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Influence of high hydrostatic pressure on the proteolysis of β-lactoglobulin A by trypsin

Published online by Cambridge University Press:  24 January 2006

Rosa Chicón
Affiliation:
Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva, 3, 28006 Madrid, Spain
Josefina Belloque
Affiliation:
Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva, 3, 28006 Madrid, Spain
Isidra Recio
Affiliation:
Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva, 3, 28006 Madrid, Spain
Rosina López-Fandiño
Affiliation:
Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva, 3, 28006 Madrid, Spain

Abstract

This work describes the effect of the hydrolysis time and pressure (0·1–400 MPa) on the proteolysis of β-lactoglobulin A (β-lg A) with trypsin, either conducting hydrolysis of β-lg under pressure or hydrolysing β-lg that was previously pressure treated. Pressurisation, before or during enzyme treatments, enhanced tryptic hydrolysis of β-lg. Trypsin degraded pressure-modified β-lg and pressure-induced β-lg aggregates, favouring proteolysis to the intermediate degradation products: (Val15-Arg40), (Val41-Lys69)S-S(Leu149-Ile162) and (Val41-Lys70)S-S(Leu149-Ile162). These were further cleaved at the later stages of proteolysis to yield: (Val15-Tyr20), (Ser21-Arg40), (Val41-Tyr60), (Trp61-Lys69)S-S(Leu149-Ile162) and (Trp61-Lys70)S-S(Leu149-Ile162). Particularly, in the tryptic hydrolysates of pre-pressurized β-lg, two other fragments linked by disulphide bonds: (Lys101-Arg124)S-S(Leu149-Ile162) and (Tyr102-Arg124)S-S(Leu149-Ile162), were found. These corresponded to rearrangement products induced by SH/SS exchange between the free thiol group of Cys121 and Cys160, that normally forms the disulphide bond Cys66-Cys160. In the light of these results, structural modifications of β-lg under high pressure are discussed.

Type
Research Article
Copyright
Proprietors of Journal of Dairy Research 2006

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