Impact of enzyme inactivation conditions during the generation of whey protein hydrolysates on their physicochemical and bioactive properties

International Journal of Food Science and Technology

Volumn 53, Issue 1, 2018, Pages 219-227

  Le Maux, Solène ^a   Nongonierma, Alice B ^a   Lardeux, Claire ^a   FitzGerald, Richard J ^a  

^a UNIVERSITY OF LIMERICK   (Ireland)

Author keywords

Antidiabetic nutriceuticals; antioxidants; dairy products; diabetes; enzymes; food processing aspects; milk proteins; processing effects; protein hydrolysates; thermal effects; whey protein concentrate

Indexed keywords

AGGREGATES; ANTIOXIDANTS; DAIRY PRODUCTS; ENZYMES; FOOD PROCESSING; HYDROLYSIS; MEDICAL PROBLEMS; PROTEINS; THERMAL EFFECTS;

MILK PROTEIN; NUTRICEUTICALS; PROCESSING EFFECTS; PROTEIN HYDROLYSATE; WHEY PROTEIN CONCENTRATE;

THERMAL PROCESSING (FOODS);

EID: 85041089907     PISSN: 09505423     EISSN: 13652621     Source Type: Journal    
DOI: 10.1111/ijfs.13576     Document Type: Article

References (32)

1. Adjonu, R., Doran, G., Torley, P. & Agboola, S. (2013). Screening of whey protein isolate hydrolysates for their dual functionality: influence of heat pre-treatment and enzyme specificity. Food Chemistry, 136, 1435–1443.
2. Conesa, C. & FitzGerald, R.J. (2013). Total solids content and degree of hydrolysis influence proteolytic inactivation kinetics following whey protein hydrolysate manufacture. Journal of Agricultural and Food Chemistry, 61, 10135–10144.
3. Conway, V., Gauthier, S.F. & Pouliot, Y. (2013). Antioxidant activities of buttermilk proteins, whey proteins, and their enzymatic hydrolysates. Journal of Agricultural and Food Chemistry, 61, 364–372.
4. Creusot, N., Gruppen, H., van Koningsveld, G.A., de Kruif, C.G. & Voragen, A.G.J. (2006). Peptide–peptide and protein–peptide interactions in mixtures of whey protein isolate and whey protein isolate hydrolysates. International Dairy Journal, 16, 840–849.
5. Donovan, M. & Mulvihill, D. (1987). Thermal denaturation and aggregation of whey proteins. Irish Journal of Food Science and Technology, 11, 87–100.
6. Eijsink, V.G.H., Gåseidnes, S., Borchert, T.V. & van den Burg, B. (2005). Directed evolution of enzyme stability. Biomolecular Engineering, 22, 21–30.
7. Embiriekah, S., Bulatović, M., Borić, M., Zarić, D. & Rakin, M. (2017). Antioxidant activity, functional properties and bioaccessibility of whey protein hydrolysates. International Journal of Dairy Technology, In press. https://doi.org/10.1111/1471-0307.12428
8. Foegeding, E.A., Davis, J.P., Doucet, D. & McGuffey, M.K. (2002). Advances in modifying and understanding whey protein functionality. Trends in Food Science & Technology, 13, 151–159.
9. Hernández-Ledesma, B., García-Nebot, M.J., Fernández-Tomé, S., Amigo, L. & Recio, I. (2014). Dairy protein hydrolysates: peptides for health benefits. International Dairy Journal, 38, 82–100.
10. Johnson, G.G., Morris, J.M. & Berk, R.S. (1967). The extracellular protease from Pseudomonas aeruginosa exhibiting elastase activity. Canadian Journal of Microbiology, 13, 711–719.
11. Juillerat-Jeanneret, L. (2014). Dipeptidyl peptidase IV and its inhibitors: therapeutics for type 2 diabetes and what else? Journal of Medicinal Chemistry, 57, 2197–2212.
12. Kilcawley, K., Wilkinson, M. & Fox, P. (2002). Determination of key enzyme activities in commercial peptidase and lipase preparations from microbial or animal sources. Enzyme and Microbial Technology, 31, 310–320.
13. Lacroix, I.M.E. & Li-Chan, E.C.Y. (2016). Food-derived dipeptidyl-peptidase IV inhibitors as a potential approach for glycemic regulation – Current knowledge and future research considerations. Trends in Food Science & Technology, 54, 1–16.
14. Lazer, I. & Lazer, I. (2010). GelAnalyzer 2010a: Freeware 1D gel electrophoresis image analysis software. Available online: http://www.gelanalyzer.com. Accessed on 9 October 2015.
15. Le Maux, S., Nongonierma, A.B., Murray, B.A., Kelly, P.M. & FitzGerald, R.J. (2015). Identification of short peptide sequences in the nanofiltration permeate of a bioactive whey protein hydrolysate. Food Research International, 77, 534–539.
16. Le Maux, S., Nongonierma, A.B., Barre, C. & FitzGerald, R.J. (2016). Enzymatic generation of whey protein hydrolysates under pH-controlled and non pH-controlled conditions: impact on physicochemical and bioactive properties. Food Chemistry, 199, 246–251.
17. Le Maux, S., Nongonierma, A.B. & FitzGerald, R.J. (2017). Peptide composition and dipeptidyl peptidase IV inhibitory properties of β-lactoglobulin hydrolysates having similar extents of hydrolysis while generated using different enzyme-to-substrate ratios. Food Research International, 99, 84–90.
18. Morris, P.E. & FitzGerald, R.J. (2009). Whey proteins and peptides in human health. In: Whey Processing, Functionality and Health Benefits (edited by C. Onwulata & P. Huth). Pp. 285–343. Oxford, UK: Wiley-Blackwell.
19. Nongonierma, A.B. & FitzGerald, R.J. (2013a). Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk-derived dipeptides and hydrolysates. Peptides, 39, 157–163.
20. Nongonierma, A.B. & FitzGerald, R.J. (2013b). Dipeptidyl peptidase IV inhibitory properties of a whey protein hydrolysate: influence of fractionation, stability to simulated gastrointestinal digestion and food-drug interaction. International Dairy Journal, 32, 33–39.
21. Nongonierma, A.B., Gaudel, C., Murray, B.A. et al. (2013). Insulinotropic properties of whey protein hydrolysates and impact of peptide fractionation on insulinotropic response. International Dairy Journal, 32, 163–168.
22. Nongonierma, A.B., Le Maux, S., Dubrulle, C., Barre, C. & FitzGerald, R.J. (2015). Quinoa (Chenopodium quinoa Willd.) protein hydrolysates with in vitro dipeptidyl peptidase IV (DPP-IV) inhibitory and antioxidant properties. Journal of Cereal Science, 65, 112–118.
23. O'Loughlin, I.B., Murray, B.A., FitzGerald, R.J., Brodkorb, A. & Kelly, P.M. (2014). Pilot-scale production of hydrolysates with altered bio-functionalities based on thermally-denatured whey protein isolate. International Dairy Journal, 34, 146–152.
24. Power, O., Jakeman, P. & FitzGerald, R.J. (2013). Antioxidative peptides: enzymatic production, in vitro and in vivo antioxidant activity and potential applications of milk-derived antioxidative peptides. Amino Acids, 44, 797–820.
25. Power, O., Fernández, A., Norris, R., Riera, F. & FitzGerald, R. (2014). Selective enrichment of bioactive properties during ultrafiltration of a tryptic digest of β-lactoglobulin. Journal of Functional Foods, 9, 38–47.
26. Puyol, P., Perez, M. & Horne, D. (2001). Heat-induced gelation of whey protein isolates (WPI): effect of NaCl and protein concentration. Food Hydrocolloids, 15, 233–237.
27. Rani, A.J. & Mythili, S. (2014). Study on total antioxidant status in relation to oxidative stress in type 2 diabetes mellitus. Journal of Clinical and Diagnostic Research, 8, 108–110.
28. Simmons, M.J.H., Jayaraman, P. & Fryer, P.J. (2007). The effect of temperature and shear rate upon the aggregation of whey protein and its implications for milk fouling. Journal of Food Engineering, 79, 517–528.
29. Spellman, D., Kenny, P., O'Cuinn, G. & FitzGerald, R.J. (2005). Aggregation properties of whey protein hydrolysates generated with Bacillus licheniformis proteinase activities. Journal of Agricultural and Food Chemistry, 53, 1258–1265.
30. Whitehurst, R.J. & Law, B.A. (2002). Enzymes in Food Technology. Sheffield: Sheffield Academic Press.
31. Wijayanti, H.B., Bansal, N. & Deeth, H.C. (2014). Stability of whey proteins during thermal processing: a review. Comprehensive Reviews in Food Science and Food Safety, 13, 1235–1251.
32. de Wit, J. (2009). Thermal behaviour of bovine β-lactoglobulin at temperatures up to 150 degrees C. A review. Trends in Food Science & Technology, 20, 27–34.