Partial purification and characterization of alpha-glucosidase fromPseudomonas fluorescensW

✍ Scribed by Arthur A. Guffanti; W. A. Corpe

• Publisher: Springer
• Year: 1976
• Tongue: English
• Weight: 688 KB
• Volume: 107
• Category: Article
• ISSN: 0302-8933
• DOI: 10.1007/bf00425338

✦ Synopsis

The e-glucosidase (C~-D-glucoside glucohydrolase, EC 3.2.1.20) of Pseudomonas fluorescens W was partially purified by (NH4)2SO4 fractionation, Sepha-dexG-200 and DEAE-cellulose column chromatography. The enzyme showed great specificity for maltose hydrolysis, with very little action against polymeric forms. Sucrose, isomaltose, a-methylglucoside, and maltobionic acid were not hydrolyzed. Turanose was a strong competitive inhibitor, and glucose a weaker one. Tris (2-amino-2-hydroxymethylpropan-1:3-diol) inhibited enzyme activity significantly only at alkaline pH. Mercuric, cupric, and silver cations strongly inhibited, and EDTA (ethylenediaminetetraacetate) weakly inhibited the enzyme. The isolated enzyme was rather unstable even at 4~ and was destroyed by freezing and lyophilization. Inositol and albumin had a slightly protective effect. Sulfhydryl-binding reagents strongly inhibited the enzyme.