The role of lid in protein-solvent interaction of the simulated solvent stable thermostable lipase from bacillus strain 42 in water-solvent mixtures

Lip 42 lipase, isolated from Bacillus sp. strain 42 was previously shown to be stable in polar organic solvent such as dimethyl sulfoxide (DMSO). Stabilities in different solvent compositions were studied based on 400C pre incubation in solvent, and the purified lipase was shown to retain at least 1...

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Main Authors: Tengku Abdul Hamid, Tengku Haziyamin, Raja Abdul Rahman, Raja Noor Zaliha, Salleh, Abu Bakar, Basri, Mahiran
Format: Article
Language:English
Published: Diagnosis Press 2009
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spelling my.iium.irep.3072011-09-05T03:38:14Z http://irep.iium.edu.my/307/ The role of lid in protein-solvent interaction of the simulated solvent stable thermostable lipase from bacillus strain 42 in water-solvent mixtures Tengku Abdul Hamid, Tengku Haziyamin Raja Abdul Rahman, Raja Noor Zaliha Salleh, Abu Bakar Basri, Mahiran Q Science (General) Lip 42 lipase, isolated from Bacillus sp. strain 42 was previously shown to be stable in polar organic solvent such as dimethyl sulfoxide (DMSO). Stabilities in different solvent compositions were studied based on 400C pre incubation in solvent, and the purified lipase was shown to retain at least 100% residual activity in up to 45% v/v DMSO. In 60% v/v DMSO, 68% of residual activity was retained, however, this dramatically reduced to 6.5% at 65% v/v DMSO. Activity enhancements were recorded at lower solvent compositions (less than 45% v/v solvent), whereby, at 30% v/v DMSO, enhancement was as much as 35%. Based on these solvent stability profile, molecular dynamic simulations were then carried out in the presence of water, 60% v/v DMSO + 40% v/v water and 100% v/v DMSO, by using a structure predicted from a highly homologous (97%) lipase (PDB:1JI3). Results showed that the flexibility changes in the helix-loop-helix motif covering catalytic triad were found to be associated with a hydrophobic cluster region. The presence of 60% v/v DMSO resulted in the disorganization of the cluster, accompanied with nonnative H-bonds formations. The cluster was retained in 100% v/v DMSO which resembled to that of water simulation. Mutant form of Lip 42, V171S contained residue substitution in the cluster and within helix-loop-helix motif. At 50C pre-incubation, the mutant lost as much of the high temperature enhancements observed in low DMSO compositions. This indicated the potential role of hydrophobic residues in helix-loop-helix motif and the cluster in interfacial activation. Diagnosis Press 2009 Article REM application/pdf en http://irep.iium.edu.my/307/1/1524-1530.pdf Tengku Abdul Hamid, Tengku Haziyamin and Raja Abdul Rahman, Raja Noor Zaliha and Salleh, Abu Bakar and Basri, Mahiran (2009) The role of lid in protein-solvent interaction of the simulated solvent stable thermostable lipase from bacillus strain 42 in water-solvent mixtures. Biotechnology & Biotechnological Equipment, 23 (4). pp. 1524-1530. ISSN 1310-2818 http://www.diagnosisp.com/dp/journals/issue.php?journal_id=1&archive=0&issue_id=25 10.2478/v10133-009-0015-5
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)
spellingShingle Q Science (General)
Tengku Abdul Hamid, Tengku Haziyamin
Raja Abdul Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
Basri, Mahiran
The role of lid in protein-solvent interaction of the simulated solvent stable thermostable lipase from bacillus strain 42 in water-solvent mixtures
description Lip 42 lipase, isolated from Bacillus sp. strain 42 was previously shown to be stable in polar organic solvent such as dimethyl sulfoxide (DMSO). Stabilities in different solvent compositions were studied based on 400C pre incubation in solvent, and the purified lipase was shown to retain at least 100% residual activity in up to 45% v/v DMSO. In 60% v/v DMSO, 68% of residual activity was retained, however, this dramatically reduced to 6.5% at 65% v/v DMSO. Activity enhancements were recorded at lower solvent compositions (less than 45% v/v solvent), whereby, at 30% v/v DMSO, enhancement was as much as 35%. Based on these solvent stability profile, molecular dynamic simulations were then carried out in the presence of water, 60% v/v DMSO + 40% v/v water and 100% v/v DMSO, by using a structure predicted from a highly homologous (97%) lipase (PDB:1JI3). Results showed that the flexibility changes in the helix-loop-helix motif covering catalytic triad were found to be associated with a hydrophobic cluster region. The presence of 60% v/v DMSO resulted in the disorganization of the cluster, accompanied with nonnative H-bonds formations. The cluster was retained in 100% v/v DMSO which resembled to that of water simulation. Mutant form of Lip 42, V171S contained residue substitution in the cluster and within helix-loop-helix motif. At 50C pre-incubation, the mutant lost as much of the high temperature enhancements observed in low DMSO compositions. This indicated the potential role of hydrophobic residues in helix-loop-helix motif and the cluster in interfacial activation.
format Article
author Tengku Abdul Hamid, Tengku Haziyamin
Raja Abdul Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
Basri, Mahiran
author_facet Tengku Abdul Hamid, Tengku Haziyamin
Raja Abdul Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
Basri, Mahiran
author_sort Tengku Abdul Hamid, Tengku Haziyamin
title The role of lid in protein-solvent interaction of the simulated solvent stable thermostable lipase from bacillus strain 42 in water-solvent mixtures
title_short The role of lid in protein-solvent interaction of the simulated solvent stable thermostable lipase from bacillus strain 42 in water-solvent mixtures
title_full The role of lid in protein-solvent interaction of the simulated solvent stable thermostable lipase from bacillus strain 42 in water-solvent mixtures
title_fullStr The role of lid in protein-solvent interaction of the simulated solvent stable thermostable lipase from bacillus strain 42 in water-solvent mixtures
title_full_unstemmed The role of lid in protein-solvent interaction of the simulated solvent stable thermostable lipase from bacillus strain 42 in water-solvent mixtures
title_sort role of lid in protein-solvent interaction of the simulated solvent stable thermostable lipase from bacillus strain 42 in water-solvent mixtures
publisher Diagnosis Press
publishDate 2009
url http://irep.iium.edu.my/307/1/1524-1530.pdf
http://irep.iium.edu.my/307/
http://www.diagnosisp.com/dp/journals/issue.php?journal_id=1&archive=0&issue_id=25
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score 13.144533