Low Molecular Weight Alkaline Thermostable α-amylase from Sp. Nov

Overview

Journal Heliyon

Specialty Social Sciences

Date 2019 Aug 8

PMID 31388592

Citations 2

Authors

Febriani

Rayyana

Mildatul Ulya

Frida Oesman

Akhmaloka

Teuku M Iqbalsyah

Affiliations

Soon will be listed here.

Abstract

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 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 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 Ba and Fe but decreased in the presence of K and Mg. Ca and Mn increased the activity slightly. The activity completely diminished with the addition of Cu. 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.

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