An Alkaline Amylopullulanase from AlkalophilicBacillussp. KSM-1378; Kinetic Evidence for Two Independent Active Sites for theα-1,4 andα-1,6 Hydrolytic Reactions
| Autor: | Kazuaki Igarashi, Susumu Ito, Katsuhisa Saeki, Katsutoshi Ara |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
biology
Stereochemistry Organic Chemistry Active site Pullulan General Medicine Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry chemistry.chemical_compound Hydrolysis chemistry Amylose Amylopectin biology.protein Maltotriose Raffinose Pullulanase activity Molecular Biology Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 59:662-666 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.59.662 |
| Popis: | Alkalophilic Bacillus sp. KSM-1378 produces an alkaline amylopullulanase that hydrolyzes both α-1,4 linkages in amylose, amylopectin, and glycogen and α-1,6 linkages in pullulan. The hydrolytic activities against amylose and pullulan were specifically inhibited by maltotriose (Ki = 0.5 mM), isomaltitol (Ki = 5.2 mM), and methyl α-D-galactoside (Ki = 40 mM) and by β-cyclodextrin (Ki = 0.9 mM), α-cyclodextrin (Ki = 11 mM), and raffinose (Ki = 31 mM), respectively, in a competitive manner in each case. Inhibition by N-bromosuccinimide of the α-amylase activity was prevented by amylose but not by pullulan, while inhibition by N-bromosuccinimide of the pullulanase activity was prevented by pullulan but not by amylose. Kinetics of reactions in the simultaneous presence of amylose and pullulan indicated that the observed rates of formation of products closely matched those predicted by a kientic model in which the α-1,4 and α-1,6 hydrolytic reactions were catalyzed at two independent active sites. Incubation of ... |
| Databáze: | OpenAIRE |
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