Chitinase is a glycosyl hydrolase that cleaves chitin into oligomers. Stability of an enzyme during industrial procedures is a challenge because it directly affects the industrial processing of enzyme catalyzed bioproducts. In this study, chitinase was produced by Glutamicibacter uratoxydans. Chitinase was subjected to stability studies in the presence of different chemicals that could either acts as enhancers, stabilizers or inhibitors. Current results suggested that chitinase was greatly stimulated by Cu+2 ions whereas, the order of potency of inhibition of chitinase by different metal ions was K + > Fe+3 > Hg+2 > Ni+2 > Ba+2 > Zn+2 > Co+2 > Mn+2 > Cs+ > Ca+2 > Na+ . Two non-ionic (Tween-20 and Tween-80) and one anionic Sodium dodecyl Sulfate (SDS) surfactants inhibited the enzyme activity. Cetyl trimethylammonium bromide (CTAB) exhibited a stabilizing effect. Only 4-(1,1,3,3-Tetramethylbutyl) phenyl-polyethylene glycol (Triton X-100) was able to enhance the catalytic performance of chitinase in 1.0 mM and 5.0 mM concentrations. Percent relative activity decreased in the presence of different organic solvents and the order of inhibition noticed was isopropanol > formaldehyde > dimethyl sulfoxide (DMSO) > methanol > chloroform > ethanol. The results suggested that chitinase from G. uratoxydans KIBGE-IB41 is sensitive against different chemicals except for Triton-X100. Therefore, it is suggested that chitinase will be an ideal candidate along with Triton-X100 to be used in the bioremediation of hydrophobic compound at the contaminated sites for the solubilization of hydrophobic contaminants from the environment.
Tayyaba Asif, Aiman Pirzada , Asma Ansari, Nadir Naveed Siddiqui, Shah Ali Ul Qader, Afsheen Aman. (2019) INFLUENCE OF CHEMICAL STRESS ON THE STABILITY OF CHITINASE PRODUCED BY GLUTAMICIBACTER URATOXYDANS KIBGE-IB41, , Volume 16, Issue 2.
