• Log In
  • New issue alert
  • Submit a manuscript
  • Register
  • Home
  • About
  • Editorial Board
  • Search
  • Archives
  • Current
  • Forthcoming

Share

Article Panel


Vol 39 (2019)
»Table of Contents
Reading Tools
  • About the author
  • How to cite this article
  • Indexing metadata
  • Print version
  • Look up terms
  • Finding References
  • Review policy

Related items
  • Author's work


Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivatives 4.0 International.
Improvement of the alkali stability of Penicillium cyclopium lipase by error-prone PCR | Huang | Electronic Journal of Biotechnology
doi:10.1016/j.ejbt.2019.04.002
Electronic Journal of Biotechnology, Vol 39 (2019)

Improvement of the alkali stability of Penicillium cyclopium lipase by error-prone PCR

Lin Huang, Dong Zheng, Yatong Zhao, Jieying Ma, Yanzhen Li, Zehua Xu, Mengying Shan, Shulin Shao, Qingwen Guo, Jie Zhang, Fuping Lu, Yihan Liu



Abstract

Background: Lipases are extensively exploited in lots of industrial fields; cold-adapted lipases with alkali-resistance are especially desired in detergent industry. Penicillium cyclopium lipase I (PCL) might be suitable for applications of detergent industry due to its high catalytic efficiency at low temperature and relatively good alkali stability. In this study, to better meet the requirements, the alkali stability of PCL was further improved via directed evolution with error-prone PCR.

Results: The mutant PCL (N157F) with an improved alkali stability was selected based on a high-throughput activity assay. After incubating at pH 11.0 for 120 min, N157F retained 70% of its initial activity, which was 23% higher than that of wild type PCL. Combined with the three-dimensional structure analysis, N157F exhibited an improved alkali stability under the high pH condition due to the interactions of hydrophilicity and β-strand propensity.

Conclusions: This work provided the theoretical foundation and preliminary data for improving alkali stability of PCL to meet the industrial requirements, which is also beneficial to improving alkali-tolerance ability of other industrial enzymes via molecular modification.




Full Text: | Reprint PDF | HTML

ISSN:  0717-3458

Contact: edbiotec@pucv.cl

Pontificia Universidad Católica de Valparaíso
Av. Brasil 2950, Valparaíso, Chile
Copyright © 1997- 2022 by Electronic Journal of Biotechnology