Abstract
BackgroundChitin is one of the most abundant biopolymers on Earth, only trailing second after cellulose. The enzyme chitinase is responsible for the degradation of chitin. Chitinases are found to be produced by wide range of organisms ranging from archaea to higher plants. Though chitin is a major component of fungal cell walls and invertebrate exoskeletons, bacterial chitinase can be industrially generated at low cost, in facile downstream processes at high production rate. Microbial chitinases are more stable, active, and economically practicable compared to the plant- and animal-derived enzymes. ResultsIn the present study, computationally obtained results showed functional characteristics of chitinase with particular emphasis on bacterial chitinase which is fulfilling all the required qualities needed for commercial production. Sixty-two chitinase sequences from four different groups of organisms were collected from the RCSB Protein Data Bank. Considering one suitable exemplary sequence from each group is being compared with others. Primary, secondary, and tertiary structures are determined by in silico models. Different physical parameters, viz., pI, molecular weight, instability index, aliphatic index, GRAVY, and presence of functional motifs, are determined, and a phylogenetic tree has been constructed to elucidate relationships with other groups of organisms. ConclusionsThis study provides novel insights into distribution of chitinase among four groups and their characterization. The results represent valuable information toward bacterial chitinase in terms of the catalytic properties and structural features, can be exploited to produce a range of chitin-derived products.
Highlights
Chitin is one of the most abundant biopolymers on Earth, only trailing second after cellulose
Just recently, a new family of chitinase from Thermococcus chitonophagus has been reported by Horiuchi et al [6] which contains two additional chitin-binding domains along with catalytic domains
Retrieval of the sequences from Research Collaboratory for Structural Bioinformatics (RCSB) Protein Data Bank (PDB) A total of 62 different chitinase sequences of archaeal, bacterial, fungal, and plant origin have been retrieved from the RCSB protein data bank on 4 October 2018
Summary
Chitin is one of the most abundant biopolymers on Earth, only trailing second after cellulose. The enzyme chitinase is responsible for the degradation of chitin. Chitinases are found to be produced by wide range of organisms ranging from archaea to higher plants. Though chitin is a major component of fungal cell walls and invertebrate exoskeletons, bacterial chitinase can be industrially generated at low cost, in facile downstream processes at high production rate. Chitin represents the second most abundant carbohydrate after cellulose, occurring as natural insoluble biopolymer featuring linear β-1,4-linkages between N-acetyl D-glucosamine (GlcNAc). It is extensively distributed in nature in different forms and constitutes, among other things, an essential component of the shells of crustaceans and Aspergillus, Trichoderma, etc. Just recently, a new family of chitinase from Thermococcus chitonophagus has been reported by Horiuchi et al [6] which contains two additional chitin-binding domains along with catalytic domains
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