Molten Globule-Triggered Inactivation of a thermostable and solvent stable lipase in hydrophilic Solvents

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 w...

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Main Authors: Tengku Abdul Hamid, Tengku Haziyamin, Raja Abd. Rahman, Raja Noor Zaliha, Salleh, Abu Bakar, Basri, Mahiran
Format: Article
Language:English
Published: Springer 2010
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Online Access:http://irep.iium.edu.my/301/2/fulltext.pdf
http://irep.iium.edu.my/301/
http://dx.doi.org/10.1007/s10930-010-9251-7
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spelling my.iium.irep.3012011-12-19T08:12:27Z http://irep.iium.edu.my/301/ Molten Globule-Triggered Inactivation of a thermostable and solvent stable lipase in hydrophilic Solvents Tengku Abdul Hamid, Tengku Haziyamin Raja Abd. Rahman, Raja Noor Zaliha Salleh, Abu Bakar Basri, Mahiran Q Science (General) QR Microbiology 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. Springer 2010 Article REM application/pdf en http://irep.iium.edu.my/301/2/fulltext.pdf 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 http://dx.doi.org/10.1007/s10930-010-9251-7 doi:10.1007/s10930-010-9251-7
institution Universiti Islam Antarabangsa Malaysia
building IIUM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider International Islamic University Malaysia
content_source IIUM Repository (IREP)
url_provider http://irep.iium.edu.my/
language English
topic Q Science (General)
QR Microbiology
spellingShingle Q Science (General)
QR Microbiology
Tengku Abdul Hamid, Tengku Haziyamin
Raja Abd. Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
Basri, Mahiran
Molten Globule-Triggered Inactivation of a thermostable and solvent stable lipase in hydrophilic Solvents
description 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.
format Article
author Tengku Abdul Hamid, Tengku Haziyamin
Raja Abd. Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
Basri, Mahiran
author_facet Tengku Abdul Hamid, Tengku Haziyamin
Raja Abd. Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
Basri, Mahiran
author_sort Tengku Abdul Hamid, Tengku Haziyamin
title Molten Globule-Triggered Inactivation of a thermostable and solvent stable lipase in hydrophilic Solvents
title_short Molten Globule-Triggered Inactivation of a thermostable and solvent stable lipase in hydrophilic Solvents
title_full Molten Globule-Triggered Inactivation of a thermostable and solvent stable lipase in hydrophilic Solvents
title_fullStr Molten Globule-Triggered Inactivation of a thermostable and solvent stable lipase in hydrophilic Solvents
title_full_unstemmed Molten Globule-Triggered Inactivation of a thermostable and solvent stable lipase in hydrophilic Solvents
title_sort molten globule-triggered inactivation of a thermostable and solvent stable lipase in hydrophilic solvents
publisher Springer
publishDate 2010
url http://irep.iium.edu.my/301/2/fulltext.pdf
http://irep.iium.edu.my/301/
http://dx.doi.org/10.1007/s10930-010-9251-7
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