NDLI: Chymotrypsin selectively digests ß-lactoglobulin in whey protein isolate away from enzyme optimal conditions: potential for native -lactalbumin purification.

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Chymotrypsin selectively digests ß-lactoglobulin in whey protein isolate away from enzyme optimal conditions: potential for native -lactalbumin purification.

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Chymotrypsin selectively digests ß-lactoglobulin in whey protein isolate away from enzyme optimal conditions: potential for native -lactalbumin purification.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lisak, Katarina Toro-Sierra, Jose Kulozik, Ulrich Bozanic, Rajka Cheison, Seronei Chelulei
Description	Country affiliation: Croatia Author Affiliation: Lisak K ( Laboratory for Milk Technology and Dairy Products, Faculty of Food Technology and Biotechnology, University of Zagreb, Zagreb, Croatia.)
Abstract	The present study examines the resistance of the -lactalbumin to -chymotrypsin (EC 3.4.21.1) digestion under various experimental conditions. Whey protein isolate (WPI) was hydrolysed using randomised hydrolysis conditions (5 and 10% of WPI; pH 7.0, 7.8 and 8.5; temperature 25, 37 and 50 °C; enzyme-to-substrate ratio, E/S, of 0.1%, 0.5 and 1%). Reversed-phase high performance liquid chromatography (RP-HPLC) was used to analyse residual proteins. Heat, pH adjustment and two inhibitors (Bowman-Birk inhibitor and trypsin inhibitor from chicken egg white) were used to stop the enzyme reaction. While operating outside of the enzyme optimum it was observed that at pH 8.5 selective hydrolysis of ß-lactoglobulin was improved because of a dimer-to-monomer transition while -la remained relatively resistant. The best conditions for the recovery of native and pure -la were at 25 °C, pH 8.5, 1% E/S ratio, 5% WPI (w/v) while the enzyme was inhibited using Bowman-Birk inhibitor with around 81% of original -la in WPI was recovered with no more ß-lg. Operating conditions for hydrolysis away from the chymotrypsin optimum conditions offers a great potential for selective WPI hydrolysis, and removal, of ß-lg with production of whey protein concentrates containing low or no ß-lg and pure native -la. This method also offers the possibility for production of ß-lg-depleted milk products for sensitive populations.
File Format	HTM / HTML
ISSN	00220299
Issue Number	1
Volume Number	80
e-ISSN	14697629
Journal	Journal of Dairy Research
Language	English
Publisher	Cambridge University Press
Publisher Date	2013-02-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Veterinary Medicine Chymotrypsin Metabolism Lactalbumin Isolation & Purification Lactoglobulins Milk Proteins Chemistry Animals Chromatography, High Pressure Liquid Hot Temperature Hydrogen-ion Concentration Hydrolysis Milk Protease Inhibitors Pharmacology Substrate Specificity Whey Proteins Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Medicine Animal Science and Zoology Food Science

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Chymotrypsin selectively digests ß-lactoglobulin in whey protein isolate away from enzyme optimal conditions: potential for native -lactalbumin purification.

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Chymotrypsin selectively digests ß-lactoglobulin in whey protein isolate away from enzyme optimal conditions: potential for native -lactalbumin purification.