enhancing biomolecule production from bacillus velezensis phcl using low-cost agricultural residues as feedstock and improving biomass hydrolysis through enzyme mutagenesis
abstract
bioproduction have been considered an alternative option for obtaining useful and
eco-friendly chemicals for industrial applications. bacillus velezensis, a trending bacterium
first isolated in 2005, is well-known for its ability in producing various economic and
environmentally-friendly biomolecules, such as industrial enzymes, biosurfactants,
antioxidants, antibiotics, etc. however, most of the studies nowadays use edible sugar for
biomolecule production which increased the production cost meanwhile raises concerns
regarding hunger and food-energy competition. meanwhile, several genomic sequencing
studies suggested that various strains of b. velezensis have the ability in producing various
lignocellulase, such as xylanase and cmcase. however, very few studies use agricultural
wastes as feedstock for producing biomolecules. therefore, for advancing the utilization of
the lignocellulosic biomass, a newly isolated b. velezensis phcl was characterized, and its
potential for bioremediation was evaluated. furthermore, various agricultural wastes were
used as a fermentation feedstock for producing various biomolecules, and the amylase
production was optimized via response surface methodology. the remaining biomass residue
was also converted to biochar for further utilization. moreover, for advancing the utilization
of agricultural waste, a gh 11 xylanase was in silico analyzed and several mutants were
constructed based on the analysis. the mutant showed better hydrolysis efficiency and
released more reducing sugar from wheat straw. this study explored another approach for
utilizing b. velezensis for value-added biomolecule production, which could be used for
bioremediation and various industrial applications, from low-cost agricultural waste.
moreover, this study also contributed to the understanding of utilizing advanced computer programs for improving enzymatic performance meanwhile exploring the undermined
structure-function relationship of xylanase. [...]