IN SILICO ON STUDY CHITINASE AND CHITIN COMPLEX
Authors: Kaushik R , PANDEY J, BHARDWAJ N, KUMAR S AND RANA S

ABSTRACT
Chitin, the second most abundant natural biopolymer, is composed of repeating units of N-acetyl?- D-glucosamine and primarily forms the structural component of protective biological matrices such as fungal cell walls and exoskeletons of insects. Chitinases are a ubiquitous class of extracellular enzymes that have gained attention in the past few years due to their wide range of biotechnological applications, especially in the field of agriculture for bio-control of fungal phytopathogens. They play an important role in the defence of organisms against chitin-containing parasites by hydrolyzing the ?-1,4-linkages in chitin and hence act as anti-fungal as well as antibiofouling agents. Moreover, the effectiveness of conventional insecticides is increasingly compromised by the occurrence of resistance and thus, chitinases offer a potential alternative to the use of chemical fungicides. In recent years, thermostable enzymes isolated from thermophilic microorganisms have gained widespread attention in industrial, medical, environmental and biotechnological applications due to their inherent stability at high temperatures and a wide range of pH optima. Determination of the three- dimensional structure of a protein can provide important details about its biological functions and its mode of action. However, despite their significance, the precise three-dimensional structures of most of the chitinases, including those isolated from Thermomyces lanuginosusis not fully characterized so far. Hence, the main focus of the present study was to gain a better understanding of the structural of chitinases computational techniques, and their relationship with their activity profiles. In silico protein modeling was helpful in predicting the 3D models of the novel chitinase class IV Brassica Juncea, followed by the prediction of its active sites. The presence of different amino acid was found to be essential for the activity of chitinase IV. A Molecular docking were performed between chitinase IV and Chitin. Keywords: Chitin, chitinases, Thermomyces lanuginosusis
Publication date: 01/04/2024
    https://ijbpas.com/pdf/2024/April/MS_IJBPAS_2024_7964.pdf
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https://doi.org/10.31032/IJBPAS/2024/13.4.7964