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Physicochemical and bioactive properties of whey protein hydrolysates produced using gastric and pancreatic proteinases

Mullally, Margaret Maria (1996) Physicochemical and bioactive properties of whey protein hydrolysates produced using gastric and pancreatic proteinases. PhD thesis, Dublin City University.

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Abstract

This project investigated the contribution of gastric and pancreatic enzymes to some physicochemical and biological activity characteristics of whey protein hydrolysates. Depending on the method of isolation, and particularly on the zymogen activation conditions, it was shown in this study that the endoproteinase and exopeptidase activities in pancreatic preparations can exist in different ratios. Furthermore, it has been shown that certain physicochemical characteristics of whey protein hydrolysates can be altered by manipulation of the zymogen activation conditions of pancreatic protease preparations. Novel whey protein derived peptide inhibitors of angiotensin I converting enzyme (ACE), generated using pancreatic proteinases, have been identified in this study. Differential scanning calorimetry (DSC) was used to study the thermal stability of an enriched fraction of [3-lactoglobulin. The susceptibility of (3-lactoglobulin to hydrolysis by gastric and pancreatic proteinases was related to the thermal stability of the protein. A pilot scale (tangential crossflow plate and frame) ultrafiltration system was investigated with the view to developing a procedure for the fractionation and continuous hydrolysis of whey proteins.

Item Type:Thesis (PhD)
Date of Award:1996
Refereed:No
Supervisor(s):Fitzgerald, Richard and Dalton, John P.
Uncontrolled Keywords:Whey protein hydrolysates; Enzymology; Gastric and pancreatic enzymes
Subjects:Biological Sciences > Biotechnology
DCU Faculties and Centres:DCU Faculties and Schools > Faculty of Science and Health > School of Biotechnology
Use License:This item is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 3.0 License. View License
ID Code:19101
Deposited On:03 Sep 2013 11:21 by Celine Campbell. Last Modified 03 Sep 2013 11:21

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