Bibliographic Details
| Title: |
A cold‐adapted and robust alkaline lipase from Marinobacter nanhaiticus boosts laundry detergent performance. |
| Authors: |
Cai, Qinzhou1 (AUTHOR), Zhang, Huifang1 (AUTHOR), Zhao, Bingshan1 (AUTHOR), Ren, Lei1 (AUTHOR), Wang, Yonghua1,2 (AUTHOR) yonghw@scut.edu.cn, Wang, Fanghua1 (AUTHOR) wangfanghua@scut.edu.cn |
| Source: |
Journal of Surfactants & Detergents. Mar2025, Vol. 28 Issue 2, p239-250. 12p. |
| Subject Terms: |
*IONIC surfactants, *LAUNDRY detergents, *LIPASES, *PROTEOLYTIC enzymes, *SURFACE active agents |
| 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 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. [ABSTRACT FROM AUTHOR] |
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| Database: |
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