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Updated: Feb 13, 2026

Prevention of Heat Stress Adverse Effects in Rats by Bacillus subtilis Strain
Published on: July 11, 2016
Isolation and characterization of a cold-active, alkaline, detergent stable α-amylase from a novel bacterium Bacillus
Nihan Arabacı1, Burhan Arıkan1
1a Department of Biology , Çukurova University , Adana , Turkey.
Abstract:
A cold-active alkaline amylase producer Bacillus subtilis N8 was isolated from soil samples. Amylase synthesis optimally occurred at 15°C and pH 10.0 on agar plates containing starch. The molecular weight of the enzyme was found to be 205 kDa by performing SDS-PAGE. While the enzyme exhibited the highest activity at 25°C and pH 8.0, it was highly stable in alkaline media (pH 8.0-12.0) and retained 96% of its original activity at low temperatures (10-40°C) for 24 hr. While the amylase activity increased in the presence of β-mercaptoethanol (103%); Ba2+, Ca2+, Na+, Zn2+, Mn2+, H2O2, and Triton X-100 slightly inhibited the activity. The enzyme showed resistance to some denaturants: such as SDS, EDTA, and urea (52, 65, and 42%, respectively). N8 α-amylase displayed the maximum remaining activity of 56% with 3% NaCl. The major final products of starch were glucose, maltose, and maltose-derived oligosaccharides. This novel cold-active α-amylase has the potential to be used in the industries of detergent and food, bioremediation process and production of prebiotics.
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