Title: Cold-active microbial enzymes: In silico approach to understand mechanism and their potential applications

Biography:

Mohammed Kuddus has completed his PhD in Enzyme Biotechnology from India. At present, he is working as a Professor and Chairman of Biochemistry Department at University of Hail, Saudi Arabia. Prof. Kuddus’s main research area includes enzyme and microbial biotechnology. He has published more than 60 research articles in reputed international journals along with 4 books and 15 book chapters; and presented more than 35 abstracts in national/international conference/symposia. He has been serving as an Editorial Board Member and Reviewer of various international reputed journals.

Abstract

Nowadays, cold-active enzymes and their anticipated applications in various industries attracted worldwide attention due to less energy requirement for their optimal activity in comparison to their meso and thermophilic counterparts. Until now, very few cold-active enzymes are known and least explored so far in various industries. In this study, cold-active cellulase from well-studied psychrophilic bacterium Pseudoalteromonas haloplanktis is evaluated for its mecahnism of action and industrial application compared to the normally used mesophilic and thermophilic cellulases by in silico approach. The cellulase structure from different origin subjected to molecular docking studies with the substrate cellulose by using MVD. The binding energy for thermo, meso and psychrophilic cellulase enzymes found to be -93.29, -75.54 and -126.60 KCals/mole, respectively. The results specify that psychrophilic cellulase enzyme from Pseudoalteromonas haloplanktis has more efficiency to bind with cellulose (Figure 1) in comparison to its mesophilic and thermophilic counterparts. The study showed that in silico approach could be used for the screening of different enzymes activity with specific substrate and cold-active cellulase may find better commercial application in food processing industry.