biostudies-literatureAhmad WHigher Education Commision, Pakistane0298716https://www.ebi.ac.uk/biostudies/studies/S-EPMC11095671biostudies-literatureUnknown19(5)The purpose of current research work was to investigate the effect of mutagenesis on endoglucanase B activity of indigenous strain of Aspergillus niger and its heterologous expression studies in the pET28a+ vector. The physical and chemical mutagens were employed to incorporate mutations in A. niger. For determination of mutations, mRNA was isolated followed by cDNA synthesis and cellulase gene was amplified, purified and sequenced both from native and mutant A. niger. On comparison of gene sequences, it was observed that 5 nucleotide base pairs have been replaced in the mutant cellulase. The mutant recombinant enzyme showed 4.5 times higher activity (428.5 µmol/mL/min) as compared to activity of native enzyme (94 µmol/mL/min). The mutant gene was further investigated using Phyre2 and I-TePloS oneHeterologous expression and characterization of mutant cellulase from indigenous strain of Aspergillus niger.PMC11095671NRPU-6485Anwar ZAhmad WZafar MfalseHeterologous expression and characterization of mutant cellulase from indigenous strain of Aspergillus niger.The purpose of current research work was to investigate the effect of mutagenesis on endoglucanase B activity of indigenous strain of Aspergillus niger and its heterologous expression studies in the pET28a+ vector. The physical and chemical mutagens were employed to incorporate mutations in A. niger. For determination of mutations, mRNA was isolated followed by cDNA synthesis and cellulase gene was amplified, purified and sequenced both from native and mutant A. niger. On comparison of gene sequences, it was observed that 5 nucleotide base pairs have been replaced in the mutant cellulase. The mutant recombinant enzyme showed 4.5 times higher activity (428.5 µmol/mL/min) as compared to activity of native enzyme (94 µmol/mL/min). The mutant gene was further investigated using Phyre2 and I-Te2024-01-01T00:00:00Z20242026-06-01T17:30:58.974Z2026-04-08T14:20:11.152ZS-EPMC110956713874870310.1371/journal.pone.0298716