Open AccessInteraction of Enzyme-Substrate from Indigenous Cellulolytic Bacteria by Bioinformatics
Author(s) -
Yanty Maryanty,
Tri adryati,
Suharjono Suharjono,
Sutiman Bambang Sumitro
Publication year - 2020
Publication title -
iop conference series. materials science and engineering
Language(s) - English
Resource type - Journals
eISSN - 1757-899X
pISSN - 1757-8981
DOI - 10.1088/1757-899x/854/1/012068
Subject(s) - asparagine , biochemistry , cellulase , in silico , tryptophan , homology modeling , cellulose , enzyme , chemistry , serine , amino acid , biology , stereochemistry , gene
This study aims to predict the degradation mechanism of cellulose substrate in silico from the results of isolation and test the potential of cellulolytic bacteria from rice fields in Greater Malang in producing cellulolytic enzymes, among others: β-1, 4 exoglunase, β-1, 4 endoglucase and β - glucosidase, identified isolates that have high potential in producing cellulolytic enzymes based on 16S rDNA ie isolates A, B, D and F. Only Isolate B was successfully predicted by its substrate enzyme interaction both homologically and based on the results of the isolation of the cellulite gene. Homology B isolate analysis results showed that the hydrogen bonds that occur in glutamic acid GLU257, tryptophan 207, serine 264 and glutamic acid 169, while hydrophobic interactions occur in tryptophan 207 bonds. While the results of the analysis based on isolation of cellulase encoding genes from isolate B were predicted in-silico showed the interaction between hydrogen bonds in tyrosin (TRY 299), glutamine (GLU201 and GLU 342.72), Asparagine (ASN 200) and glycine (GLY 384). This interaction is slightly different from the insilico results obtained homologically i.e there is no interaction with serine and glutamate acid, but with asparagine. Isolate B predicted that its homology in silico can degrade cellulose substrate with the binding affinity of -7.0 Kcal/mol while based on the results of isolation of cellulase encoding genes shows the degradation ability of cellulose substrate with the binding affinity of -6.5 Kcal/mol.