ORIGINAL RESEARCH article
Front. Bioeng. Biotechnol.
Sec. Industrial Biotechnology
Volume 13 - 2025 | doi: 10.3389/fbioe.2025.1589087
Versatile biocatalyst: Lipase from Streptomyces gobitricini for ester synthesis and detergent innovation
Provisionally accepted
- 1Biochemistry Department, College of Sciences, King Saud University, Riyadh, Saudi Arabia
- 2Laboratoire de Biochimie et de Génie Enzymatique des Lipases, Ecole Nationale d'Ingénieurs de Sfax, Sfax, Tunisia
- 3Science Department, Environmental and biotechnology research group, College of Rivière-Du-Loup, Rivière-Du-Loup, QC G5R 1R1, Quebec, Canada
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The growing demand for reliable and stable biocatalysts has spurred research into microbial lipases for diverse industrial applications. This study focused on enhancing the production and purification of a lipase from Streptomyces gobitricini (LipS.g). Maximal lipase activity (420 U/mL) was achieved during the stationary phase after 84 h of incubation at 45°C and pH 8.0, using 2% glucose and 2% yeast extract as carbon and nitrogen sources, respectively. Calcium, olive oil, and Tween, at 1%, significantly enhanced LipS.g production, highlighting the role of triglycerides and detergents in enzyme induction and substrate emulsification. The purified 50-kDa enzyme displayed maximal activity at 50°C and pH 9.0, with thermal stability between 40-55°C and pH 5.0-10.0. While LipS.g efficiently hydrolyzed short and medium-chain triglycerides, it exhibited a preference for long-chain substrates, with a maximum reaction rate of 2500 µmol/min/mg and a Km value of 6.45 mM toward triolein (C18). LipS.g also demonstrated remarkable stability in detergent formulations, retaining more than 85% activity in the presence of surfactants, oxidizing agents, boron compounds, and enzyme inhibitors. Additionally, LipS.g catalyzed the esterification of oleic acid with starch and ethanol to produce starch oleate and ricinoleic acid. These findings establish LipS.g as a promising biocatalyst for applications in biocatalysis and detergent formulations, with potential uses in the food, beverage, cosmetic, and pharmaceutical industries.
Keywords: Industrial applications, Biocatalysis, Lipase purification, stability, Detergent formulations, Esterification
Received: 06 Mar 2025; Accepted: 02 May 2025.
Copyright: © 2025 Alonazi, KRAYEM, Alzahrani, Al-Ghamdi, Horchani and Ben Bacha. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: Abir Ben Bacha, Biochemistry Department, College of Sciences, King Saud University, Riyadh, Saudi Arabia
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