1988 Volume 52 Issue 1 Pages 207-210
Glycyrrhizinic acid hydrolase produced by Aspergillus niger selectively hydrolyzed the 3-O-β-D-glucuronide linkage of glycyrrhizinic acid. The substrate specificity of this enzyme was investigated for synthetic glucuronides of aliphatic alcohols as well as natural glucuronide saponins. It was revealed that the glucuronide linkage with low molecular weight alcohols was not cleaved by this enzyme, while the 3-O-β-D-glucuronide linkage of saponins of oleanolic acid was selectively hydrolyzed. It was also disclosed that both the 4-hydroxyl and carboxyl groups of the glucuronide moiety must be unsubstituted for hydrolysis by this enzyme.
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