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Repository of Research and Investigative Information

Baqiyatallah University of Medical Sciences

A cold-adapted endoglucanase from camel rumen with high catalytic activity at moderate and low temperatures: an anomaly of truly cold-adapted evolution in a mesophilic environment

(2018) A cold-adapted endoglucanase from camel rumen with high catalytic activity at moderate and low temperatures: an anomaly of truly cold-adapted evolution in a mesophilic environment. Extremophiles. pp. 315-326. ISSN 1431-0651

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Abstract

Endoglucanases are important enzymes in plant biomass degradation. They have current and potential applications in various industrial sectors including human and animal food processing, textile, paper, and renewable biofuel production. It is assumed that the cold-active endoglucanases, with high catalytic rates in moderate and cold temperatures, can improve the cost-effectiveness of industrial processes by lowering the need for heating and, thus, energy consumption. In this study, the endoglucanase CelCM3 was procured from a camel rumen metagenome via gene cloning and expression in Escherichia coli BL21 (DE3). The maximum activity of the enzyme on carboxymethyl cellulose (CMC) was obtained at pH 5 and 30 A degrees C with a V (max) and K (m) of 339 U/mg and 2.57 mg/ml, respectively. The enzyme with an estimated low melting temperature of 45 A degrees C and about 50 activity at 4 A degrees C was identified to be cold-adapted. A thermodynamic analysis corroborated that CelCM3 with an activation energy (E (a)), enthalpy of activation (Delta H), and Gibb's free energy (Delta G) of, respectively, 18.47 kJ mol(-1), 16.12 kJ mol(-1), and 56.09 kJ mol(-1) is a cold-active endoglucanase. In addition, CelCM3 was tolerant of metal ions, non-ionic detergents, urea, and organic solvents. Given these interesting characteristics, CelCM3 shows promise to meet the requirements of industrial applications.

Item Type: Article
Keywords: Endoglucanase Cold-adapted Camel rumen Metagenome Catalytic activity cellulase expression cloning purification enzymes metagenomics optimization performance gene Biochemistry & Molecular Biology Microbiology
Divisions:
Page Range: pp. 315-326
Journal or Publication Title: Extremophiles
Journal Index: ISI
Volume: 22
Number: 2
Identification Number: https://doi.org/10.1007/s00792-018-0999-6
ISSN: 1431-0651
Depositing User: مهندس مهدی شریفی
URI: http://eprints.bmsu.ac.ir/id/eprint/3886

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