1. Certain Properties of α-Glucosidase fromMucor racemosus
- Author
-
Junjiro Ozawa, Yoshiki Yamasaki, and Yukio Suzuki
- Subjects
biology ,Chemistry ,Mucor racemosus ,Starch ,Maltose ,Isomaltose ,General Biochemistry, Genetics and Molecular Biology ,Enzyme assay ,Turanose ,chemistry.chemical_compound ,Biochemistry ,Amylose ,Maltotriose ,biology.protein ,General Agricultural and Biological Sciences - Abstract
The substrate and inhibitor specificities, and α-glucosyltransfer products of the purified α-glucosidase from the mycelia of Mucor racemosus were investigated. The enzyme hydrolyzed maltose, maltotriose, phenyl α-maltoside, isomaltose, soluble starch, and amylose liberating glucose, but did not act on sucrose. The enzyme hydrolyzed phenyl a-maltoside into glucose and phenyl α-glucoside. Maltotriose was the main a-glucosyltransfer product formed from maltose, and isomaltose was that from soluble starch. Tris and turanose inhibited the enzyme activity, but PCMB and EDTA did not. The enzyme hydrolyzed amylose liberating a-glucose. The enzyme was a glycoprotein containing 4.1% of neutral sugar. The neutral sugar was identified as mannose in the acid hydrolyzate of the enzyme.
- Published
- 1977