Premium
Oxidative cross‐linking of wheat arabinoxylans by manganese peroxidase. Comparison with laccase and horseradish peroxidase. Effect of cysteine and tyrosine on gelation
Author(s) -
FigueroaEspinoza MariaCruz,
Morel MarieHélène,
Surget Anne,
Rouau Xavier
Publication year - 1999
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/(sici)1097-0010(19990301)79:3<460::aid-jsfa268>3.0.co;2-7
Subject(s) - phanerochaete , ferulic acid , chemistry , peroxidase , horseradish peroxidase , laccase , hydrogen peroxide , biochemistry , tyrosine , cysteine , lignin , covalent bond , food science , enzyme , organic chemistry
The potential of manganese peroxidase (MnP) from Phanerochaete chrysosporium to cross‐link wheat arabinoxylans, and to covalently link cysteine and tyrosine to the ferulic acid esterified on arabinoxylans, was investigated. MnP was able to gel arabinoxylans by oxidative coupling of their feruloyl groups, with concominant formation of dehydrodimers of ferulic acid. Whereas at high concentrations cysteine delayed gelation, at low concentrations it had no effect. Tyrosine did not affect gelation, but it accelerated the consumption of ferulic acid. The MnP was compared to laccase from Pycnoporus cinnabarinus and the couple hydrogen peroxide/horseradish peroxidase (H 2 O 2 /POD). © 1999 Society of Chemical Industry