PREDICTED STRUCTURE OF ENDOGLUCANASE Bacillus amyloliquefaciens PSM 3.1

• Main Author: Ch T, Joshua
• Format: Final Project
• Language: Indonesia
• Subjects: Kimia
• Online Access: https://digilib.itb.ac.id/gdl/view/35226
• Institution: Institut Teknologi Bandung

Cellulase is an enzyme which catalyzes the hydrolysis of cellulose into a simple sugar. Cellulase is mainly produced by fungi, bacteria, and protozoa. There are several kinds of cellulases and each of them has different protein structures and catalytic mechanisms. The marine bacteria Bacillus amyloliquefaciens PSM 3.1 is a bacterium producing cellulase and the protein structure of this enzyme has never been determined yet. In order to build a model structure of endoglucanase from B. amyloliquefaciens PSM 3.1, its amino acid sequence and their similar amino acid sequences from the database were aligned, and the result showed that the endoglucanase sequence of B. amyloliquefaciens PSM 3.1 had a sequence homology with the endoglucanase of Bacillus agaradhaerens. Based on this, the endoglucanase structure of B. agaradhaerens was used as a template for modelling of endoglucanase structure of B. amyloliquefaciens PSM 3.1. By using SWISS-MODEL, the endoglucanase structure of B. amyloliquefaciens PSM 3.1 was built. The characterization of model structure from endoglucanase B. amyloliquefaciens showed a triad catalytic active-site located at Thr256–His229–Glu169.