Advances in Microbial Alkaline Proteases: Addressing Industrial Bottlenecks Through Genetic and Enzyme Engineering
- PMID: 40372653
- DOI: 10.1007/s12010-025-05270-9
Advances in Microbial Alkaline Proteases: Addressing Industrial Bottlenecks Through Genetic and Enzyme Engineering
Abstract
Microbial alkaline proteases are versatile enzymes chiefly employed in various industrial sectors, viz., food processing, detergents, leather, textile, pharmaceutical industries. However, the existing bottlenecks, such as lower enzyme yields, stability, purification, specificity, and catalytic rates, bring resistance toward their industrial suitability. The robust microbes are prominent sources of stable enzymes. However, further challenges may exist, such as low yield, difficult purification, and lesser enzymatic efficiency. With the advent of advanced genomic and enzyme engineering approaches, such bottlenecks can be overcome. Initially, the microbial genomes can be used as novel repositories for stable enzyme sequences for further heterologous production with higher enzymatic yields and an easier purification process. Moreover, enzyme improvement through directed evolution and rational engineering could enhance enzyme stability and efficiency. Currently, conventional enzyme improvement methods are increasingly replaced by Artificial Intelligence-Machine Learning (AI-ML) and computational data-driven tools that provide precise information for tailoring enzymes for industrial endeavors. Hence, the current review encompasses a deliberate study of microbial alkaline proteases, their major industrial applications, and the bottlenecks in their commercial implementations. Further, it presents in-detailed solutions, including genetic and enzyme engineering, and insights toward incorporating advanced tools like AI-ML and de novo enzyme engineering to subside the existing challenges.
Keywords: AI-ML tools; Alkaline proteases; Bottlenecks; De novo enzyme engineering; Genetic engineering; Industrial applications.
© 2025. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
Conflict of interest statement
Declarations. Ethics Approval and Consent to Participate: Not applicable. Consent for Publication: Not applicable. Competing interests: The authors declare no competing interests.
References
-
- Adrio, J., & Demain, A. (2014). Microbial enzymes: Tools for biotechnological processes. Biomolecules, 4(1), 117–139. https://doi.org/10.3390/biom4010117 - PubMed - PMC
-
- Beg, Q. K., & Gupta, R. (2003). Purification and characterization of an oxidation-stable, thiol-dependent serine alkaline protease from Bacillus mojavensis. Enzyme and Microbial Technology, 32(2), 294–304. https://doi.org/10.1016/S0141-0229(02)00293-4
-
- Chen, S., Maulu, S., Wang, J., Xie, X., Liang, X., Wang, H., … Xue, M. (2024). The application of protease in aquaculture: Prospects for enhancing the aquafeed industry. Animal Nutrition, 16, 105–121. https://doi.org/10.1016/j.aninu.2023.11.001
-
- Sharma, K. M., Kumar, R., Panwar, S., & Kumar, A. (2017). Microbial alkaline proteases: Optimization of production parameters and their properties. Journal of Genetic Engineering and Biotechnology, 15(1), 115–126. https://doi.org/10.1016/j.jgeb.2017.02.001 - PubMed - PMC
-
- Tacias-Pascacio, V. G., Castañeda-Valbuena, D., Morellon-Sterling, R., Tavano, O., Berenguer-Murcia, Á., Vela-Gutiérrez, G., … Fernandez-Lafuente, R. (2021). Bioactive peptides from fisheries residues: A review of use of papain in proteolysis reactions. International Journal of Biological Macromolecules, 184, 415–428. https://doi.org/10.1016/j.ijbiomac.2021.06.076
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
