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Toshiyuki Furutani

Bio: Toshiyuki Furutani is an academic researcher from Osaka City University. The author has contributed to research in topics: Lipase & Triacylglycerol lipase. The author has an hindex of 9, co-authored 15 publications receiving 238 citations.

Papers
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Journal ArticleDOI
TL;DR: In this paper, a screening of suitable enzymes for the desired reaction was carried out, and a higher activity for n-acylation with Lipase Q L was found, but not for the o-acyl compound.

44 citations

Journal ArticleDOI
TL;DR: In this paper, a practical synthesis of methyl (2R,3S)-3-(4methoxyphenyl)glycidate (−)-2a, a key intermediate for diltiazem ( 3 ), was described.

35 citations

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TL;DR: In this article, the authors investigated lipase-catalyzed hydrolysis in water and dioxane-water with a simple colorimetric method and found that most of the lipases showed high activity in water, but some showed activity in 50% Dioxane water several tens times higher than those in water.

34 citations

Journal ArticleDOI
TL;DR: A practical synthesis of methyl (2R,3S)-3-(4-methoxyphenyl)glycidate (-)-2, a key intermediate for diltiazem, was developed and efficiently separated by the use of novel and simple equipment.
Abstract: A practical synthesis of methyl (2R,3S)-3-(4-methoxyphenyl)glycidate (-)-2, a key intermediate for diltiazem (1), was developed. Treatment of methyl (E)-4-methoxycinnamate 3 with chiral dioxirane, generated from chiral ketone 4, provided (-)-2 in 77% ee and 89% yield. The crude mixture of (-)-2 and 4 was efficiently separated by the use of novel and simple equipment performing a lipase-catalyzed transesterification and a continuous dissolution and crystallization to furnish the optically pure (-)-2 and recovery of 4 in 74% and 91% yield, respectively.

31 citations

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TL;DR: Investigation of lipase-catalyzedo-acylations of n -acyl ethanolamines were investigated in organic solvent and Lipase QL proved to be useful for acylation using optically active fatty acid.

26 citations


Cited by
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Journal ArticleDOI
TL;DR: This paper presents results of aalysis experiment conducted at the Dalian Institute of Chemical Physics of Chinese Academy of Sciences (Dalian 116023) and Jingmen Technological College (Jingmen 448000) using gas chromatography for the recovery of Na6(CO3) from Na2SO4.
Abstract: Laboratory for Advanced Materials and New Catalysis, School of Chemistry and Materials Science, Hubei University, Wuhan 430062, China,Laboratory of Natural Gas Utilization and Applied Catalysis, Dalian Institute of Chemical Physics of Chinese Academy of Sciences, Dalian 116023,China, and Jingmen Technological College, Jingmen 448000, ChinaReceived June 30, 2004

864 citations

Journal ArticleDOI
TL;DR: These results suggest that lipases recognize these "well-defined" hydrophobic supports as solid interfaces and they become adsorbed through the external areas of the largeHydrophobic active centers of their "open and hyperactivated structure", which becomes a very promising immobilization method with general application for most lipases.
Abstract: A number of bacterial lipases can be immobilized in a rapid and strong fashion on octyl-agarose gels (e.g., lipases from Candida antarctica, Pseudomonas fluorescens, Rhizomucor miehei, Humicola lanuginosa, Mucor javanicus, and Rhizopus niveus). Adsorption rates in absence of ammonium sulfate are higher than in its presence, opposite to the observation for typical hydrophobic adsorption of proteins. At 10 mM phosphate, adsorption of lipases is fairly selective allowing enzyme purification associated with their reversible immobilization. Interestingly, these immobilized lipase molecules show a dramatic hyperactivation. For example, lipases from R. niveus, M. miehei, and H. lanuginosa were 6-, 7-, and 20-fold more active than the corresponding soluble enzymes when catalyzing the hydrolysis of a fully soluble substrate (0.4 mM p-nitrophenyl propionate). Even higher hyperactivations and interesting changes in stereospecificity were also observed for the hydrolysis of larger soluble chiral esters (e.g. (R,S)-2-hydroxy-4-phenylbutanoic ethyl ester). These results suggest that lipases recognize these "well-defined" hydrophobic supports as solid interfaces and they become adsorbed through the external areas of the large hydrophobic active centers of their "open and hyperactivated structure". This selective interfacial adsorption of lipases becomes a very promising immobilization method with general application for most lipases. Through this method, we are able to combine, via a single and easily performed adsorption step, the purification, the strong immobilization, and a dramatic hyperactivation of lipases acting in the absence of additional interfaces, (e.g., in aqueous medium with soluble substrate). Copyright 1998 John Wiley & Sons, Inc.

510 citations

Journal ArticleDOI
TL;DR: Different approaches for lipase immobilization mainly related to the further use of immobilized derivatives to carry out enantio and regioselective hydrolysis in high water-activity systems are reviewed.

477 citations

Journal ArticleDOI
TL;DR: Ketones with an Attached Chiral Moiety, Chiral Iminium Salt-Catalyzed Epoxidation, and Other Carbohydrate-Based Catalysts 3976 2.8.2.
Abstract: 2.6.4. Other Carbohydrate-Based Catalysts 3976 2.7. Carbocyclic Ketones 3977 2.8. Ketones with an Attached Chiral Moiety 3979 3. Chiral Iminium Salt-Catalyzed Epoxidation 3979 3.

413 citations