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Transformation of 3,5‐dimethoxy‐4‐hydroxy cinnamic acid and its derivatives using enzyme from white‐rot fungus Trametes versicolor : Enzyme characteristics and its application
Author(s) -
Lacki K.,
Duvnjak Z.
Publication year - 1996
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/(sici)1097-4660(199603)65:3<211::aid-jctb399>3.0.co;2-a
Subject(s) - cinnamic acid , enzyme , chemistry , transformation (genetics) , trametes versicolor , food science , biochemistry , organic chemistry , stereochemistry , laccase , gene
Transformation of 3,5‐dimethoxy‐4‐hydroxy cinnamic acid (sinapic acid), sinapaldehyde, sinapine and sinapoyl in the model system containing an enzyme secreted by the fungus Trametes versicolor was investigated. The affinity of this enzyme was highest for sinapic acid followed by sinapaldehyde and sinapine. The optimum temperature and pH for these transformations were 50°C and pH 3·3, 50°C and pH 4·5, 60°C and pH 4·0 for sinapaldehyde, sinapine, and sinapic acid, respectively. The apparent heat of the enzyme‐sinapic acid complex formation is −2557·6 J mol −1 . Higher concentrations of sinapine and sinapic acid caused enzyme inhibition. When canola meal was treated with this enzyme the phenolics content in this commodity was decreased by 90%.