TpGUS79A had strict specificity toward the glycan moiety but poor specificity toward the aglycone moiety. TpGUS79A belonged to glycoside hydrolase family 79 (GH79) but shared low amino acid sequence identity (<35%) with the available GH79 GUS enzymes. The gene for TpGUS79A was then cloned and verified by heterologous expression in Pichia pastoris. First, TpGUS79A was purified and identified through matrix-assisted laser desorption ionization–tandem time of flight mass spectrometry (MALDI-TOF-TOF MS) and deglycosylation, indicating that TpGUS79A is a highly N-glycosylated monomeric protein with a molecular mass of around 85 kDa, including around 25 kDa of glycan moiety. In this study, we isolated a β-glucuronidase (TpGUS79A) from the filamentous fungus Talaromyces pinophilus Li-93 that can specifically and precisely convert GL to GAMG without the formation of the by-product glycyrrhetinic acid (GA) from the further hydrolysis of GAMG.

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