Characterization of a Thermostable α-Amylase from <i>Bacillus licheniformis</i> 104.K for Industrial Applications

• Published in: Microorganisms
• Main Authors: Askar Kholikov, Khushnut Vokhidov, Azizjon Murtozoyev, Zoé S. Tóth, Gergely N. Nagy, Beáta G. Vértessy, Akhmadzhan Makhsumkhanov
• Format: Article
• Language: English
• Published: MDPI AG 2025-07-01
• Subjects: <i>Bacillus licheniformis</i>; α-amylase; GH13_5 subfamily; thermostability; recombinant enzyme; affinity chromatography
• Online Access: https://www.mdpi.com/2076-2607/13/8/1757

This study describes the characterization of a novel thermostable α-amylase from a <i>Bacillus licheniformis</i> 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 <i>B. licheniformis</i> 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.