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The non-covalent immobilization of β-glucuronidase enzyme obtained from Rhizopus oryzae was carried out by entrapment in natural fiber (papaya and coconut). The bioconversion capability of immobilized enzyme was analyzed based on conversion of glycyrrhizin to 18β-glycyrrhetinic acid under different conditions. The hydrolytic activity of the β-glucuronidase enzyme was highly depended on the microbial source and matrix, in which enzyme was immobilized. R. oryzae β-glucuronidase immobilized in papaya fibers produced the highest GA content (13.170 μg/mL) at 10 h of reaction. However R. oryzae β-glucuronidase immobilized in coconut fibers produced the highest GA content (21.425 μg/mL) at 15 h of reaction. Online Molinspiration software was used to predict drug like molecular properties of the 18β-glycyrrhetinic acid, and software suggested that the compounds had potential of becoming the orally active molecules. Therefore, in silico studies were conducted on proposed 18β-glycyrrhetinic acid to select the best possible drug candidates based on drug properties and bioactivity score of the compounds.

Immobilization of β-glucuronidase: biocatalysis of glycyrrhizin to 18β-glycyrrhetinic acid and in-silico lead finding