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: | , , , |
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| 格式: | Article |
| 語言: | English |
| 出版: |
Springer
2010
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| 主題: | |
| 在線閱讀: | 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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| 總結: | 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. |
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