Authors
Chao Zhang, Jing Chen, Peixun Zhang, Jinnan Zong, Mingyu Geng, Xuying Yao, Jinxu Sun
Published in
Letters in applied microbiology. Jul 26, 2025. Epub Jul 26, 2025.
Abstract
Cold-active cellulases attract significant attention for their potential in energy-efficient bioprocesses under low-temperature conditions. In this study, a psychrotolerant bacterial strain, Pseudomonas fragi HsL3-1, was isolated from Hengshui Lake sediments and found to produce a novel endoglucanase, EG-22SJ. The enzyme demonstrated optimal activity at pH 5.0 and 25°C, retaining over 80% and 60% of peak activity at 15°C and 5°C, respectively, and exhibited exceptional tolerance to 20% organic solvents (e.g. n-hexane enhanced activity by 29.8%) and 1% surfactants (e.g. Tween 80). Kinetic analysis revealed high substrate affinity for CMC-Na with a Kₘ of 0.583 mg·mL-1 and Vₘₐₓ of 401 μmol·L⁻¹·min⁻¹. Activity was significantly activated by Ca²⁺ and Mg²⁺ but inhibited by Cu²⁺ and Hg²⁺. Culture optimization via response surface methodology increased cellulase production to 8.71 U·mL-1 under conditions of 15.24 g·L-1 CMC-Na, 20.54°C, pH 6.85, and 1.95% inoculation, yielding a 1.24-fold improvement. These integrated properties position EG-22SJ as a robust biocatalyst for sustainable low-temperature applications like biofuel production, food processing, and detergent formulation, highlighting the potential of non-extreme environments for enzyme discovery.
PMID:
40720756
Bibliographic data and abstract were imported from PubMed on 29 Jul 2025.
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