TRYPTIC AND CHYMOTRYPTIC HYDROLYSIS OF BETA-LACTOGLOBULIN-A, BETA-LACTOGLOBULIN-B AND BETA-LACTOGLOBULIN-AB AT AMBIENT AND HIGH-PRESSURE

Authors
VANWILLIGE RWG FITZGERALD RJ
Citation
Rwg. Vanwillige et Rj. Fitzgerald, TRYPTIC AND CHYMOTRYPTIC HYDROLYSIS OF BETA-LACTOGLOBULIN-A, BETA-LACTOGLOBULIN-B AND BETA-LACTOGLOBULIN-AB AT AMBIENT AND HIGH-PRESSURE, Milchwissenschaft, 50(4), 1995, pp. 183-186
Citations number
24
Categorie Soggetti
Food Science & Tenology
Journal title
Milchwissenschaft → ACNP
ISSN journal
00263788
Volume
50
Issue
4
Year of publication
1995
Pages
183 - 186
Database
ISI
SICI code
0026-3788(1995)50:4<183:TACHOB>2.0.ZU;2-F
Abstract
The differences in enzymatic hydrolysis of beta-lactoglobulin (beta-Ig ) A, B and AB by trypsin and chymotrypsin at ambient and high pressure have been studied. At ambient pressure, native beta-Ig A is hydrolyse d by trypsin and chymotrypsin approx. 3 times faster than beta-Ig B. T his difference might be ascribed to the substitution of Asp(64) in bet a Ig A with Gly(64) in beta-Ig B, which is located in an elongated loo p of the beta-Ig molecule. At higher pressures (100 MPa and 300 MPa) t he genetic variant associated differences in beta-Ig hydrolysis rates disappeared.