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 enzymatic activities w...
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| Format: | Article |
| Language: | English |
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Springer
2010
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| Online Access: | http://psasir.upm.edu.my/id/eprint/15715/ http://psasir.upm.edu.my/id/eprint/15715/1/Molten%20globule.pdf |
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| 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 |
| building | UPM Institutional Repository |
| collection | Online Access |
| 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 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. |
| first_indexed | 2025-11-15T08:04:11Z |
| format | Article |
| id | upm-15715 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T08:04:11Z |
| publishDate | 2010 |
| publisher | Springer |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-157152016-09-26T07:23:57Z http://psasir.upm.edu.my/id/eprint/15715/ Molten globule-triggered inactivation of a thermostable and solvent stable lipase in hydrophilic solvents Tengku Abdul Hamid, Tengku Haziyamin Raja Abdul Rahman, Raja Noor Zaliha Salleh, Abu Bakar Basri, Mahiran 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. Springer 2010 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/15715/1/Molten%20globule.pdf 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 http://link.springer.com/article/10.1007/s10930-010-9251-7?view=classic 10.1007/s10930-010-9251-7 |
| spellingShingle | Tengku Abdul Hamid, Tengku Haziyamin Raja Abdul Rahman, Raja Noor Zaliha Salleh, Abu Bakar Basri, Mahiran Molten globule-triggered inactivation of a thermostable and solvent stable lipase in hydrophilic solvents |
| title | 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_short | 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 |
| url | http://psasir.upm.edu.my/id/eprint/15715/ http://psasir.upm.edu.my/id/eprint/15715/ http://psasir.upm.edu.my/id/eprint/15715/ http://psasir.upm.edu.my/id/eprint/15715/1/Molten%20globule.pdf |