7897.

8. Rahimuddin, S, Khoja, S, Zuhair, M M, Howell, N K and Brown, J E. (2007). Inhibition of peroxidation in UVA-treated skin fibroblasts by luteolin and its glucosides. Eur. J. Lipid Sci. 109, 647-655.

9. Wu, W, Clifford MN and Howell NK (2007). The effect of instant green tea on the foaming and rheological properties of egg albumen proteins. J. Sci. Food Agric. 87, 1810-1819.

10. Sarkardei, S and Howell, NK (2007). Effects of Freeze-drying on Lipids of Atlantic Mackerel (Scomber scombrus) and Horse Mackerel (Trachurus trachurus) by FT-Raman spectroscopy. Food Chemistry 103, 62-70.

11. Sarkardei, S and Howell, NK. (2008). Effects of natural antioxidants on stored freeze-dried Atlantic Mackerel (Scomber scombrus) lipids and proteins. JSFA. Submitted.

12. Sarkardei, S and Howell, NK. (2007). Effects of natural antioxidants on stored freeze-dried food product formulated using Horse Mackerel (Trachurus trachurus). IJFST , 43, 309-315.

13. Sarkardei, S., Kass. G and Howell, NK Cytotoxicity of oil extracted from stored freeze-dried food product formulated using mackerel (Scomber scombrus) with and without antioxidants in cultured colonal human intestinal cancer caco-2 cells. JSFA . Submitted

14. Saeed, S, Gillies, D, Wagner, G and Howell, N. K. (2006). ESR and NMR spectroscopy studies on formation of dityrosine in emulsions containing oxidised methyl linoleate. Food and Chemical Toxicology 44, 1385-1392.

15. Nandutu, A M, Clifford, M and Howell, N.K. (2007). Analysis of phenolic compounds in Ugandan sweet potato varieties (NSP, SPK AND TZ). African Journal of Biochemistry Research Vol. 1 (3), 029-036.

16. Cheow, CS, Norizah, MS, Kyaw, ZY and Howell, NK. (2007). Preparation and characterisation of gelatins from the skins of sin croaker (Johnius dussumieri) and shortfin scad (Decapterus macrosoma). Food Chemistry, 101, 386-391.

17. Badii, F and Howell, N.K. (2006). Fish gelatin: structure, gelling properties and interaction with egg albumen proteins. Food Hydrocolloids 20, 630-640.

18. Leelapongwattana, K, Benjakul, S, Visessanguan, W and Howell, Nazlin K. (2008). Effect of some additives on the inhibition of lizardfish trimethylamine-N-oxide demethylase and frozen storage stability of minced flesh. Int. J. Food Sci Technol. 43(3):448-455.

19. Leelapongwattana K, Benjakul S, Visessanguan W, and Howell, N.K.(2008).
Raman spectroscopic analysis and rheological measurements on natural actomyosin from haddock (Melanogrammus aeglefinus) during refrigerated (4oC) and frozen (-10 oC) storage in the presence of trimethylamine-N-oxide demethylase from kidney of lizardfish (Saurida tumbil). Food Chem. 106, 1253-1263.

20. Intarasirisawat R, Benjakul S, Visessanguan, W and Howell, N.K. (2007).
Autolysis study of bigeye snapper (Priacanthus macracanthus) skin and its effect on gelatin
Food Hydrocolloids 21 (4): 537-544.

21. Leelapongwattana, K., Benjakul, S., Visessanguan, W. and Howell, N. K. (2008). Effect of trimethylamine-N-oxide demethylase from lizardfish kidney on biochemical changes of haddock natural actomyosin stored at 4 and -10C. Eur. Food Res. Technol. 226, 833-841.

22. Leelapongwattana, K., Benjakul, S., Visessanguan, W. and Howell, N. K. (2007). Effect of some additives on the inhibition of lizardfish trimethylamine-N-oxide demethylase and frozen storage stability of minced flesh. Int. J. Food Sci. Technol. Accepted.

23. Leelapongwattana, K., Benjakul, S., Visessanguan, W. and Howell, N. K. (2007). Effects of inhibitors and antioxidants on physicochemical and biochemical changes of haddock muscle induced by lizardfish trimethylamine-N-oxide demethylase during frozen storage. J. Sci. Food Agric. in review.

24. Leelapongwattana K, Benjakul S, Visessanguan W, Howell NK. (2005). Physicochemical and biochemical changes in whole lizardfish (Saurida micropectoralis) muscles and fillets during frozen storage. J. Food Biochemistry 29, 547-569.

25. Leelapongwattana, K, Benjakul, S, Visessanguan, W and Howell, N. K.(2005). Physicochemical and biochemical changes during frozen storage of minced flesh of lizardfish (Saurida micropectoralis). Food Chemistry 90, 141-150.

26. Wu, W, Clifford MN and Howell NK (2006). The effect of instant green tea on the foaming and rheological properties of whey proteins. J. Sci. Food Agric. Accepted.

27. Saeed, S and Howell, NK (2006). Fourier-transform Raman spectroscopy studies in emulsions containing -lactoglobulin and oxidised methyl linoleate. J Sci Food Agric. Submitted.

28. Saeed, S and Howell, NK (2006). Changes in the gelling and conformational properties of -lactoglobulin in the presence of oxidised lipids. Food Hydrocolloids. Submitted.

29. Badii, F and Howell, N. K. Effect of green tea polyphenols, and vitamin E and C on lipid oxidation and protein denaturation in freeze-dried horse mackerel. J. Agric. Food Chem. Submitted.

30. Badii, F and Howell, N. K. The effect of natural antioxidants on the physicochemical properties of stored dried horse mackerel. J. Sci. Food Agric. Submitted.

31. Badii, F, Odote P, Kazungu, J, Abbey, L, Kandando, R, Shamasundar, B, Cheow Chong Seng, and Howell, NK. Composition and nutritional analysis of under-utilised fish species in Africa and Asia. J. Food Biochemistry. Submitted.

32. Dileep, A.O. Shamasundar, B.A. Binsi, P.K, Badii, F and Howell N.K. (2007). Influence of corn and tapioca starch on the dynamic viscoelastic behaviour of ribbonfish (Trichiurus spp) meat stored in ice. Journal of Food Science. In press.

33. Dileep, A. O., Shamasundar, B.A., Binsi, P.K., Badii, F and Howell, N.K. (2005). Effect of ice storage on the physicochemical and dynamic viscoelastic properties of ribbonfish (Trichiurus spp). J. Food Science 70, 537-545.

34. Cheow, CS, Kyaw, ZY, Howell, NK and Dzulkifly, M.H. (2005). Relationship between physicochemical properties of starches and expansion of fish cracker (keropok). Journal of Food Quality 27, (1), 1-12..

35. Cheow, CS et al . Preparation and characterization of gelatin from Scianidae, Sin Croaker and Carangidae. Journal of Food Quality. Accepted.

36. Ngarize, S, Herman, H., Adams, A and Howell, N.K. (2004). Comparison of changes in the secondary structure of unheated, heated and high-pressure treated -lactoglobulin and ovalbumin proteins using Fourier Transform Raman spectroscopy and self deconvolution. J.Agric. Food Chem. 52, 6470-6477.

37. Ngarize, S, Adams, A and Howell, N.K. (2005). A comparative study of heat and high pressure induced gels of whey and egg albumen proteins and their binary mixtures. Food Hydrocolloids. 19, 984-996.

38. Ngarize, S, Adams, A and Howell, N.K. (2004). Studies on egg albumen and whey protein interactions by FT-Raman spectroscopy and rheology. Food Hydrocolloids 18, 49-59.

39. Ngarize, S, Adams, A and Howell, N.K. (2006). A study of the effects of sugars on the rheological properties and molecular interactions of unheated, heated and high pressure treated whey and egg albumen proteins.. Food Hydrocolloids. Accepted.

40. Ngarize, S, Adams, A and Howell, N.K. (2006). A study of the effects of salt on the rheological properties and molecular interactions of unheated, heated and high pressure treated ovalbumin and -lactoglobulin proteins.. Food Hydrocolloids. Accepted.

41. Badii, F and Howell, N.K.(2004). Elucidation of protein aggregation in frozen cod and haddock by transmission electron microscopy/ immunocytochemistry, light microscopy and atomic force microscopy. J Sci. Food Agric. 84, 1919-1928.

42. Saeed, S and Howell, N.K. (2004). Rheological and differential scanning calorimetry studies on structural and textural changes in frozen Atlantic mackerel (Scomber scombrus). J Sci. Food Agric. 84, 1216-1222.

43. Alonso, J, Canet, W, Howell, N and Alique, R (2003) Purification and Characterization of Carrot Pectinesterase (Daucus carota L) J. Sci Food and Agric.83, 1600-1606.

44. Badii, F and Howell, N.K. (2003). Elucidation of molecular changes in the water soluble proteins in cod by circular dichroism and FT-Raman spectrsocopy. J. Sci Food and Agric. Submitted.

45. Saeed, S and Howell, N.K. (2003). Biochemical and rheological changes in frozen Atlantic mackerel (Scomber scombrus). J. Sci Food and Agric. In press.

46. Badii, F and Howell, N.K. (2003). Elucidation of the effect of formaldehyde and lipids on collagen from frozen cod by Raman spectroscopy and differential scanning calorimetry. J. Agric. Food Chemistry, 51, 1440-1446.

47. Comfort, S and Howell, N.K. (2003). Gelation properties of soluble wheat proteins and meat protein mixtures. Food Hydrocolloids 17, 149-159.

48. Saeed, S and Howell, N.K. (2002). Effect of lipid oxidation and frozen storage on muscle proteins of Atantic mackerel (Scomber scombrus). J Sci Food Agric. 82, 579-586.

49. Badii, F and Howell, N.K. (2002). Effect of antioxidants, citrate and cryoprotectants on protein solubility and texture of frozen cod (Gadus morhua). J. Agric. Food Chemistry, 50, 2053-2061.

50. Badii, F and Howell, N.K. (2002). Changes in the texture and structure of cod and haddock fillets during frozen storage. Food Hydrocolloids 16, 313-319.

51. Badii, F and Howell, N.K. (2002) A comparison of biochemical changes in cod (Gadus morhua) and haddock (Melanogrammus aeglefinus) during frozen storage. J. Sci. Food Agric. 82, 87-97.

52. Howell, N.K., Herman, H and Li-Chan, E.C.Y (2001). Elucidation of protein-lipid interactions in a lysozyme-corn oil system by Fourier Transform Raman spectroscopy. J. Agric. Food Chemistry 49, 1529-1533.

53. Saeed, S and Howell, N.K.(2001). 12-Lipoxygenase activity in the muscle tissue of Atlantic mackerel (Scomber scombrus) and its prevention by antioxidants. J Sci Food Agric. 81, 1-6.

54. Kyaw, Z.Y., Yu, S.Y, Dzulkifly, M.H and Howell, N.K.(2001). Effect of fish:starch ratio on viscoelastic and microstructure of fish cracker (keropok) dough. International Journal of Food Science and Technology. 36, 1-7.

55. Cheow,C.S., Yu,S.Y., Howell,N.K., Che Man,Y & Mohamad, S.K.(1999). Effect of salt and fish contents on the microstructure and expansion of fish cracker (keropok). J Sci Food Agric. 79, 879-885.

56. Medina, I., Saeed, S. and Howell, N.K.(1999). Enzymatic oxidative activity in sardine (Sardina pilchardus) and herring (Cuplea harengus) during chilling and correlation with freshness. Europ. Food Res. Technol. 210, 34-38.

57. Saeed, S., Fawthrop, S.A. and Howell, N.K. (1999). Electron spin resonance (ESR) study on free-radical transfer in food lipid-protein interaction. J Sci Food Agric. 79, 1809-1816.

58. Cheow,C.S., Yu,S.Y. & Howell, N.K. (1999). Effect of salt, sugar and MSG on the viscoelastic properties of fish cracker gel. J. Food Processing and Preservation. 23, 21-37.

59. Howell, N.K., Arteaga, G., Nakai, S and Li-Chan, E.C.Y. (1999). Raman spectral analysis in the C-H stretching region of proteins and amino acids for investigation of hydrophobic interactions. J. Agric. Food Chem. 47, 924-933.

60. Saeed, S and Howell, N.K. (1999). High performance liquid chromatography (HPLC) and spectroscopic studies on fish oil oxidation products extracted from frozen Atlantic mackerel. J. American Oil Chem. Soc. 76, (3), 391-397.

61. Mendes, R., Batista, I, Kandando, R and Howell, N. (1998).Influence of washing parameters on the characteristics of horse mackerel (Trachurus trachurus) mince. Journal of Food Biochemistry 22, 511-528.

62. Howell, N., Bristow E., Emma Copeland, G-L Friedli, G.L. (1998). Interaction of deamidated soluble wheat protein with sodium alginate. Food Hydrocolloids 12, 317-324.

63. Alonso, J., Howell, N.K. and Canet, W. (1997). Isolation and characterisation of pectin esterase from grapefruit. J Sci Food Agric. 75, 352-358.

64. Howell, N.K., Shavila, Y., Grootveld, M and Williams, S. (1996). High resolution NMR and magnetic resonance imaging (MRI) studies on fresh and frozen cod (Gadus morhua). Journal of Magnetic Resonance Analysis 2, 180-181.

65. Friedli, G and Howell, N.K. (1995). LOQ small angle neutron scattering studies (SANS) on gliadin and deamidated gliadin. EPSRC ISIS 95 Annual Report. Rutherford Appleton Laboratory Report No RAL-95-050 Vol.2. A473.

66. Howell, N.K. and Li-Chan, E.C.Y. (1996). Elucidation of the Interaction of Lysozyme and Whey Proteins by Raman spectroscopy. International Journal of Food Science and Technology 31 439-452.

67. Friedli, G.L.and Howell, N. (1996). Gelation properties of deamidated soluble wheat protein. Food Hydrocolloids 10, 255-261.

68. Howell, N.K. Shavila,Y. Grootveld, M. and Williams, S. (1996). High resolution NMR and Magnetic Resonance Imaging of Fresh and Frozen Cod (Gadus morhua) and Haddock (Melanogrammus aeglefinus). Journal of the Science of Food and Agriculture 72, 49-56.

69. Howell, N.K., Yeboah, N.and Lewis, D.F.V. (1995) Interactions of Lysozyme with Whey Proteins. International Journal of Food Science and Technology 30, 813-824.

70. Howell, N.K. and Taylor, C.(1995). Effect of ascorbic acid on the physicochemical and functional properties of globular proteins. International Journal of Food Science and Technology 30, 321-334.

71. Howell N. K. and Taylor, C (1991). Effect of amidation on the foaming and physicochemical properties of bovine serum albumin. International Journal of Food Science and Technology, 26, 385-395.

72. Murphy, M.C. and Howell, N.K.(1991). Functional properties of native and positively and negatively charged modified bovine serum albumin. J Sci Food Agric 55, 489-492.

73. Murphy, M.C. and Howell, N.K.(1991). Effects of the Attachment of Small Molecules by Carbodiimide-mediated Condensation on the Physicochemical and Functional Properties of Bovine Serum Albumin. J Sci Food Agric. 55, 117-140.

74. Murphy, M.C. and Howell, N.K.(1991).Effect of the Attachment of Valine Residues on the Physicochemical and Functional Properties of Bovine Serum Albumin. J Sci Food Agric. 54, 245-253.

75. Murphy, M.C and Howell, N.K.(1990). Effect of Thiolation on the Physicochemical and Functional Properties of Bovine Serum Albumin. J Sci Food Agric 53, 549-558.

76. Murphy, M.C.and Howell, N.K.(1990). Effect of Succinylation on the Functional and Physicochemical Properties of Bovine Serum Albumin. J Sci Food Agric 51, 109-123.

77. Howell, N.K. and Lawrie, R.A.(1987). Functional aspects of blood plasma proteins. 5.Viscosity. Journal of Food Technology 22, 145-151.

78. Howell, N.K. and Lawrie, R.A.(1985).Functional Aspects of blood plasma proteins. 4. Elucidation of the mechanism of gelation of plasma and egg albumen proteins. Journal of Food Technology 20, 489-504.

79. Howell, N.K and Lawrie, R.A.(1984). Functional Aspects of blood plasma proteins. 3. Interaction with other proteins and stabilisers. Journal of Food Technology 19, 297-313.

80. Howell, N.K. and Lawrie, R.A. (1984) Functional Aspects of blood plasma proteins. 2. Gelling properties. Journal of Food Technology 19, 289-295.

81. Howell, N.K. and Lawrie, R.A. (1983). Functional Aspects of Blood Plasma Proteins.1. Separation and characterisation. Journal of Food Technology (1983) 18, 747-762.

82. Howell, N.K. and Lawrie, R.A.(1981). Functional aspects of blood plasma fractions. Meat Research Workers D-4:383-384.

83. Howell, N. (1978). Functional properties of animal proteins in food. J. International Flavours and Food Additives, 6, 119-126.

84. Guy, R.C.E., Willcox, C. and Karmali, N. (1974). A Method for Measuring the Chemical Deterioration in Egg Protein Quality caused by Processing and Storage. J. Food Technology 8, 1-5.


B. INVITED REFEREED BOOK CHAPTERS

By
and collagen


1. Nazlin K Howell and Chitundu Kasase (2009). Bioactive peptides and proteins from fish muscle and collagen. In Biologically Active Food Proteins and Peptides in Health – Fundamental and Clinical Aspects. Blackwell-Wiley Publ. London. In press.

2. Meng, G, Howell, NK and Li-Chan ECY (2006). Investigation of protein-lipid interactions by vibrational spectroscopy. In Lipid Analysis and Lipidomics.: New Techniques and Applications. Ed. M.M. Mossoba, J.K.G. Kramer, J.T. Brenna and R.E. McDonald. AOACS Press.Pp 355-376.

3. Howell, N.K. (2005). Interaction of proteins with small molecules. In Ingredient Interactions -Effects on Food Quality. Ed. A. Gaonkar and A. McPherson. CRC Press Taylor and Francis, Florida.2nd Ed. Pp.309-341.

4. Howell, N.K., Saeed, S and Gillies, D (2005). ESR and NMR spectroscopy studies on emulsions containing -lactoglobulin and oxidised methyl linoleate. In Magnetic Resonance in Food Science: A Multivariate Challenge. Ed. S B Engleson, P S Belton and H J Jakobsen. Royal Society of Chemistry, UK. Pp 104-112.

5. Howell, N.K. (2004). Fish gelatin: structure, gelling properties and interaction with other food proteins. In Gums and Stabilisers for the Food Industry 12. Ed. P.A. Williams and G.O. Philips. The Royal Society of Chemistry, Cambridge, UK. Pp. 167-178.

6. Howell, N.K. (2004). The chemistry of quality enhancement in low-value fish. In Quality of Fresh and Processed Foods. American Chemical Society. Ed. A. Spanier. Kluwer Academic/Plenum Publishers, New York. Pp 135-145.

7. Howell, N.K. (2002). Elucidation of protein-lipid interactions. In Gums and Stabilisers for the Food Industry 11. Ed. P.A. Williams and G.O. Philips. The Royal Society of Chemistry, Cambridge, UK. Pp. 136-144.

8. Howell, N.K. (2000). Advances in protein interactions. In Gums and stabilisers for the food industry 10. Ed. P.A. Williams and G.O. Philips. The Royal Society of Chemistry, Cambridge, UK. Pp . 217-227.

9. Howell, N.K. and Saeed, S. (1999). The application of electron spin resonance spectroscopy to the detection and transfer of free radicals in protein-lipid systems. In: Applications of Magnetic Resonance in Food Science. Ed. P.S.Belton, B.P. Hills and G.A. Webb. The Royal Society of Chemistry, Cambridge, UK. Pp 133-143.

10. Howell, N.K. and Saeed, S. (1999). The effect of antioxidants on the production of lipid oxidation products and transfer of free radicals in oxidised lipid-protein systems. In: Antioxidants in Human Health and Disease. Ed. T.K. Basu, N.J Temple and M.L. Garg. CAB International, Oxford, UK. pp 43-54.

11. Howell, N.K. (1999). Gelation properties and interactions of fish proteins. In: Food Hydrocolloids I: Physical Chemistry and Industrial Application of Gels, Polysaccharides and Proteins. Ed.K. Nishinari. Elsevier, Amsterdam Pp 399-406.

12. Somers, P and Howell, N.K. (1997). Gelation properties of smooth and skeletal muscle myosin proteins. In Gums and stabilisers for the food industry 9. Ed. P.A. Williams and G.O. Philips. The Royal Society of Chemistry, Cambridge, UK. Pp 136-144.

13. Howell, N.K.(1996) Chemical and enzymatic modifications of food proteins. In Food Proteins: Properties and Applications Vol 1. Ed. S. Nakai and H.W. Modler. Food Science and Technology Series. VCH Publishers, New York. pp. Pp 235-280. ISBN: 1-56081-691-0.

14. Howell, N.K. (1995). Synergism and Interactions in Mixed Food Protein Systems. In Biopolymer Mixtures, Ed. S.E. Harding, S.E.Hill and J. Mitchell. University of Nottingham Press, pp 329-347. ISBN: 1-897676-247.

15. Howell, N.K. (1995). Interaction of proteins with small molecules. In Ingredient Interactions -Effects on Food Quality. Ed. A. Gaonkar. Marcel Dekker, New York. Pp.269-289. ISBN:0-8247-9347-1.

16. Howell, N.K. (1994). Elucidation of protein-protein interactions in gels and foams. In Gums and stabilisers for the food industry 7. Ed. G.O. Philips., P.A. Williams and D.J. Wedlock, Oxford University Press. UK. Pp 77-89. ISBN:0-19-963465-3.

17. Howell, N.K. (1992). Protein-protein Interactions. In Biochemistry of Food Proteins. Ed.B.J.F.Hudson. Elsevier Applied Science Publ.Ltd., Essex, pp 35-74. ISBN 1-85166-768.
18. Howell, N.K.(1991). Protein-Protein Interactions. In Developments in Food Proteins -7 Ed.B.J.F.Hudson. Elsevier Applied Science Publ.Ltd., Essex, pp 231-270.

C. INVITED RESEARCH PAPERS AND REVIEWS

1. Howell, N.K. and Saeed, S (2006). Rheological and spectroscopic studies of emulsions containing proteins and oxidized lipids. Proceedings of the 4th International Symposium on Food Rheology and Structure. Ed. P. Fischer, P. Erni, and E.J Windhab. ETH Swiss Federal Institute of Technology, Zurich. Pp 323-326.

2. Howell, N.K., Saeed, S and Badii, F. (2005). Molecular mechanisms of protein-lipid interactions. The International Conference on Nanotechnology: Science and Applications (Nanotech Insight 2005),Ed. A Haist and MMS Abdel-Mottaleb, Chemnitz University of Technology, Germany. Pp 140-141.

3. Howell, N.K. (2001). Biochemical changes and processing of under-utilised marine fish in Africa and Asia. EC Fisheries Cooperation Bulletin 14, 45-47.

4. Howell, N. K. (2001). Changements et transformation biochimiques des poissons de mer peu employes en Afrique et en Asia. CE Cooperation Peche Bulletin 14, 48-50.

5. Howell, N.K. (2000). EC Synopsis of selected R&D projects in the field of fisheries and aquaculture. ISBN 92-828-7143-6. Pp 46-49.

6. Howell, N.K.(1999). Protein-protein and protein-polysaccharide interactions in food gels. Food Ingredients and Analysis International, 4, 23-30.

7. Flair-Flow dissemination report F-FE 290/98 (1998). Toughening in Frozen Fish. EU FAIR project.CT95.1111.

8. Howell, N.K. (1998). Biochemical changes and protein interactions leading to aggregation and toughening in frozen fish. Third European Marine Science and Technology Conference Project Synopses Vol. VI: Fisheries and Aquaculture (FAIR 1994-1998). Published by the European Commission, Luxembourg. ISBN No . 92-828-3039-X. Pp 110-113.

9. Howell, N.K. (1997). Processing of and related biochemical studies on the under-utilised marine fish/crustacea species in Africa and Asia. Scientific cooperation of the European Union with the countries of South-East Asia. Published by the European Commission EC DG XII Luxembourg. ISBN No . 92-828-0574-3. Pp 108-109.

10. Flair-Flow dissemination report F-FE 204/96 (1995). Mechanisms of aggregation of proteins in frozen fish. EU FAR project.

11. Howell, N.K. (1995). Processing of and related biochemical studies on the under-utilised marine fish/crustacea species in Africa and Asia. European Commission Life Sciences and technologies for developing countries STD 3 Agriculture. Published by EC DG XII Luxembourg. ISBN No . 92-827-6619-5. Pp 306-307.

12. Howell, N.K.(1995).Elucidation of aggregation mechanisms of proteins in frozen fish. Fisheries and Aquaculture Research Vol.1 pp 243-246. Published by EU DG XII Luxembourg. ISBN No . 92-826-9926-9.

13. Howell, N.K. (1990). Food protein ingredients, structure and function. Food Technology International Europe, 175-179.


D. INVITED BOOK REVIEWS

1. Howell, N.K. (2002). EU Food Law edited by Kaarin Goodburn. In Food Research International. Elsevier. In press

2. Howell, N.K. (1994). Protein interactions edited by H. Visser. In International J Food Science and Technology.

3. Howell, N.K. (1986). Developments in food proteins-3 Ed. B.J.F. Hudson. in Trends in analytical chemistry 5, XX11-XX111.

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