Polar Organic Solvent Added to an Aqueous Solution Changes Hydrolytic Property of Lipase

Tsuzuki, Wakako; Ue, Akemi; Nagao, Akihiko

doi:10.1271/bbb.67.1660

Cited by 41 publications

(27 citation statements)

References 23 publications

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“…Therefore, the water content and hydrophobicity (Log P) of organic solvent have a dramatic influence on the properties of enzymes. It was revealed that there was an optimum water content (~10% w/w) for enzyme properties, at which the enzyme properties are similar to the ones found in pure water [24]. At lower water content, the enzyme is very rigid; while at higher water content the enzyme starts to unfold.…”

Section: Effect Of Log P Value Of Organic Solventmentioning

confidence: 80%

“…For instance, the Rhizomucor miehei lipase (ROL) activity decreases from 100% to 0% with the increase of alcohol concentration, and the decreasing rate increases with the increase of carbon chain length from methanol to butanol [24]. The activity inhibition of ROL might stemmed from the fact that the OH group acted as a product inhibitor, competing with that of the substrate in the case of the hydrolytic reaction [24]. Similarly, the papain showed 60% and 20% of its original activity in 90% and 99% v/v methanol aqueous solution.…”

Section: Effect Of the Functional Groups Of Organic Solventmentioning

confidence: 99%

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Enzyme Stability and Activity in Non-Aqueous Reaction Systems: A Mini Review

et al. 2016

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Abstract:Enormous interest in biocatalysis in non-aqueous phase has recently been triggered due to the merits of good enantioselectivity, reverse thermodynamic equilibrium, and no water-dependent side reactions. It has been demonstrated that enzyme has high activity and stability in non-aqueous media, and the variation of enzyme activity is attributed to its conformational modifications. This review comprehensively addresses the stability and activity of the intact enzymes in various non-aqueous systems, such as organic solvents, ionic liquids, sub-/super-critical fluids and their combined mixtures. It has been revealed that critical factors such as Log P, functional groups and the molecular structures of the solvents define the microenvironment surrounding the enzyme molecule and affect enzyme tertiary and secondary structure, influencing enzyme catalytic properties. Therefore, it is of high importance for biocatalysis in non-aqueous media to elucidate the links between the microenvironment surrounding enzyme surface and its stability and activity. In fact, a better understanding of the correlation between different non-aqueous environments and enzyme structure, stability and activity can contribute to identifying the most suitable reaction medium for a given biotransformation.

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Section: Effect Of Log P Value Of Organic Solventmentioning

confidence: 80%

Section: Effect Of the Functional Groups Of Organic Solventmentioning

confidence: 99%

Enzyme Stability and Activity in Non-Aqueous Reaction Systems: A Mini Review

et al. 2016

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“…The resulting supernatant was used as the enzyme solution (Takano et al, 1986). Lipase activity was assayed by fluorometry (Tsuzuki et al, 2003). The increase in 4-methylumbelliferone (4MU), caused by enzymatic hydrolysis of 4-methylumbelliferyl palmitate (4MUP), was measured by fluorescence intensity at 450 nm (excitation at 320 nm) using a Shimadzu RF-5300PC fluorescence spectrophotometer.…”

Section: Methodsmentioning

confidence: 99%

Effect of Superheated Steam Treatment on Enzymes Related to Lipid Oxidation of Brown Rice

Satou

Takahashi

Yoshii

2010

FSTR

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When brown rice is preserved for a long period of time, a stale flavor (komai-shu) develops as a result of lipid oxidation by enzymes. In order to inactivate the enzymes, brown rice was treated with superheated steam. Superheated steam treatment for about 1 min, at all temperatures, caused a decrease in the enzymatic activity related lipid oxidation. On the other hand, the degree of starch damage did not increase during superheated steam treatment below 150℃. These results show that superheated steam treatment at a low temperature and for a short time is enough to inactivate the enzyme in brown rice, and does not influence starch quality. It was expected that enzyme inactivation by superheated steam treatment would be effective in suppressing the generation of stale flavor during long preservation periods.

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“…These changes are due to the disturbance of the hydrophobic interaction which would involve a change of conformation [20]. Moreover, alcohols with the long side chains have a stronger inhibitory effect on hydrolysis by enzyme than those with short side chains [21]. The increase in the hydrocarbon chain involves an increase in the denaturing ability of alcohol [22] In this paper, our objective was to develop new approaches to facilitate production of only intermediate peptides after peptic hydrolysis of bovine hemoglobin.…”

Section: Introductionmentioning

confidence: 99%