Effect of dimethylsulfoxide on hydrolysis of lipase

To establish an industrially feasible reaction process, the effect of dimethylsulfoxide (DMSO) added to an aqueous solution on the hydrolysis of lipase was investigated using fluorescent substrates. Several Upases from microorganisms were improved in their hydrolysis activities against 4-methylumbel...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2001-09, Vol.65 (9), p.2078-2082
Main Authors: Tsuzuki, W. (National Food Research Inst., Tsukuba, Ibaraki (Japan)), Ue, A, Kitamura, Y
Format: Article
Language:English
Subjects:
Animals
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Dimethyl Sulfoxide - chemistry
dimethylsulfoxide
Fluorometry - methods
Fundamental and applied biological sciences. Psychology
HYDROLYSIS
Kinetics
lipase
Lipase - chemistry
Lipase - metabolism
Methods. Procedures. Technologies
Pancreas - enzymology
Pseudomonas fluorescens - enzymology
Solubility
Solvents - chemistry
TRIACYLGLYCEROL LIPASE
Tryptophan - analysis
Tryptophan - chemistry
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Summary:To establish an industrially feasible reaction process, the effect of dimethylsulfoxide (DMSO) added to an aqueous solution on the hydrolysis of lipase was investigated using fluorescent substrates. Several Upases from microorganisms were improved in their hydrolysis activities against 4-methylumbelliferyl oleate by DMSO. Variation was found in the effect of DMSO depending on the species of lipase. After the high stability of the lipase from Pseudomonasfluorescens in DMSO solution was confirmed, hydrolysis by this lipase of four acy1-4-methylumbelliferones was studied kinetically at different DMSO concentrations. DMSO added to an aqueous solution increased the V submax of this lipase for a substrate with strong hydrophobicity, and decreased that value for a substrate with an opposite property. On the other hand, DMSO had a very small effect on K subm for each substrate. A fluorometric study suggested that DMSO induced a change of the chemical environment that surrounded tryptophan residues of the lipase. Such conformational change would be one of the causes of the DMSO-induced alteration of its reactive property. These results suggest that the addition of DMSO may be a novel method of 'solvent engineering' of this enzyme.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.65.2078