Literature DB >> 27222303

A new family-3 glycoside hydrolase from Penicillium oxalicum BL 3005 catalyzing tyrosol glucosylation to form salidroside.

Xue-Peng Yang1,2, Fang-Fang Wang1,2, Ji Yan1,2, Ke Ma1,2, Duo-Bin Mao1,2.   

Abstract

A glycoside hydrolase from Penicillium oxalicum BL 3005 was purified to apparent homogeneity. Its molecular mass was estimated to be 90 kDa by SDS-PAGE. The enzyme was identified to be a new member of family-3 by peptide sequence. High transglycosylation activity was found in the hydrolytic reaction of cellobiose. In the reaction, salidroside (4-hydroxyphenethyl O-β-d-glucopyranoside) was formed by adding tyrosol as the glycosyl acceptor. The optimum reaction pH and temperature were pH 6.5 and 55 °C, respectively. The maximum yield of salidroside was almost 20 g/L. These results indicated that the β-glucosidase of P. oxalicum can be considered as a very promising catalyst for the synthesis of salidroside.
© 2016 International Union of Biochemistry and Molecular Biology, Inc.

Entities:  

Keywords:  Penicillium oxalicum; cellobiose; salidroside; transglycosylation; β-glucosidase

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Year:  2016        PMID: 27222303     DOI: 10.1002/bab.1508

Source DB:  PubMed          Journal:  Biotechnol Appl Biochem        ISSN: 0885-4513            Impact factor:   2.431


  1 in total

1.  Enzymatic Biosynthesis of Simple Phenolic Glycosides as Potential Anti-Melanogenic Antioxidants.

Authors:  Hogwuan Jung; JaeWook Oh; Younghae Kwon; Woongshin Kang; Minsuk Seo; Yurin Seol; Je Won Park
Journal:  Antioxidants (Basel)       Date:  2022-07-19
  1 in total

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