Tengku Abdul Hamid, Tengku Haziyamin and Raja Abd. 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
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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 nzymatic activities were retained in up to45% v/v solvent compositions. The near-UV CD spectra indicated that ertiary 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 b-sheet and an increase in a-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.
Item Type: | Article (Journal) |
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Additional Information: | 4261/301 |
Uncontrolled Keywords: | molten globule, solven stable lipase, hydrophilic solvent, overexpression, thermostable lipase |
Subjects: | Q Science > Q Science (General) Q Science > QR Microbiology |
Kulliyyahs/Centres/Divisions/Institutes (Can select more than one option. Press CONTROL button): | Kulliyyah of Science |
Depositing User: | Dr Tengku Haziyamin Tengku Abd Hamid |
Date Deposited: | 31 May 2011 11:25 |
Last Modified: | 19 Dec 2011 16:12 |
URI: | http://irep.iium.edu.my/id/eprint/301 |
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