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Single residue substitution at N-terminal affects temperature stability and activity of L2 lipase


Bukhari, Noramirah and Leow, Adam Thean Chor and Raja Abdul Rahman, Raja Noor Zaliha and Mohd Shariff, Fairolniza (2020) Single residue substitution at N-terminal affects temperature stability and activity of L2 lipase. Molecules, 25 (15). art. no. 3433. pp. 1-18. ISSN 1420-3049


Rational design is widely employed in protein engineering to tailor wild-type enzymes for industrial applications. The typical target region for mutation is a functional region like the catalytic site to improve stability and activity. However, few have explored the role of other regions which, in principle, have no evident functionality such as the N-terminal region. In this study, stability prediction software was used to identify the critical point in the non-functional N-terminal region of L2 lipase and the effects of the substitution towards temperature stability and activity were determined. The results showed 3 mutant lipases: A8V, A8P and A8E with 29% better thermostability, 4 h increase in half-life and 6.6 °C higher thermal denaturation point, respectively. A8V showed 1.6-fold enhancement in activity compared to wild-type. To conclude, the improvement in temperature stability upon substitution showed that the N-terminal region plays a role in temperature stability and activity of L2 lipase.

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Official URL or Download Paper: https://www.mdpi.com/1420-3049/25/15/3433

Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
DOI Number: https://doi.org/10.3390/molecules25153433
Publisher: MDPI AG
Keywords: Lipase; Thermostability; Rational design; Stability prediction; Homology modelling
Depositing User: Nurul Ainie Mokhtar
Date Deposited: 02 Oct 2023 03:56
Last Modified: 02 Oct 2023 03:56
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.3390/molecules25153433
URI: http://psasir.upm.edu.my/id/eprint/85827
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