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Bioscience, Biotechnology, and Biochemistry Volume 70, 2006 - Issue 12
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Original Articles

Stereoselective Reduction of Carbonyl Compounds Using the Cell-Free Extract of the Earthworm, Lumbricus rubellus, as a Novel Source of Biocatalyst

Kohji ISHIHARADepartment of Life Science, Okayama University of Science
&
Nobuyoshi NAKAJIMAIndustry, Government, and Academic Promotional Center, Regional Cooperative Research Organization, Okayama Prefectural University
Pages 3077-3080 | Received 18 Jul 2006, Accepted 04 Aug 2006, Published online: 22 May 2014

  • 1) Wong, C.-H., and Whitesides, G. M., “Enzymes in Synthetic Organic Chemistry, Tetrahedron Organic Series” Vol. 12, 1st ed., Pergamon, Elsevier, Amsterdam, pp. 41–194 (1994).
  • 2) Sugai, T., Application of enzyme- and microorganism-catalyzed reaction to organic synthesis. Curr. Org. Chem., 3, 373–406 (1999).
  • 3) Ishihara, K., Hamada, H., Hirata, T., and Nakajima, N., Biotransformation using plant cultured cells. J. Mol. Cat. B: Enzymatic, 23, 145–170 (2003).
  • 4) Nakamura, K., Inoue, K., Ushio, K., Oka, S., and Ohno, A., Stereochemical control on yeast reduction of α-keto esters: reduction by immobilized bakers’ yeast in hexane. J. Org. Chem., 53, 2589–2593 (1988).
  • 5) Nakamura, K., Kawai, Y., Nakajima, N., and Ohno, A., Stereochemical control of microbial reduction. 17. Mechanism to control the enantioselectivity in the reduction with bakers’ yeast. J. Org. Chem., 56, 4778–4783 (1991).
  • 6) Wada, M., Kataoka, M., Kawabata, H., Yasohara, Y., Kizaki, N., Hasegawa, J., and Shimizu, S., Purification and characterization of NADPH-dependent carbonyl reductase, involved in stereoselective reduction of ethyl 4-chloro-3-oxobutanoate, from Candida magnoliae. Biosci. Biotechnol. Biochem., 62, 280–285 (1998).
  • 7) Ishihara, K., Iwai, K., Yamaguchi, H., Nakajima, N., Nakamura, K., and Ohshima, T., Stereoselective reduction of α- and β-keto esters with aerobic thermophiles, Bacillus strains. Biosci. Biotechnol. Biochem., 60, 1896–1898 (1996).
  • 8) Ishihara, K., Nishitani, M., Yamaguchi, H., Nakajima, N., Ohshima, T., and Nakamura, K., Preparation of optically active α-hydroxy esters: stereoselective reduction of α-keto esters using thermophilic actinomycetes. J. Ferment. Bioeng., 84, 268–270 (1997).
  • 9) Ishihara, K., Yamaguchi, H., Nakajima, N., and Nakamura, K., Stereocontrolled reduction of α-keto esters with thermophilic actinomycete, Streptomyces thermocyaneoviolaceus IFO 14271. J. Mol. Cat. B: Enzymatic, 10, 429–434 (2000).
  • 10) Ishihara, K., Yamaguchi, H., Adachi, N., Hamada, H., and Nakajima, N., Stereocontrolled reduction of α- and β-keto esters with micro green algae, Chlorella strains. Biosci. Biotechnol. Biochem., 64, 2099–2103 (2000).
  • 11) Keiline, D. Q., On the pharyngeal or salivary gland of the earthworm. J. Microsc. Sci., 65, 33–61 (1920).
  • 12) Tanaka, B., and Nakata, S., Studies of antipyretic components in the Japanese earthworm. Tokyo Igaku Zasshi (in Japanese) 29, 67–97 (1974).
  • 13) Mishra, P. C., and Dash, M. C., Digestive enzymes of some earthworms. Experientia, 36, 1156–1157 (1980).
  • 14) Nakajima, N., Mihara, H., and Sumi, H., Characterization of potent fibrinolytic enzymes in earthworm Lumbricus rubellus. Biosci. Biotechnol. Biochem., 57, 1726–1730 (1993).
  • 15) Nakajima, N., Sugimoto, M., and Ishihara, K., Earthworm-serine protease: characterization, molecular cloning, and application of the catalytic functions. J. Mol. Cat. B: Enzymatic, 23, 191–212 (2003).
  • 16) Sigimoto, M., Ishihara, K., and Nakajima, N., Structure and function of an isozyme of earthworm proteases as a new biocatalyst. J. Mol. Cat. B: Enzymatic, 23, 405–409 (2003).
  • 17) Nakajima, N., Sugimoto, M., Tsuboi, S., Tsuji, H., and Ishihara, K., An isozyme of earthworm serine proteases acts on hydrolysis of triacylglycerol. Biosci. Biotechnol. Biochem., 69, 2009–2011 (2005).
  • 18) Nakamura, K., Kondo, S., Kawai, Y., Nakajima, N., and Ohno, A., Purification and characterization of α-keto ester reductases from bakers’ yeast. Biosci. Biotechnol. Biochem., 58, 2236–2240 (1994).
  • 19) Ushio, K., Yamauchi, S., and Masuda, K., Preparation of enantiomerically pure (S)-2-hydroxy heptanoate via bakers’ yeast catalyzed hydrolytic resolution. Biotechnol. Lett., 13, 495–500 (1991).

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