E3S Web Conf.
Volume 233, 20212020 2nd International Academic Exchange Conference on Science and Technology Innovation (IAECST 2020)
|Number of page(s)||8|
|Section||BFS2020-Biotechnology and Food Science|
|Published online||27 January 2021|
Directed evolution and immobilization of new lipase Lip 906
1 School of Courses, Guangdong Pharmaceutical University, Guangzhou 510006, PR China
China and Guangdong key Laboratory of Pharmaceutical Bioactive Substances, Guangdong Pharmaceutical University, Guangzhou 510006, PR China
2 Guangzhou Yachun Cosmetics Manufacturing Co., Ltd, Guangzhou, 510080, China
* These authors contributed equally to this work.
Corresponding author: He Li: Email: firstname.lastname@example.org
In this experimental study, a new lipase named Lip 906 was screened out from a metagenomic library in the laboratory. To improve the stability of the enzyme and develop and apply it as soon as possible, we adopted directed evolution and immobilization methods. A random mutation library was constructed by error-prone PCR and finally, a mutant lipase Lip 5-D with increased enzyme activity was screened out and immobilized. The activity of the mutant enzyme Lip 5-D was improved by 4 times compared with the wild-type lipase Lip 906. The optimal reaction temperature rose by 4 °C, and by 3 °C after immobilization. The optimal reaction pH increased from 7.8 to 7.5. Both temperature stability and pH stability were improved. The mutant enzyme Lip 5-D can maintain about 70% of the relative activity after incubation at 65 °C for 2 h, and it can keep 60% at pH 3-10. Error-prone PCR and immobilization improve the catalytic activity and stability of the enzyme, and promote its development and application in many industries.
© The Authors, published by EDP Sciences 2021
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