Fuente: PubMed "microbial biotechnology" Int J Biol Macromol. 2026 May 29:152798. doi: 10.1016/j.ijbiomac.2026.152798. Online ahead of print.ABSTRACTMicrobial alkaline proteases represent some of the most crucial industrial enzymes, supporting diverse biotechnological processes. In this study, Bacillus atrophaeus WML2023L1, isolated from compost soil, was optimized for high-level alkaline protease production of 8941.46 ± 119.41 U/mL. The purified enzyme (BWLP) with an approximate molecular weight of 28 kDa, showed strong activity and stability across a broad pH range and moderate temperatures, and remained stable in oxidizing conditions. Additive-response profiling showed that Mn2+ enhanced activity, non-ionic surfactants, especially Triton X-100, were generally compatible, and BWLP remained stable in 1% hydrogen peroxide (H2O2) but was impaired at higher oxidant levels. A multi-scale computational approach linking enzyme structure, substrate interactions, and dynamic behavior with experimentally observed catalytic properties revealed how metal ions modulate catalytic-triad hydrogen bonding, explained competitive pocket occupancy and peptide-binding effects of surfactants, and clarified peroxide-driven structural perturbations. Organic solvents with small polar groups displaced cavity water and reduced catalytic competence, whereas bulkier polyols caused minimal interference. Our findings reveal the previously untapped potential of B. atrophaeus as a source of robust enzymes, as exemplified by BWLP, which shows high promise for industrial applications under variable chemical conditions.PMID:42217692 | DOI:10.1016/j.ijbiomac.2026.152798