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HYDROLYSATES FROM WHEAT BRAN ALBUMIN AS COLOR‐ADDING AGENTS AND INHIBITORS OF APPLE POLYPHENOL OXIDASE
Author(s) -
CAMPASRÍOS MANUEL DE JESÚS,
MERCADORUIZ JORGE NEMESIO,
VALDÉZCOVARRUBIAS MIGUEL ANGEL,
ISLASRUBIO ALMA ROSA,
MENDOZAWILSON ANA MARÍA,
BALANDRÁNQUINTANA RENÉ RENATO
Publication year - 2012
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2011.00553.x
Subject(s) - browning , polyphenol oxidase , hydrolysate , chemistry , food science , polyphenol , bran , biochemistry , hydrolysis , enzyme , antioxidant , raw material , peroxidase , organic chemistry
Albumin from wheat bran was subjected to proteolysis. Molecular weight profile and particle size distribution were analyzed in the hydrolysates, which were later assayed in both crude extracts and surfaces of apple mesocarp in order to test their effect on polyphenol oxidase activity and enzymatic browning; the latter measured as L *, hue ° and chroma *. Both the electrophoretic pattern and the size distribution showed, upon the hydrolysis, the appearance of aggregates with higher molecular weight than albumin. Polyphenol oxidase in crude extracts of apple was inhibited up to 40% by hydrolysates in a mixed way. The application of hydrolysates to mesocarp resulted in the impartment of a slight brownish color to the tissue and there were significant differences on L *, hue ° and chroma * with respect to treatments but not with respect to time ( P  < 0.05). PRACTICAL APPLICATIONS The hydrolysates produced from wheat bran albumin give their color to apple tissue when applied on its surface and also inhibit apple polyphenol oxidase, so the color is maintained with time. This property could be advantageous in situations where both color imparting and control of the enzymatic browning are desirable. Important aspects to consider are: the imparted color was nice by sight and wheat bran is an inexpensive source of proteins.

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