Multivariate strategy in screening of enzymes to be used for whey protein hydrolysis in an enzymatic membrane reactor

International Dairy Journal

Volumn 17, Issue 4, 2007, Pages 393-402

  Cheison, Seronei Chelulei ^a,b   Wang, Zhang ^a   Xu, Shi Ying ^a  

^a JIANGNAN UNIVERSITY   (China)

^b MASENO UNIVERSITY   (Kenya)

Author keywords

Enzymatic membrane reactor; Enzyme selection; Free amino acids; Protease N; Residual enzyme activity

Indexed keywords

AMINO ACIDS; BIOREACTORS; CARBOXYLIC ACIDS; CASEIN; HYDROLYSIS; PH EFFECTS;

ENZYMATIC MEMBRANE REACTOR; FREE AMINO ACIDS (FAA); HYDROLYSATES; PROTEASE; TRICHLOROACETIC ACID (TCA);

ENZYME KINETICS;

EID: 33846013181     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2006.05.006     Document Type: Article

References (36)

1. Adamson J.N., and Reynolds E.C. Characterization of casein phosphopeptides prepared using alcalase: Determination of enzyme specificity. Enzyme and Microbial Technology 19 (1996) 202-209
2. Adler-Nissen J. Controlled hydrolysis and the empirical characterisation of various substrates and enzymes. Enzymic hydrolysis of food proteins (1986), Elsevier Applied Science, London, UK 113-169
3. Anson M.L. The estimation of pepsin, trypsin, papain, and cathepsin with haemoglobin. Journal of General Physiology 22 (1938) 79-89
4. Argüello M.A., Álvarez S., Riera F.A., and Álvarez R. Utilization of enzymatic detergents to clean inorganic membranes fouled by whey proteins. Separation and Purification Technology 41 (2005) 147-154
5. Cheison, S. C. (2003). Studies on inhibition of angiotensin-I converting enzyme (ACE) by casein non-phosphorylated peptides. M.Sc. thesis, Southern Yangtze University, Wuxi China.
6. Cheison S.C., and Wang Z. Bioactive milk peptides: Redefining the food-drug interphase-review. African Journal of Food, Nutrition, Science, Agriculture and Development 3 1 (2003) 29-38
7. Cheison, S. C., Wang, Z., & Xu, S. Y. (2006). Use of macroporous adsorption resin for simultaneous desalting and debittering of whey protein hydrolysates. Food Science and Technology, 7, in press (in Chinese with English abstract).
8. Chiang W.-D., Tsou M.-J., Tsai Z.-Y., and Tsai T.-C. Angiotensin I-converting enzyme inhibitor derived from soy protein hydrolysate and produced by using membrane reactor. Food Chemistry 98 4 (2006) 725-732
9. Davis J.P., Doucet D., and Foegeding E.A. Foaming and interfacial properties of hydrolyzed β-lactoglobulin. Journal of Colloid and Interface Science 288 (2005) 412-422
10. Davis P.J., and Williams S.C. Protein modification by thermal processing. Allergy 53 Suppl. 46 (1998) 102-105
11. Deeslie W.D., and Cheryan M. Continuous enzymatic modification of proteins in an ultrafiltration reactor. Journal of Food Science 46 (1981) 1035-1042
12. Exl B.-M. A review of recent developments in the use of moderately hydrolysed whey formulae in infant nutrition. Nutrition Research 21 (2001) 355-379
13. Fox P.F., Morrissey P.A., and Mulvihill D.M. Chemical and enzymatic modification of food proteins. In: Hudson B.J.F. (Ed). Developments in food proteins-1 (1982), Applied Science, London, UK 1-60
14. Guadix A., Camacho F., and Guadix E.M. Production of whey protein hydrolysates with reduced allergenicity in a stable membrane reactor. Journal of Food Engineering 72 (2006) 398-405
15. Hale M.B. Relative activities of commercially available enzymes in hydrolysis of fish protein. Food Technology 23 (1969) 107-110
16. Hambling S.G., McAlpine A.S., and Sawyer L. β-Lactoglobulin. In: Fox P.F. (Ed). Advanced dairy chemistry-1: Proteins (1992), Elsevier Science Publishers Ltd., Essex, UK 141-190
17. Hsu H.W., Vavak D.L., Satterlee L.D., and Miller G.A. A multienzyme technique for estimating protein digestibility. Journal of Food Science 42 5 (1977) 1269-1273
18. Iametti S., Rasmussen P., Frøkiær H., Ferranti P., Addeo F., and Bonomi F. Proteolysis of bovine β-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity. European Journal of Biochemistry 269 (2002) 1362-1372
19. Jurado E., Camacho F., Luz-on G., and Vicaria J.M. Kinetic model for lactose hydrolysis in a recirculation hollow-fibre bioreactor. Chemical Engineering Science 59 (2004) 397-405
20. Kristinsson H.G., and Rasco B.A. Kinetics of the hydrolysis of Atlantic salmon (Salmo salar) muscle proteins by alkaline proteinases and a visceral serine proteinase mixture. Process Biochemistry 36 (2000) 131-139
21. Mahmoud M.I. Physicochemical and functional properties of protein hydrolysates in nutritional products. Food Technology 48 10 (1994) 89-95
22. Manninen A.H. Protein hydrolysates in sports and exercise: A brief review. Journal of Sports Science and Medicine 3 (2004) 60-63
23. Meisel H. Biochemical properties of bioactive peptides derived from milk proteins: Potential nutraceuticals for food and pharmaceutical applications. Livestock Production Science 50 (1997) 125-138
24. Morato A.F., Carreira R.L., Junqueira R.G., and Silvestre M.P.C. Optimization of casein hydrolysis for obtaining high contents of small peptides: Use of subtilisin and trypsin. Journal of Food Composition and Analysis 13 (2000) 843-857
25. Mountzouris K.C., Gilmour S.G., Grandison A.S., and Rastall R.A. Modelling of oligodextran production in an ultrafiltration stirred-cell membrane reactor. Enzyme and Microbial Technology 24 (1999) 75-85
26. Mullally M.M., O'Callaghan D.M., FitzGerald R.J., Donnelly W.J., and Dalton J.P. Proteolytic and peptidolytic activities in commercial pancreatic protease preparations and their relationship to some whey protein hydrolysate characteristics. Journal of Agricultural and Food Chemistry 42 (1994) 2973-2981
27. Mutilangi W.A.M., Panyam D., and Kilara A. Hydrolysates of proteolysis of heat-denatured whey proteins. Journal of Food Science 60 5 (1995) 1104-1109
28. O'Meara G.M., and Munro P.A. Selection of a proteolytic enzyme to solubilise lean beef tissue. Enzyme and Microbial Technology 6 (1984) 181-185
29. Pace C., and McGrath T. Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation. Journal of Biological Chemistry 255 (1980) 3862-3865
30. Prevot-D'Alvise N., Lesueur-Lambert C., Fertin-Bazus A., Fertin B., Dhulster P., and Guillochon D. Continuous enzymatic solubilization of alfalfa proteins in an ultrafiltration reactor. Enzyme and Microbial Technology 34 (2004) 380-391
31. Smyth M., and FitzGerald R.J. Relationship between some characteristics of WPC hydrolysates and the enzyme complement in commercially available proteinase preparations. International Dairy Journal 8 9 (1998) 819-827
32. Thankam E.B., and Rajkumar G.S. Purification and characterization of alkaline proteinase from Alcaligenes faecalis. Biotechnology and Applied Biochemistry 35 (2002) 149-154
33. van der Ven C., Gruppen H., de Bont D.B.A., and Voragen A.G.J. Reversed phase and size exclusion chromatography of milk protein hydrolysates: Relation between elution from reversed phase column and apparent molecular weight distribution. International Dairy Journal 11 (2001) 83-92
34. van der Ven C., Gruppen H., de Bont D.B.A., and Voragen A.G.J. Optimization of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology. International Dairy Journal 12 (2002) 813-820
35. Wal J.-M. Thermal processing and allergenicity of foods. Allergy 58 (2003) 727-729
36. Whitaker J.R. Enzymatic modification of proteins applicable to foods. In: Feeney R.E., and Whitaker J.R. (Eds). Food proteins: Improvement through chemical and enzymatic modifications. Advances in chemistry series 160 (1977), American Chemical Society, Washington, DC, USA 95-155