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

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.

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

“…Indeed, the enzyme displayed the lowest K m value (0.16 mM) for the glucosylation of HPP2 compared to those for HPP3 (0.22 mM), displaying StSPGT’s preference for HPP2 as the acceptor substrate over HPP3. These apparent K m values appear to be comparable to those reported for other microbial- or plant-origin simple phenolic glycosyltransferases [ 1 , 16 , 22 , 28 ]. Depending upon the donor substrates, several fold differences were found in the K m values; 0.16 and 0.22 mM when a Glc moiety was incorporated into each aglycone vs. 0.41 and 0.50 mM when a 2′dGlc-moiety was.…”

“…However, when it comes to their corresponding glycosides, although their bio-absorption rate is not as high, their solubility and bioavailability can be enhanced more than aglycones [ 1 , 3 , 16 , 18 ]. In this regard, several studies [ 22 , 23 , 24 , 25 , 26 , 27 , 28 ] in which various organic or enzymatic synthesis methods were employed have consistently reported the manufacture of a series of SP glycosides. Enhanced bioactivities through structural modifications to the parental molecules are recognized as a feasible tool for the reformulation of the dosage forms of cosmetics and medicines; the enzymatic biosynthesis of glycosides using glycosyltransferase (GT) is capable of transferring the sugar moiety from the nucleotide activated glycosyl donors onto the hydroxyl function within the target aglycones ( ; accessed on 1 July 2022).…”