✦ LIBER ✦
Characterization of high pI α-glucosidase from germinated barley seeds: substrate specificity, subsite affinities and active-site residues
✍ Scribed by Hana Im; Cynthia A. Henson
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 984 KB
- Volume
- 277
- Category
- Article
- ISSN
- 0008-6215
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✦ Synopsis
Substrate specificity and subsite affinities of high pl o~-glucosidase from germinated barley (Hordeum vulgare L.) seeds were investigated by kinetics. The enzyme has only one maltose binding site per molecule and shows high activity on small maltooligosaccharides and nigerose. Hydrolysis of isomaltose and p-nitrophenyl c~-glucoside is moderate. Trehalose is not hydrolyzed at detectable rates. The ratios of the maximum velocities for maltose, nigerose, isomaltose, p-nitrophenyl ot-glucoside and malto-triose, -tetraose, -pentaose, -