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

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 p...

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Main Authors: Bukhari, Noramirah, Leow, Adam Thean Chor, Raja Abdul Rahman, Raja Noor Zaliha, Mohd Shariff, Fairolniza
Format: Article
Published: MDPI AG 2020
Online Access:http://psasir.upm.edu.my/id/eprint/85827/
https://www.mdpi.com/1420-3049/25/15/3433
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spelling my.upm.eprints.858272023-10-02T03:56:34Z http://psasir.upm.edu.my/id/eprint/85827/ Single residue substitution at N-terminal affects temperature stability and activity of L2 lipase Bukhari, Noramirah Leow, Adam Thean Chor Raja Abdul Rahman, Raja Noor Zaliha Mohd Shariff, Fairolniza 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. MDPI AG 2020 Article PeerReviewed 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 https://www.mdpi.com/1420-3049/25/15/3433 10.3390/molecules25153433
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
description 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.
format Article
author Bukhari, Noramirah
Leow, Adam Thean Chor
Raja Abdul Rahman, Raja Noor Zaliha
Mohd Shariff, Fairolniza
spellingShingle Bukhari, Noramirah
Leow, Adam Thean Chor
Raja Abdul Rahman, Raja Noor Zaliha
Mohd Shariff, Fairolniza
Single residue substitution at N-terminal affects temperature stability and activity of L2 lipase
author_facet Bukhari, Noramirah
Leow, Adam Thean Chor
Raja Abdul Rahman, Raja Noor Zaliha
Mohd Shariff, Fairolniza
author_sort Bukhari, Noramirah
title Single residue substitution at N-terminal affects temperature stability and activity of L2 lipase
title_short Single residue substitution at N-terminal affects temperature stability and activity of L2 lipase
title_full Single residue substitution at N-terminal affects temperature stability and activity of L2 lipase
title_fullStr Single residue substitution at N-terminal affects temperature stability and activity of L2 lipase
title_full_unstemmed Single residue substitution at N-terminal affects temperature stability and activity of L2 lipase
title_sort single residue substitution at n-terminal affects temperature stability and activity of l2 lipase
publisher MDPI AG
publishDate 2020
url http://psasir.upm.edu.my/id/eprint/85827/
https://www.mdpi.com/1420-3049/25/15/3433
_version_ 1781706648993136640
score 13.154949

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