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Functional properties of oat proteins modified by acylation, trypsin hydrolysis or linoleate treatment
Author(s) -
Ma C. Y.,
Wood D. F.
Publication year - 1987
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02542510
Subject(s) - succinylation , acylation , chemistry , trypsin , hydrolysis , chromatography , solubility , biochemistry , acetylation , organic chemistry , lysine , amino acid , enzyme , gene , catalysis
Proteins extracted from defatted oats were chemically modified by acylation (succinylation and acetylation), potassium linoleate treatment or partial hydrolysis with trypsin. Total essential amino acid content was slightly lowered by acetylation, but unaffected by succinylation. Gel filtration chromatography showed some dissociation of oat polypeptides by succinylation, while trypsin hydrolysis caused considerable breakdown of the protein. Solubility and emulsifying properties were significantly improved by all the modifications. Fat binding capacity was improved by acylation and linoleate treatment, while water hydration capacity and foaming properties were improved by trypsin and linoleate modifications. The gelling property was improved by acylation. When meat protein was substituted with oat protein in model wieners, there was a decrease in cook yield, cohesiveness and firmness. However, when compared to the unmodified oat protein, succinylation led to an improvement in performance in an emulsified meat system.