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Biologically Active Components Inactivation and Protein Insolubilization during Heat Processing of Soybeans
Author(s) -
SAVAGE W.D.,
WEI L.S.,
SUTHERLAND J.W.,
SCHMIDT S.J.
Publication year - 1995
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1995.tb05630.x
Subject(s) - chemistry , trypsin , urease , lipoxygenase , trypsin inhibitor , blanching , biochemistry , enzyme , solubility , limiting , kunitz sti protease inhibitor , hydrolysis , chromatography , food science , organic chemistry , mechanical engineering , engineering
Inactivation of lipoxygenase, trypsin inhibitor, urease and retention of protein solubility during water blanching of dehulled soybeans at 90°, 95° and 100°C were investigated. Lipoxygenase was the most heat labile, followed by urease and then trypsin inhibitor. Processing time based on “acceptable inactivation time” (AI) was proposed. AI value was longest for trypsin inhibitor, followed by urease and then lipoxygenase. The combined effect of heat on protein solubility and biologically active components inactivation was expressed as “PDI at acceptable inactivation time” (PDIAI). PDIAI value for the processing “limiting factor,” trypsin inhibitor inactivation, at the three temperatures were 36.7%, 42.5%, and 34.8%, respectively.