Molten Globule-Triggered Inactivation of a Thermostable and Solvent Stable Lipase in Hydrophilic Solvents |
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Authors: | Tengku Haziyamin Tengku Abdul Hamid Raja Noor Zaliha Raja Abd Rahman Abu Bakar Salleh Mahiran Basri |
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Institution: | (1) Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, University Putra Malaysia, 43400 Serdang, Selangor, Malaysia;(2) Department of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, University Putra Malaysia, 43400 Serdang, Selangor, Malaysia;(3) Department of Chemistry, Faculty of Science, University Putra Malaysia, 43400 Serdang, Selangor, Malaysia; |
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Abstract: | 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. |
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