Screening, cloning, enzymatic properties of a novel thermostable cellulase enzyme, and its potential application on water hyacinth utilization

Cellulose is the cheapest, natural, renewable organic substance that used as a carbon source in various fields. Water hyacinth, an aquatic plant rich cellulose, often raw material fuel production. However, natural cellulase can be hardly industrial production on account of its low thermal stability and activity. In this study, metagenomic library was constructed. Then, new gene, cel1029, screened by Congo red staining expressed prokaryotic system. Enzymatic properties Cel1029 were explored, including optimum temperature pH, pH stability, tolerance against solvents, metal ions, salt solutions. Finally, ability degrading water hyacinth identified evaluated. displayed high homology with endoglucanase glycoside hydrolase family 5 (GH5) had across broad range. More than 86% enzymatic activities retained between 4 60 °C after 24 h incubation. Single-factor analysis orthogonal design further conducted to determine optimal conditions for highest reducing sugar yield hyacinth. Interestingly, efficiently transformed 430.39 mg/g 22 h. These findings may open door significant applications novel GH5 (NCBI Reference Sequence: MK051001, Cel1029) help identify more efficient methods degrade cellulose-rich plants.