In silico Characterization of Cellulases from Genus Bacillus
Journal Title: International Journal of Current Research and Review - Year 2017, Vol 9, Issue 13
Abstract
Background: Cellulases are hydrolytic enzymes which hydrolyze β-1,4-glycosidic linkage in cellulose and these are present in many microorganisms including bacteria, fungi and protozoa. The three types of cellulases involved in complete hydrolysis of cellulose are endoglucanase, exoglucanase and β-glucosidase. Various structural and functional domains are present in cellulases and among all these domains, cellulose binding and catalytic domains are found to be important for the hydrolysis of cellulose. Cellulases have showed promising applications in different industrial sectors like paper and pulp, textile, laundry, bioethanol production, brewing, detergent and waste management. A major focus has been given in the recent past by researchers to understand the functional domains and catalytic mechanism of this enzyme to make their effective use for industrial applications. Material and Methods: The protein sequences of cellulases belonging to different Bacillus sp. were retrieved using Uniprot and then physicochemical properties were analyzed using ProtParam and Protscale. Multiple sequence alignment of retrieved sequences was performed using Clustal W and phylogenetic tree was constructed using Mega 6.0 software. SOPMA and GOR IV tools were used for the prediction of secondary structure. The tertiary structure of enzyme was computed using Raptor X. Results: The molecular weight of cellulases were found to range between 49,263-94,682 Da with hydropathicity ranges between -0.292 to -0.580. The acidic amino acid glutamate was found at the active site and methionone was found at the N-terminal of enzyme. The results have shown that the sequence is highly diversed at N-terminus and C-terminus region between different types of cellulases with conserved sequences in the middle. The phylogenetic tree has showed high similarity amongst retrieved sequences. From the tertiary structure, a great degree of variability in α-helix, extended strand in β ladder, hydrogen bonded turn, bend and coil was observed between different types of cellulases. Conclusion: This study provides insights about the physicochemical properties, hydrohobicity, structure and function of cellulases, which would help to exploit this enzyme at industrial level.
Authors and Affiliations
Balwinder Singh Sooch
Keywords
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- EP ID EP606441
- DOI 10.7324/IJCRR.2017.9136
- Views 115
- Downloads 0
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