Qinzhou Cai, Huifang Zhang, Bingshan Zhao, Lei Ren, Yonghua Wang, Fanghua Wang
{"title":"来自南海马林杆菌的一种适应低温且强健的碱性脂肪酶可提高洗衣粉性能","authors":"Qinzhou Cai, Huifang Zhang, Bingshan Zhao, Lei Ren, Yonghua Wang, Fanghua Wang","doi":"10.1002/jsde.12793","DOIUrl":null,"url":null,"abstract":"Cold‐adapted, alkali‐stable lipases with surfactant tolerance are highly sought after in the detergent industry. In this study, we recombinantly expressed and characterized a novel lipase from <jats:italic>Marinobacter nanhaiticus</jats:italic> (MNL). The purified MNL exhibited high stability within a temperature range of 10–30°C and pH values of 8–10, demonstrating optimal activity at 20°C and pH 8. MNL has a preference for substrates with medium chains with the best activity being 3768.6 U/mg using <jats:italic>p</jats:italic>‐nitrophenyl decanoate as a substrate. Remarkably, MNL showed enhanced enzymatic activity in the presence of ionic surfactants and displayed notable resilience when exposed to proteases. Washing performance analysis further revealed MNL's high proficiency in removing oil‐based stains from fabrics. Collectively, these results suggest that MNL holds significant promise as a valuable component in laundry detergent formulations.","PeriodicalId":17083,"journal":{"name":"Journal of Surfactants and Detergents","volume":"60 1","pages":""},"PeriodicalIF":1.6000,"publicationDate":"2024-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"A cold‐adapted and robust alkaline lipase from Marinobacter nanhaiticus boosts laundry detergent performance\",\"authors\":\"Qinzhou Cai, Huifang Zhang, Bingshan Zhao, Lei Ren, Yonghua Wang, Fanghua Wang\",\"doi\":\"10.1002/jsde.12793\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Cold‐adapted, alkali‐stable lipases with surfactant tolerance are highly sought after in the detergent industry. In this study, we recombinantly expressed and characterized a novel lipase from <jats:italic>Marinobacter nanhaiticus</jats:italic> (MNL). The purified MNL exhibited high stability within a temperature range of 10–30°C and pH values of 8–10, demonstrating optimal activity at 20°C and pH 8. MNL has a preference for substrates with medium chains with the best activity being 3768.6 U/mg using <jats:italic>p</jats:italic>‐nitrophenyl decanoate as a substrate. Remarkably, MNL showed enhanced enzymatic activity in the presence of ionic surfactants and displayed notable resilience when exposed to proteases. Washing performance analysis further revealed MNL's high proficiency in removing oil‐based stains from fabrics. Collectively, these results suggest that MNL holds significant promise as a valuable component in laundry detergent formulations.\",\"PeriodicalId\":17083,\"journal\":{\"name\":\"Journal of Surfactants and Detergents\",\"volume\":\"60 1\",\"pages\":\"\"},\"PeriodicalIF\":1.6000,\"publicationDate\":\"2024-08-13\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Surfactants and Detergents\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.1002/jsde.12793\",\"RegionNum\":4,\"RegionCategory\":\"工程技术\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"CHEMISTRY, APPLIED\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Surfactants and Detergents","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1002/jsde.12793","RegionNum":4,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
A cold‐adapted and robust alkaline lipase from Marinobacter nanhaiticus boosts laundry detergent performance
Cold‐adapted, alkali‐stable lipases with surfactant tolerance are highly sought after in the detergent industry. In this study, we recombinantly expressed and characterized a novel lipase from Marinobacter nanhaiticus (MNL). The purified MNL exhibited high stability within a temperature range of 10–30°C and pH values of 8–10, demonstrating optimal activity at 20°C and pH 8. MNL has a preference for substrates with medium chains with the best activity being 3768.6 U/mg using p‐nitrophenyl decanoate as a substrate. Remarkably, MNL showed enhanced enzymatic activity in the presence of ionic surfactants and displayed notable resilience when exposed to proteases. Washing performance analysis further revealed MNL's high proficiency in removing oil‐based stains from fabrics. Collectively, these results suggest that MNL holds significant promise as a valuable component in laundry detergent formulations.
期刊介绍：
Journal of Surfactants and Detergents, a journal of the American Oil Chemists’ Society (AOCS) publishes scientific contributions in the surfactants and detergents area. This includes the basic and applied science of petrochemical and oleochemical surfactants, the development and performance of surfactants in all applications, as well as the development and manufacture of detergent ingredients and their formulation into finished products.
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