Guffanti A A, Corpe W A
Arch Microbiol. 1976 Apr 1;107(3):269-76. doi: 10.1007/BF00425338.
The alpha-glucosidase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20) of Pseudomonas fluorescens W was partially purified by (NH4)2SO4 fractionation, Sephadex G-200 and DEAE-cellulose column chromatography. The enzyme showed great specificity for maltose hydrolysis, with very little action against polymeric forms. Sucrose, isomaltose, alpha-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 degrees C, and was destroyed by freezing and lyophilization. Inositol and albumin had a slightly protective effect. Sulfhydryl-binding reagents strongly inhibited the enzyme.
荧光假单胞菌W的α-葡萄糖苷酶（α-D-葡萄糖苷葡糖水解酶，EC 3.2.1.20）通过硫酸铵分级沉淀、葡聚糖G-200和二乙氨基乙基纤维素柱色谱进行了部分纯化。该酶对麦芽糖水解具有高度特异性，对聚合形式的作用很小。蔗糖、异麦芽糖、α-甲基葡萄糖苷和麦芽酮酸不被水解。松二糖是一种强竞争性抑制剂，葡萄糖是较弱的抑制剂。三（2-氨基-2-羟甲基丙烷-1:3-二醇）仅在碱性pH下显著抑制酶活性。汞、铜和银阳离子强烈抑制该酶，而乙二胺四乙酸（EDTA）则微弱抑制该酶。分离出的酶即使在4℃也相当不稳定，并且会因冷冻和冻干而被破坏。肌醇和白蛋白有轻微的保护作用。巯基结合试剂强烈抑制该酶。
