| Literature DB >> 27222303 |
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.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