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CHARACTERIZATION OF PLASTEIN REACTION PRODUCTS FORMED BY PEPSIN, α‐CHYMOTRYPSIN, AND PAPAIN TREATMENT OF EGG ALBUMIN HYDROLYSATES
Author(s) -
EDWARDS J. H.,
SHIPE W. F.
Publication year - 1978
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.1365-2621.1978.tb15272.x
Subject(s) - chemistry , papain , trichloroacetic acid , chromatography , hydrolysate , chymotrypsin , hydrolysis , pepsin , sodium dodecyl sulfate , peptide bond , covalent bond , trypsin , peptide , enzyme , organic chemistry , biochemistry
ABSTRACT Gelled plastein reaction products were prepared by treating concentrated peptic hydrolysates of egg albumin with pepsin, α‐chymotrypsin, and papain. The relative firmness of these homogeneous gels was determined by comparing force‐distance curves obtained from puncture tests made with the Instron Universal Testing Machine. The effects of the choice of enzyme and degree of substrate hydrolysis on the plastein yield (increase in 10% Trichloroacetic acid precipitable material) and water solubility were investigated. Electrophoresis of plastein products in the presence of sodium dodecyl sulfate (SDS) indicated that no high molecular weight, protein‐like material was produced by the plastein reaction. It is suggested that plastein reactions lead to the formation of insoluble peptide aggregates. These aggregates are thought to be held together by noncovalent bonds rather than by covalent, peptide bonds, as has been reported previously.