We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
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.
- Authors
Khalili Ghadikolaei, Kamran; Gharechahi, Javad; Haghbeen, Kamahldin; Akbari Noghabi, Kambiz; Hosseini Salekdeh, Ghasem; Shahbani Zahiri, Hossein
- 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 <italic>Escherichia coli</italic> BL21 (DE3). The maximum activity of the enzyme on carboxymethyl cellulose (CMC) was obtained at pH 5 and 30 °C with a <italic>V</italic>max and <italic>K</italic>m of 339 U/mg and 2.57 mg/ml, respectively. The enzyme with an estimated low melting temperature of 45 °C and about 50% activity at 4 °C was identified to be cold-adapted. A thermodynamic analysis corroborated that CelCM3 with an activation energy (<italic>E</italic>a), enthalpy of activation (Δ<italic>H</italic>), and Gibb’s free energy (Δ<italic>G</italic>) 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.
- Subjects
PLANT biomass; BIODEGRADATION; CARBOXYMETHYLCELLULOSE; METAGENOMICS; MOLECULAR cloning
- Publication
Extremophiles, 2018, Vol 22, Issue 2, p315
- ISSN
1431-0651
- Publication type
Article
- DOI
10.1007/s00792-018-0999-6