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Molten globule-triggered inactivation of a thermostable and solvent stable lipase in hydrophilic solvents


Citation

Tengku Abdul Hamid, Tengku Haziyamin and Raja Abdul Rahman, Raja Noor Zaliha and Salleh, Abu Bakar and Basri, Mahiran (2010) Molten globule-triggered inactivation of a thermostable and solvent stable lipase in hydrophilic solvents. The Protein Journal, 29 (4). pp. 290-297. ISSN 1572-3887; ESSN: 1573-4943

Abstract

The use of lipase in hydrophilic solvent is usually hampered by inactivation. The solvent stability of a recombinant solvent stable lipase isolated from thermostable Bacillus sp. strain 42 (Lip 42), in DMSO and methanol were studied at different solvent-water compositions. The enzymatic activities were retained in up to 45% v/v solvent compositions. The near-UV CD spectra indicated that tertiary structures were perturbed at 60% v/v and above. Far-UV CD in methanol indicated the secondary structure in Lip 42 was retained throughout all solvent compositions. Fluorescence studies indicated formations of molten globules in solvent compositions of 60% v/v and above. The enzyme was able to retain its secondary structures in the presence of methanol; however, there was a general reduction in β-sheet and an increase in α-helix contents. The H-bonding arrangements triggered in methanol and DMSO, respectively, caused different forms of tertiary structure perturbations on Lip 42, despite both showing partial denaturation with molten globule formations.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Science
Faculty of Biotechnology and Biomolecular Sciences
DOI Number: https://doi.org/10.1007/s10930-010-9251-7
Publisher: Springer
Keywords: Molten globule; Solvent stable lipase; Hydrophilic solvent; Overexpression; Thermostable lipase
Depositing User: Najwani Amir Sariffudin
Date Deposited: 16 Oct 2013 05:10
Last Modified: 26 Sep 2016 07:23
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1007/s10930-010-9251-7
URI: http://psasir.upm.edu.my/id/eprint/15715
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