Abstract
The aim of the present study was to evaluate the β-mannosidase activity (β-d-mannoside mannohydrolase, EC 3.2.1.25) of human synovial fluid. It was shown to have a pH requirement of 3.5–4.0 and a Km value of 3.4·10−3 M using a p-nitro-phenyl-β-mannopyranoside as the substrate. β-Mannosidase is significantly more heat-labile than mammalian α-mannosidase; substrate competition studies suggest it is an independent glycosidase; and p-nitrophenyl-β-galactoside is observed to inhibit this enzyme. A wide distribution of β-mannosidase activity in mammalian tissue was demonstrated.
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