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Expression and characterization of a thermostable lipase from Thermomyces dupontii

Xiao-Jun Li, Qi Li, Xing-Xin Zhan, Yu-Juan Zhang, Guo-Lan Xiong, and Jian-Yong Zheng

Department of Foundamental Medicine, Xinyu University, Xinyu, People’s Republic of China

 

E-mail: lxj341401@163.com

Received: 16 September 2021  Accepted: 4 January 2022

Abstract:

Interest in the identification of thermostable lipases for industrial applications is growing. Herein, the novel thermostable lipase TDL2 was identified from the thermophilic fungus Thermomyces dupontii ATCC 16461 and its gene was cloned and overexpressed in Pichia pastoris. The recombinant TDL2 was purified and biochemically characterized. The optimal conditions for hydrolytic activity were identified as 50 °C and pH 8.5. Interestingly, the enzyme was stable at 50 °C and stable over the pH range of 6.5–9.0. Additionally, the activity analysis for various p-nitrophenyl acyl esters indicated that the lipase TDL2 showed higher specific activity for medium- and long-chain substrates, as well as the highest activity toward p-nitrophenyl laurate. Furthermore, the lipase TDL2 exhibited excellent enantioselectivity (E > 200) in the kinetic resolution of 2-carboxyethyl-3-cyano-5-methylhexanoic acid ethyl ester. Given the excellent enantioselectivity, TDL2 is an interesting enzyme for industrial applications.

Keywords: Lipase; Thermomyces dupontii; Thermostable; Characterization; Enantioselectivity

Full paper is available at www.springerlink.com.

DOI: 10.1007/s11696-022-02068-5

 

Chemical Papers 76 (5) 2811–2821 (2022)

Tuesday, April 23, 2024

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