The purification and properties of an α-glucoside of Saccharomyces italicus Y1225
作者： Harlyn Halvorson , Loretta Ellias
DOI: 10.1016/0006-3002(58)90237-3
关键词: Hydrolysis 、 Enzyme 、 Alkyl 、 Tris 、 Alcohol 、 Substrate (chemistry) 、 Chemistry 、 Stereochemistry 、 Glucoside 、 Aglycone 、 Organic chemistry
摘要: Abstract The purification and properties of α-glucosidase from Saccharomyces italicus Y1225 have been studied. enzyme hydrolyzes α- D -glucosides to glucose the aglycone alcohol. pH optimum is 6.6–6.8. purified has a broad specificity against alkyl- aryl-α- but restricted holosides. -thioglucosides are complexants not substrates enzyme. activated by sulfhydryl agents K+, Na+, NH4+ or Li+, it inhibited amines at alkaline pH, sensitive heavy metals, p-chloromercuribenzoate iodoacetate. inhibition Tris both competitive with substrate. pKM-pH plots suggest that substrate hydrolysis involves an ionizable group pKa molecular weight approximately 85,000.
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