Abstract
Enzymatic hydrolysis of soy protein isolate by Corolase PP under high hydrostatic pressure conditions was studied and the effects of hydrolysis on antioxidant and antihypertensive activities were investigated. As observed, high hydrostatic pressure (80–300MPa) enhanced the hydrolytic efficiency of Corolase PP and decreased the surface hydrophobicity of the hydrolysates. Hydrolysates obtained at 200MPa for 4h had higher bioactivities (reducing power, ABTS radical-scavenging and ACE inhibitory activities). The molecular weight (MW) determination indicated that hydrolysis at high hydrostatic pressure could increase the production of small peptides (<3kDa) and the amino acid sequences of these peptides with different inhibitory abilities, less than 3kDa, in hydrolysates were identified using matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI TOF MS). These results indicated that high hydrostatic pressure combined with Corolase PP treatments could be used as a potential technology to produce bioactive peptides from soy protein isolate.
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