Affiliation:
1. School of Food Science and Engineering South China University of Technology Guangzhou People's Republic of China
2. Guangdong Youmei Institute of Intelligent Bio‐manufacturing Foshan People's Republic of China
Abstract
AbstractCold‐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.
Funder
National Key Research and Development Program of China
National Natural Science Foundation of China
Special Project for Research and Development in Key areas of Guangdong Province
Science and Technology Planning Project of Guangdong Province
Basic and Applied Basic Research Foundation of Guangdong Province