Versatile biocatalyst: lipase from Streptomyces gobitricini for ester synthesis and detergent innovation
Background/objectivesThe 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).MethodsMaximal lipase activ...
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Frontiers Media S.A.
2025-05-01
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| Series: | Frontiers in Bioengineering and Biotechnology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fbioe.2025.1589087/full |
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| author | Areej Ali Alzahrani Najeh Krayem Mona Alonazi Jihan M. Al-Ghamdi Habib Horchani Abir Ben Bacha |
| author_facet | Areej Ali Alzahrani Najeh Krayem Mona Alonazi Jihan M. Al-Ghamdi Habib Horchani Abir Ben Bacha |
| author_sort | Areej Ali Alzahrani |
| collection | DOAJ |
| description | Background/objectivesThe 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).MethodsMaximal 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.ResultsCalcium, 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°C and 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.ConclusionThese 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. |
| format | Article |
| id | doaj-art-c709b946fe38436fb747a3dc00cb2f72 |
| institution | OA Journals |
| issn | 2296-4185 |
| language | English |
| publishDate | 2025-05-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Bioengineering and Biotechnology |
| spelling | doaj-art-c709b946fe38436fb747a3dc00cb2f722025-08-20T02:31:00ZengFrontiers Media S.A.Frontiers in Bioengineering and Biotechnology2296-41852025-05-011310.3389/fbioe.2025.15890871589087Versatile biocatalyst: lipase from Streptomyces gobitricini for ester synthesis and detergent innovationAreej Ali Alzahrani0Najeh Krayem1Mona Alonazi2Jihan M. Al-Ghamdi3Habib Horchani4Abir Ben Bacha5Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi ArabiaLaboratory of Biochemistry and Enzymatic Engineering of Lipases, ENIS, University of Sfax, Sfax, TunisiaDepartment of Biochemistry, College of Science, King Saud University, Riyadh, Saudi ArabiaDepartment of Biochemistry, College of Science, King Saud University, Riyadh, Saudi ArabiaScience Department, Environmental and biotechnology research group, College of Rivière-Du-Loup, Quebec, QC, CanadaDepartment of Biochemistry, College of Science, King Saud University, Riyadh, Saudi ArabiaBackground/objectivesThe 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).MethodsMaximal 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.ResultsCalcium, 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°C and 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.ConclusionThese 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.https://www.frontiersin.org/articles/10.3389/fbioe.2025.1589087/fullindustrial applicationsbiocatalysislipase purificationstabilitydetergent formulationsesterification |
| spellingShingle | Areej Ali Alzahrani Najeh Krayem Mona Alonazi Jihan M. Al-Ghamdi Habib Horchani Abir Ben Bacha Versatile biocatalyst: lipase from Streptomyces gobitricini for ester synthesis and detergent innovation Frontiers in Bioengineering and Biotechnology industrial applications biocatalysis lipase purification stability detergent formulations esterification |
| title | Versatile biocatalyst: lipase from Streptomyces gobitricini for ester synthesis and detergent innovation |
| title_full | Versatile biocatalyst: lipase from Streptomyces gobitricini for ester synthesis and detergent innovation |
| title_fullStr | Versatile biocatalyst: lipase from Streptomyces gobitricini for ester synthesis and detergent innovation |
| title_full_unstemmed | Versatile biocatalyst: lipase from Streptomyces gobitricini for ester synthesis and detergent innovation |
| title_short | Versatile biocatalyst: lipase from Streptomyces gobitricini for ester synthesis and detergent innovation |
| title_sort | versatile biocatalyst lipase from streptomyces gobitricini for ester synthesis and detergent innovation |
| topic | industrial applications biocatalysis lipase purification stability detergent formulations esterification |
| url | https://www.frontiersin.org/articles/10.3389/fbioe.2025.1589087/full |
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