Properties of α-Mannosidase Partially Purified from the Apple Snail, Pomacea canaliculata

Abstract

  Pomacea canaliculata α-mannosidase (260 kDa), composed of at least two isoforms with different pI, was partially purified. The activity was maximum at pH 4 and unaltered after incubation at 60°C for 60 min. ZnCl₂, CaCl₂, NaCl, and SH-reagents increased the activity, while MnCl₂ and EDTA inhibited it. The enzyme catalyzed the hydrolysis of α1-2, α1-3, and α1-6 mannosidic linkages.