Immobilization of thermostable, bacterial cellulase from Stenotrophomonas maltophilia in agar-agarose matrices and its characterization

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Research Paper 01/09/2018
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Immobilization of thermostable, bacterial cellulase from Stenotrophomonas maltophilia in agar-agarose matrices and its characterization

Rohini Tamilanban, Sam Ebenezer Rajadas, Vignesh Sounderrajan, Shakila Harshavardhan
Int. J. Biosci. 13(3), 198-208, September 2018.
Copyright Statement: Copyright 2018; The Author(s).
License: CC BY-NC 4.0

Abstract

Cellulase the biocatalyst for conversion of cellulose into simple sugars is gaining global economic importance owing to its wide application in various industrial and clinical domains. Commercial cellulase is preferred to be stable in adverse conditions and to be recovered from the reactor once the process is done. Hence, a search for such a cellulase still exists even though it was discovered six decades ago. In this study, purified thermostable cellulase from Stenotrophomonas maltophilia was immobilized on an agar-agarose matrix, and the properties of immobilized cellulase were studied. The optimum temperature and pH for immobilized enzyme activity were found to be 50oC and 8.0 respectively. The immobilized enzyme exhibited its stability at much wider alkaline pH ranges and higher temperatures even after 24 hours incubation. Km and Vmax values of the immobilized enzyme were 6.618 mg/ml and 131.578 µmol/min/mg of protein respectively. Both free and immobilized forms of enzymes were inhibited significantly by Hg2+ metal ion and the activity of the latter was affected in the presence of detergents and additives at higher concentration. The agar-agarose immobilized enzyme could be reused up to 5 repeated cycles and it is stable for at least 1 month when stored at 4oC. Hence this immobilized cellulase with good storage stability than the soluble one can be considered for commercial applications.

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