Related Experiment Video
Updated: Aug 19, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
A thermostable glucoamylase from a thermophilic Bacillus sp.: characterization and thermostability
Rupinder K Gill1, Jagdeep Kaur
1Department of Biotechnology, Panjab University, Chandigarh, 160 014, India.
Abstract:
A thermostable glucoamylase (GA) showed optimum activity at 70 degrees C and pH 5.0. It was highly stable at pH 7.0. The half-life of the enzyme at pH 7.0 was 13, 8, and 3 h 40 min at 60, 65, and 70 degrees C respectively. The residual activity of the enzyme sample incubated at 5 psi (110 degrees C) for 30 min was about 32% of the control set (incubated at 4 degrees C), while no activity was observed at 10 and 15 psi. The thermostability of the enzyme was enhanced twofold in the presence of 0.5% (w/v) starch at 5 psi. Thin-layer chromatography indicated that this enzyme is a GA.
More Related Videos
10:26Elucidating β-1,3-Glucanase and Peroxidase Physicochemical Properties of Wheat Cell Wall Defense Mechanism Against Diuraphis noxia Infestation
Published on: July 26, 2024
12:23Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Related Concept Videos
Diversity of Archaea IV
Hyperthermophilic Bacteria
Factors Influencing Microbial Growth: Temperature
Microbes in Food Production