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A new family‐3 glycoside hydrolase from Penicillium oxalicum BL 3005 catalyzing tyrosol glucosylation to form salidroside
Author(s) -
Yang XuePeng,
Wang FangFang,
Yan Ji,
Ma Ke,
Mao DuoBin
Publication year - 2016
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1508
Subject(s) - salidroside , tyrosol , cellobiose , chemistry , glycoside , glycosyl , glycoside hydrolase , hydrolysis , stereochemistry , yield (engineering) , cellulase , organic chemistry , biochemistry , chromatography , phenols , materials science , metallurgy
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.