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

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Abstract
This work describes the effect of the hydrolysis time and pressure (0·1-lactoglobulin A (-lg under pressure or hydrolysing -lg. Trypsin degraded pressure-modified -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 -lg under high pressure are discussed.

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