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Low molecular weight alkaline thermostable ?-amylase from Geobacillus sp. nov.


ABSTRACT: Industrial demands for enzymes that are stable in a broad range of conditions are increasing. Such enzymes, one of which is ?-amylase, could be produced by extremophiles. This study reports a thermostable ?-amylase produced by a newly isolated Geobacillus sp. nov. from a geothermal area. The phylogenetic analysis of the 16S rRNA gene showed that the isolate formed a separate branch with 95% homology to Geobacillus sp. After precipitation using ammonium sulphate followed by ion-exchange chromatography, the enzyme produced a specific activity of 25.1 (U/mg) with a purity of 6.5-fold of the crude extract. The molecular weight of the enzyme was approximately 12.2 kDa. The optimum activity was observed at 75 °C and pH 8. The activity increased in the presence of Ba2+ and Fe2+ but decreased in the presence of K+ and Mg2+. Ca2+ and Mn2+ increased the activity slightly. The activity completely diminished with the addition of Cu2+. EDTA and PMSF also sharply reduced enzyme activity. Although the stability was moderate, the low molecular weight could be an important feature for its future applications.

SUBMITTER: Febriani 

PROVIDER: S-EPMC6667821 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature

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Low molecular weight alkaline thermostable α-amylase from <i>Geobacillus</i> sp. nov.

Febriani   Rayyana   Ulya Mildatul M   Oesman Frida F   Akhmaloka   Iqbalsyah Teuku M TM  

Heliyon 20190729 7


Industrial demands for enzymes that are stable in a broad range of conditions are increasing. Such enzymes, one of which is α-amylase, could be produced by extremophiles. This study reports a thermostable α-amylase produced by a newly isolated <i>Geobacillus</i> sp. nov. from a geothermal area. The phylogenetic analysis of the 16S rRNA gene showed that the isolate formed a separate branch with 95% homology to <i>Geobacillus</i> sp. After precipitation using ammonium sulphate followed by ion-exch  ...[more]

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