Biochemical approaches of increasing thermostability of beta-amylase from Bacillus megaterium B6.

Purification and Characterization of a Novel Thermostable and Acid Stable α-Amylase from Bacillus Sp. Iranian S1

This study reports the purification and biochemical characterization of thermostable and acidic-pH-stable α-amylase from Bacillus sp. Iranian S1 isolated from the desert soil (Gandom-e-Beryan in Lut desert, Iran). Amylase production was found to be growth associated. Maximum enzyme production was in exponential phase with activity 2.93 U ml-1 at 50°C and pH 5. The enzyme was purified by isoprop...

Characterization of an a-Amylase with Broad Temperature Activity from an Acid-Neutralizing Bacillus cereus Strain

Bacillus sp. GUF8, isolated from acidic soil samples of a tea farm was identified as Bacillus cereus, based on 16S rDNA sequencing and standard bacterial identification methods. Following optimization of enzyme production, the resulting α-amylase was purified by acetone precipitation and ion exchange chromatography. Consequently, thermostability and kinetic parameters of the purified enzyme wer...

The Role of Highly Conserved Tryptophan in the Sixth Conserved Region at Substrate Specificity of α- amylase

Early in this study, an α-Amylase from Bacillus megaterium WHO (BMW) was isolated from hot springs of Ramsar (North of Iran), and its gene was cloned in E.coli. Based on its conserved sequence regions and substrate specificity, it was classified as intermediary group enzymes with the specificity of oligo-1,6-glucosidase and neopullulanase subfamilies. In the sixth conserved re...

Thermostable α-amylase from Lignocellulosic Residues Using Bacillus amyloliquefaciens

Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis alpha-amylase.

The irreversible thermal inactivation of Bacillus licheniformis alpha-amylase was studied. A two-step behaviour in the irreversible denaturation process was found. Our experimental results are consistent only with the two-step model and rule out the two-isoenzyme one. They suggest that the deactivation mechanism involves the existence of a temperature-dependent intermediate form. Therefore the ...