β-glucosidase and β-galactosidase from the periplasmic space of Rhizobium trifolii cells

Abstract

High amounts of β-glucosidase (MW 74,000) and β-galactosidase (MW 122,000) were isolated from the periplasmic space of Rhizobium trifolii 4S (infectious strain), compared with the cell homogenate. The characterization of β-glucosidase and β-galactosidase was determined. Both enzymes were inhibited by the addition of Cu2+, Fe2+, Zn2+, Hg2+ and p-chloromercuribenzoic acid. The β-glucosidase exhibited a strong hydrolytic activity on cellobiose, sophorose and laminaribiose to glucose, and the β-galactosidase degraded lactose and 0-β-d-galactosyl-1,3-d-arabinoside to their respective components. Both enzymes hydrolyzed polysaccharide only slightly. © 1982, Applied Microbiology, Molecular and Cellular Biosciences Research Foundation. All rights reserved.