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Purification of Bacillus licheniformis Lipase and its Application as an Additive in Detergent for Destaining
Journal of Surfactants and Detergents  (IF1.902),  Pub Date : 2021-04-22, DOI: 10.1002/jsde.12514
Rania Bredai, Ines Belhaj Ben Romdhane, Imen Bouchaala, Karima Srih Belghith, Hafedh Belghith

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.