Characterization of a Thermostable α-Amylase from Bacillus licheniformis 104.K for Industrial Applications
Askar Kholikov, Khushnut Vokhidov, Azizjon Murtozoyev, Zoé S. Tóth, Gergely Nagy, Beáta G. Vértessy, Akhmadzhan Makhsumkhanov
Abstract
This study describes the characterization of a novel thermostable α-amylase from a Bacillus licheniformis 104.K strain isolated from the Kashkadarya region of Uzbekistan. Phylogenetic analysis revealed that the thermostable α-amylase belongs to glycoside hydrolase family 13 subfamily 5 (GH13_5) and shares high sequence similarity with known α-amylases. Our results demonstrate that the recombinant α-amylase exhibits optimal activity at pH 6.0 and 90 °C, retaining full activity after 30 min at 60 °C. The addition of CaCl2 significantly enhanced thermostability, with the enzyme retaining more than 95% of its initial activity at 70 °C after 30 min. Our findings indicate that α-amylase from B. licheniformis 104.K is a functional, thermostable enzyme with potential industrial applications. This study highlights the commercial significance of thermostable amylases and the need to identify novel, cost-effective, and sustainable sources. The results of this study will contribute to the fields of enzyme applications, stabilizing additives, and genetic engineering of thermostable genes.