The intracellular α-galactosidase of a rumen strain of Streptococcus bovis

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Abstract
Cell extracts prepared from a rumen strain of Streptococcus bovis grown on glucose contain [alpha]-galactosidase, amylase, sucrose phosphorylase and occasionally isomaltase, but no other carbohydrases. fa the absence of phosphate sucrose is not hydrolyzed and sugars of the raffinose series are hydrolyzed to galactose and sucrose. The a-galactosidase readily hydrolyzes melibiose and other oligosaccharides containing [alpha]-(1[forward arrow]6)-linked galactose, but only hydrolyzes methyl [alpha]-D-galactoside, melibi-itol and manninotri-itol slowly; methyl [beta]-L-arabinopyranoside and 4-O-[alpha]-D-galactosyl-D-galactose are not hydrolyzed. The enzyme has optimum activity in the pH range 5.6-6.3 and temperature range 37-42[degree]. It may act as a transferase giving, with melibiose, sucrose or raffinose as acceptors, a single tri- or tetra-saccharide.