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FLOW PROPERTIES OF OAT PROTEIN DISPERSIONS 1
Author(s) -
MA C.Y.
Publication year - 1993
Publication title -
journal of texture studies
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.593
H-Index - 54
eISSN - 1745-4603
pISSN - 0022-4901
DOI - 10.1111/j.1745-4603.1993.tb01287.x
Subject(s) - deamidation , hydrolysis , chemistry , trypsin , acylation , flow properties , dissociation (chemistry) , salt (chemistry) , protein aggregation , chromatography , biochemistry , organic chemistry , enzyme , physics , mechanics , catalysis
The effects of protein and salt concentrations, anions, and heating on thejlow properties of oat globulin dispersions were studied. Flow properries were greatly influenced by the conformation and state of aggregation‐dissociation of the oat protein polypeptides. Chemical modijications including deamidation, acylation, trypsin hydrolysis and linoleate treatment also change the flow characteristics of oat protein concentrates and isolates.