Preparation of an optically pure secondary alcohol of synthetic pyrethroids using microbial lipases

Mitsuda, Satoshi; Umemura, Takeaki; Hirohara, Hideo

doi:10.1007/bf00265812

Cited by 46 publications

(15 citation statements)

References 17 publications

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“…The hydrolysis rate increased with chain length from t-butyl hexanoate (nϭ4) to TBO (nϭ6), but decreased with further increases in chain length, indicating that the hydrolytic activity was dependent on the acyl chain length of the substrate, and C 8 acid moiety gave the highest activity. Similar behaviors were reported for the hydrolysis of esters of 4-hydroxy-3-methyl-2-(2-propynyl)-cyclopent-2-enone (HMPC) (Mitsuda et al, 1988) and dl-3-chloro-2-methyl propanol (Lavayre et al, 1982) using microbial or pancreatic lipases. To our knowledge, this is the first report of microorganism-producing lipase which uses t-butyl esters as the substrate.…”

Section: Substrate Specificitysupporting

confidence: 72%

“…Many different kinds of microbial lipases have been reported, and they have received much attention because of their potential use in industry (Björkling et al, 1991;Harwood, 1989). However, the known lipases scarcely hydrolyze esters containing a bulky alcohol moiety, such as tertiary-alcohol esters, although primary-alcohol esters (Amaya et al, 1995;Linko et al, 1995;Zaidi et al, 1995) and secondary-alcohol esters (Iwai et al, 1980;Mitsuda et al, 1988) are good substrates for lipases. This lack of ability to hydrolyze bulky alcohol esters hindered the wide use of lipases for complex compounds.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Screening and identification of a novel lipase from Burkholderia sp. YY62 which hydrolyzes t-butyl esters effectively.

Yeo

Nihira

Yamada

1998

J. Gen. Appl. Microbiol.

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Lipases (EC 3.1.1.3, glycerol ester hydrolase) catalyze the hydrolysis of triacylglycerols to glycerol and free fatty acids. Recently, a variety of new applications of lipase have emerged, especially in enantioselective hydrolysis of esters (Nakano et al., 1994;Tsai and Wei, 1994;Waagen et al., 1994;Wu et al., 1990), ester synthesis in organic solvents (Anderson and Callahan, 1960;Armstrong et al., 1988;Bornscheuer, 1995;Klibanov, 1989;Loffet et al., 1989;Makita et al., 1987;Turner and Winterman, 1995) and in modification of sugars or chiral drugs (Bornemann et al., 1992;Margolin, 1993;Patil et al., 1991). Many different kinds of microbial lipases have been reported, and they have received much attention because of their potential use in industry (Björkling et al., 1991;Harwood, 1989). However, the known lipases scarcely hydrolyze esters containing a bulky alcohol moiety, such as tertiary-alcohol esters, although primary-alcohol esters (Amaya et al., 1995;Linko et al., 1995;Zaidi et al., 1995) and secondary-alcohol esters (Iwai et al., 1980;Mitsuda et al., 1988) are good substrates for lipases. This lack of ability to hydrolyze bulky alcohol esters hindered the wide use of lipases for complex compounds. Therefore, we started to obtain a lipase that hydrolyzes t-butyl octanoate (TBO) as a model substrate for bulky esters, and isolated a microorganism that produces a new type lipase from soil samples. In this report, we describe the primary characterization of this lipase and taxonomic identification of the producer. Materials and Methods Preparation of t-butyl esters.The t-butyl alcohol esters used in this work were prepared from t-butyl alcohol and corresponding acid chlorides. The typical protocol for the synthesis of TBO is described below. Octanoyl chloride (48 g, 0.3 M) was added dropwise to a mixture of 2-methyl-2-propanol (80 g, 1.08 M), anhydrous pyridine (25.6 g, 0.32 M), and 4-dimethyl aminopyridine (1 g, 8.2 mM) in 800 ml of hexane at 0-5°C for 2 h. After 14 h reaction at room temperature, water (400 ml) was added to the mixture and the hexane layer was separated. The hexane solution was washed with water, 1 N HCl solution and sodium carbonate solution. The hexane layer was separated, washed with water, dried over sodium sulfate and concentrated under reduced pressure to yield 39.3 g (65.5%) of oil.

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Section: Substrate Specificitysupporting

confidence: 72%

mentioning

confidence: 99%

Screening and identification of a novel lipase from Burkholderia sp. YY62 which hydrolyzes t-butyl esters effectively.

Yeo

Nihira

Yamada

1998

J. Gen. Appl. Microbiol.

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“…Lipases constitute an important class of high selectivity and stereo-specificity industrial enzymes and are currently used in a wide variety of applications: bio-transformation of fats and oils, polymer synthesis and preparation of esters for food, for cosmetic industry and for diesel engine fuels (biodiesel ester) as well as for the production of optically pure compounds for the pharmaceutical industry [1][2][3][4][5][6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Hydrolysis of Alkyl Ester on Lipase/Silicalite-1 Catalyst

et al. 2007

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Pure silica zeolites have been prepared in powder and pellets form with different surface chemical properties in order to investigate how the binding forces in the lipase enzyme adsorption influence the final conformation of the immobilized enzyme and its catalytic activity. The catalytic activity of the adsorbed lipase have been tested in the alkyl esters hydrolysis reaction. The higher alkyl-esters conversion is observed for the lipase immobilized on the supports prepared in OH -media compared to the fluoride media supports. The obtained results can be explained by the two different non-covalent interactions between the external surface of zeolites and the enzyme.

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“…They found that P. fluorescens lipase yielded the highest reaction rate. By combining methods of enzymatic resolution with a chemical inversion of the (R)-alcohol, Mitsuda et al [112,113,114,115] also developed an efficient process for the total conversion of racemic 4-hydroxy-3-methyl-2-(2-propynyl)-cyclopent-2-enone (HM PC) to the (S)-form, which is an important intermediate in the preparation of insecticidally active synthetic pyre-throids. The enzyme involved was a lipase from a microbial source.…”

Section: Insecticidesmentioning

confidence: 98%