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Volumn 62, Issue 8, 1998, Pages 1589-1591

Glycolaldehyde production from ethylene glycol with immobilized alcohol oxidase and catalase

Author keywords

Alcohol oxidase; Catalase; Ethylene glycol; Glycolaldehyde; Immobilized enzyme

Indexed keywords


EID: 0346685216     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.62.1589     Document Type: Article
Times cited : (8)

References (12)
  • 1
    • 85009619939 scopus 로고
    • Japan Kokai Tokkyo Koho, 8669740
    • Kitagawa, S., Yokoi, T., and Minafuji, M., Japan Kokai Tokkyo Koho, 8669740 (Apr. 10, 1986).
    • (1986) , pp. 10
    • Kitagawa, S.1    Yokoi, T.2    Minafuji, M.3
  • 2
    • 85009610558 scopus 로고
    • Japan Kokai Tokkyo Koho, 8745548
    • Honda, T. and Terada, K., Japan Kokai Tokkyo Koho, 8745548 (Feb. 27, 1987).
    • (1987)
    • Honda, T.1    Terada, K.2
  • 3
    • 85009610494 scopus 로고
    • Japan Kokai Tokkyo Koho, 91279342
    • Seto, T., Odagiri, M., and Imanari, M., Japan Kokai Tokkyo Koho, 91279342 (Dec. 10, 1991).
    • (1991)
    • Seto, T.1    Odagiri, M.2    Imanari, M.3
  • 4
    • 5544247619 scopus 로고    scopus 로고
    • Effect of a small amount of oxygen on a life of Cu-Zn catalyst in the formation of glycolaldéhyde from ethylene glycol
    • (in Japanese)
    • Seto, T. and Imanari, M., Effect of a small amount of oxygen on a life of Cu-Zn catalyst in the formation of glycolaldéhyde from ethylene glycol. Nippon Kagaku Kaishi (in Japanese), 615-620 (1997).
    • (1997) Nippon Kagaku Kaishi , pp. 615-620
    • Seto, T.1    Imanari, M.2
  • 5
    • 0029635958 scopus 로고
    • A new enzymatic method for glycolaldéhyde production from ethylene glycol
    • Isobe, K. and Nishise, H., A new enzymatic method for glycolaldéhyde production from ethylene glycol. J. Mol. Catalysis B: Enzymatic, 1, 37-43 (1995).
    • (1995) J. Mol. Catalysis B: Enzymatic , vol.1 , pp. 37-43
    • Isobe, K.1    Nishise, H.2
  • 6
    • 0003099824 scopus 로고
    • Enzymes
    • Bergmeyer, H. U., VCH Verlagsgesellschaft, Weinheim
    • Bergmeyer, H. U., Grassl, L., and Walter, H.-E., Enzymes. In”Methods of Enzymatic Analysis, Volume II”, ed. Bergmeyer, H. U., VCH Verlagsgesellschaft, Weinheim, pp. 126-328 (1983).
    • (1983) Methods of Enzymatic Analysis , vol.2 , pp. 126-328
    • Bergmeyer, H.U.1    Grassl, L.2    Walter, H.-E.3
  • 7
    • 0000534915 scopus 로고
    • Continuous production of maltose using dual immobilized enzyme system
    • Yoshida, M., Oishi, K., Kimura, T., Ogata, M., and Nakakuni, T., Continuous production of maltose using dual immobilized enzyme system. Agric. Biol. Chem., 53, 3139-3142 (1989).
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 3139-3142
    • Yoshida, M.1    Oishi, K.2    Kimura, T.3    Ogata, M.4    Nakakuni, T.5
  • 8
    • 0003049911 scopus 로고
    • The microbial metabolism of methanol. Part I. Formation and crystallization of methanol-oxidizing enzyme in a methanol-utilizing yeast
    • sp. No. 2201
    • Tani, Y., Miya, T., Nishikawa, H., and Ogata, K., The microbial metabolism of methanol. Part I. Formation and crystallization of methanol-oxidizing enzyme in a methanol-utilizing yeast, Kloeckera sp. No. 2201. Agric. Biol. Chem., 36, 68-75 (1972).
    • (1972) Kloeckera , vol.36 , pp. 68-75
    • Tani, Y.1    Miya, T.2    Nishikawa, H.3    Ogata, K.4
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0031305769 scopus 로고    scopus 로고
    • Inactivation of Cu, Zn-superoxide dismutase by intermediates of Maillard reaction and glycolytic pathway and some sugars
    • Ukeda, H., Hasegawa, Y., Ishii, T., and Sawamura, M., Inactivation of Cu, Zn-superoxide dismutase by intermediates of Maillard reaction and glycolytic pathway and some sugars. Biosci. Biotech. Biochem., 61, 2039-2042 (1997).
    • (1997) Biosci. Biotech. Biochem. , vol.61 , pp. 2039-2042
    • Ukeda, H.1    Hasegawa, Y.2    Ishii, T.3    Sawamura, M.4
  • 11
    • 0028934990 scopus 로고
    • Mechanism of protein modification by glyoxal and glycolaldéhyde, reactive intermediates of the Maillard reaction
    • Glomb, M. A. and Monnier, V. M., Mechanism of protein modification by glyoxal and glycolaldéhyde, reactive intermediates of the Maillard reaction. J. Biol. Chem., 270, 10017-10026 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 10017-10026
    • Glomb, M.A.1    Monnier, V.M.2
  • 12
    • 0023664488 scopus 로고
    • Effect of phosphate on the kinetics and specificity of glycation of protein
    • Watkins, N. G., Neglia-Fisher, C. I., Dyer, D. G., Thorpe, S. R., and Baynes, J. W., Effect of phosphate on the kinetics and specificity of glycation of protein. J. Biol. Chem., 262, 7207-7212 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 7207-7212
    • Watkins, N.G.1    Neglia-Fisher, C.I.2    Dyer, D.G.3    Thorpe, S.R.4    Baynes, J.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.