Purification of Bacillus licheniformis Lipase and its Application as an Additive in Detergent for Destaining |
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| Authors: | Rania Bredai Ines Belhaj Ben Romdhane Imen Bouchaala Karima Srih Belghith Hafedh Belghith |
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| Affiliation: | 1. Laboratory of Plant Biotechnology Applied to the Improvement of Cultures, Faculty of Sciences of Sfax, University of Sfax, PB 802, Sfax, 3018 Tunisia;2. Laboratory of Molecular Biotechnology of Eukaryotes, Biotechnology Center of Sfax, University of Sfax, BP “1177”, Sfax, 3018 Tunisia |
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| Abstract: | In this study, we aimed to optimize the nutritional and environmental conditions for the production of a novel lipase (LBL) from Bacillus licheniformis (GenBank accession no. MT118724). This strain was characterized by morphological and biochemical assays and Sanger sequencing of 16S rDNA. The crude lipolytic activity reached a maximum level 7.5 U mL−1 at 40 °C and pH 8.0 using olive oil as substrate. Additionally, the crude enzyme maintained 100% of its initial activity after incubation for 1 h at 50 °C and pH 9.0. It is mandatory to note that LBL lipase displayed appreciable stability over a wide pH range and extreme temperatures. After purification, the optimal lipolytic activity was observed at pH 8.0 and 40 °C. LBL was shown to be a monomeric protein with an estimated molecular weight of 40 kDa. This novel lipase exhibited high stability and excellent compatibility compared to lipase extracted from Thermomyces lanuginosa (Lipolase® from Novozymes, Denmark) toward various detergents. Washing performance analysis revealed that it efficiently removes tomato sauce stain from cotton cloth. All these interesting enzymatic properties favor this new lipase as a potent candidate for applications in detergent formulations. |
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| Keywords: | Bacillus licheniformis Lipase Purification Characterization Detergent formulation |
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