Abstract
The stability of biocatalysts is an important criterion for a sustainable industrial operation economically. T1 lipase is a thermoalkalophilic enzyme derived from Geobacillus zalihae strain T1 (T1 lipase) that was isolated from palm oil mill effluent (POME) in Malaysia. We report here the results of high temperatures molecular dynamics (MD) simulations of T1 lipase in explicit solvent. We found that the N-terminal moiety of this enzyme was accompanied by a large flexibility and dynamics during temperature-induced unfolding simulations which preceded and followed by clear structural changes in two specific regions; the small domain (consisting of helices α3 and α5, strands β1 and β2, and connecting loops) and the main catalytic domain or core domain (consisting of helices α6- α9 and connecting loops which located above the active site) of the enzyme. The results suggest that the small domain of model enzyme is a critical region to the thermostability of this organism.
Keywords: Thermostability, thermoalkalophilic enzyme, lipase, protein dynamics, flexibility
Protein & Peptide Letters
Title: Deciphering the Flexibility and Dynamics of Geobacillus zalihae Strain T1 Lipase at High Temperatures by Molecular Dynamics Simulation
Volume: 16 Issue: 11
Author(s): Mohd Basyaruddin Abdul Rahman, Roghayeh Abedi Karjiban, Abu Bakar Salleh, Donald Jacobs, Mahiran Basri, Adam Leow Thean Chor, Habibah Abdul Wahab and Raja Noor Zaliha Raja Abd Rahman
Affiliation:
Keywords: Thermostability, thermoalkalophilic enzyme, lipase, protein dynamics, flexibility
Abstract: The stability of biocatalysts is an important criterion for a sustainable industrial operation economically. T1 lipase is a thermoalkalophilic enzyme derived from Geobacillus zalihae strain T1 (T1 lipase) that was isolated from palm oil mill effluent (POME) in Malaysia. We report here the results of high temperatures molecular dynamics (MD) simulations of T1 lipase in explicit solvent. We found that the N-terminal moiety of this enzyme was accompanied by a large flexibility and dynamics during temperature-induced unfolding simulations which preceded and followed by clear structural changes in two specific regions; the small domain (consisting of helices α3 and α5, strands β1 and β2, and connecting loops) and the main catalytic domain or core domain (consisting of helices α6- α9 and connecting loops which located above the active site) of the enzyme. The results suggest that the small domain of model enzyme is a critical region to the thermostability of this organism.
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Abdul Rahman Basyaruddin Mohd, Karjiban Abedi Roghayeh, Salleh Bakar Abu, Jacobs Donald, Basri Mahiran, Thean Chor Leow Adam, Wahab Abdul Habibah and Abd Rahman Zaliha Raja Raja Noor, Deciphering the Flexibility and Dynamics of Geobacillus zalihae Strain T1 Lipase at High Temperatures by Molecular Dynamics Simulation, Protein & Peptide Letters 2009; 16 (11) . https://dx.doi.org/10.2174/092986609789353763
DOI https://dx.doi.org/10.2174/092986609789353763 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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