Thermal adaptation analysis of Bacterial chitinases: comparison of chemical Characteristics and residues composition

Chitin and chitin-derived products have wide variety of medical and industrial applications. Chitinases are glycosyl hydrolases that catalyze the conversion of chitin biopolymer to low molecular weight chitooligomers [1-2].Computational tools and techniques can analyse and identify the sequentially and structurally properties, which trigger the chitinase (enzymes) to tolerate the extreme temperature and or PH, then these results could be used for designing and reconstruction chitinases with desired temperature and/or PH characteristics.Therefore, in this study twenty amino acid sequnces of mesophilic, thermophilic, hyperthermophilic and psychrophilic chitinase were assessed to identify the variation in their physiochemical properties and amino acids composition which are responsible in making them to adapt in various conditions. Physiochemical properties using ProtParam tool [3], showed positivley charged residues (Arg+Lys) to be stastically significant contributing for the thermostability of chitinase.Multiple sequence alignment of the amino acid sequences of chitinases showed DxxDxDxE motis conserved between catalytic domains of variouse chitinases. Cysteine (C) was high in the psychrophilic chitinases in comparison to their counterpart.

کلیدواژه ها:

chitinase ، tempreature and cysteine