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...

Full description

Bibliographic Details
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
Subjects:	Q Science (General) QR Microbiology
Online Access:	http://irep.iium.edu.my/301/ http://irep.iium.edu.my/301/ http://irep.iium.edu.my/301/ http://irep.iium.edu.my/301/2/fulltext.pdf

id	iium-301
recordtype	eprints
spelling	iium-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 PeerReviewed 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
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
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/ http://irep.iium.edu.my/301/ http://irep.iium.edu.my/301/ http://irep.iium.edu.my/301/2/fulltext.pdf
first_indexed	2023-09-18T20:07:26Z
last_indexed	2023-09-18T20:07:26Z
_version_	1777407252348534784

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

Similar Items