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- W2394647593 abstract "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." @default.
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- W2394647593 date "2016-09-26" @default.
- W2394647593 modified "2023-10-16" @default.
- W2394647593 title "A new family-3 glycoside hydrolase from <i>Penicillium oxalicum</i> BL 3005 catalyzing tyrosol glucosylation to form salidroside" @default.
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- W2394647593 doi "https://doi.org/10.1002/bab.1508" @default.
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