Novel Thermostable α-Amylase from Bacillus subtilis: Molecular Characterization, Optimization, and Docking-Based...

Area of Science:

• Biotechnology
• Enzymology
• Molecular Biology

Background:

• Bacterial alpha-amylases are crucial enzymes with broad industrial applications.
• There is a continuous need for novel alpha-amylases with improved properties for various biotechnological processes.

Purpose of the Study:

• To isolate and characterize a novel alpha-amylase-producing bacterium.
• To determine the enzyme's substrate specificity and binding interactions using molecular docking.

Main Methods:

• Isolation and identification of amylolytic bacteria (Bacillus subtilis S4).
• Enzyme characterization (optimal temperature, pH, time).
• Gene sequencing, protein analysis, homology modeling, and molecular docking.

Main Results:

• Bacillus subtilis S4 exhibited high amylolytic activity (63.68 U/ml).
• Optimal activity at 40°C and pH 7.0.
• Molecular docking showed highest affinity for amylopectin (-7.2 kcal/mol), identifying key catalytic residues.

Conclusions:

• The novel alpha-amylase from B. subtilis S4 possesses desirable industrial traits like stability and thermotolerance.
• It is a promising candidate for cost-effective starch processing and other biotechnological applications.