Characterization of a novel thermophilic beta-glucosidase from sp. and its application in the transformation of notoginsenoside R1.

A novel β-glucosidase (Thglu3) was identified from sp. which had biotransformation activity for notoginsenoside R1 (NR-R1). Sequence analysis of Thglu3 revealed that it could be classified into glycoside hydrolase family 3 (GH3). The gene encoding a 719-amino acid protein was cloned and expressed in The recombinant enzyme was purified, and its molecular weight was approximately 81 kDa. The recombinant Thglu3 exhibited an optimal activity at 75 °C and pH 6.4. The β-glucosidase had high selectivity for cleaving the outer glucose moiety at the C20 position of NR-R1, which produced the more pharmacologically active notoginsenoside R2 (NR-R2). Under the optimal reaction conditions for gram-scale production, 30 g NR-R1 was transformed to NR-R2 using 20 g crude enzyme at pH 6.4 and 75 °C within 1 h with a molar yield of 93%. This study was the first report of the highly efficient and selective gram-scale transformation of NR-R2 from NR-R1 by a thermophilic β-glucosidase.