Purification and properties of cephalosporin-C deacetylase from the yeast, Rhodotorula glutinis 38B1, useful for bioconversion of 7- aminocephalosporanic acid derivatives

Journal of Fermentation and Bioengineering

Volumn 85, Issue 1, 1998, Pages 53-57

  Sakai, Yasuyoshi ^a   Abe, Tetsuya ^a   Aoki, Motoi ^a   Ohbayashi, Yohko ^a   Yamamoto, Keizo ^b   Tani, Yoshiki ^a,c   Kato, Nobuo ^a  

^a KYOTO UNIVERSITY   (Japan)

^b ASAHI CHEMICAL INDUSTRY CO   (Japan)

^c NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

7 aminocephalosporanic acid; Cephalosporin C deacetylase; Deacetyl 7 aminocephalosporanic acid; Rhodotorula glutinis

Indexed keywords

AMINO ACIDS; BIOCONVERSION; CHARACTERIZATION; ENZYME KINETICS; PURIFICATION; YEAST;

CEPHALOSPORIN C DEACETYLASE; RHODOTORULA GLUTINIS;

ENZYMES;

7 AMINOCEPHALOSPORANIC ACID; ACYLTRANSFERASE; DEACETYLCEPHALOSPORIN C;

ARTICLE; BIOTRANSFORMATION; CHEMICAL MODIFICATION; DERIVATIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME PURIFICATION; ENZYME SUBSTRATE; GLYCOSYLATION; NONHUMAN; RHODOTORULA; YEAST;

RHODOTORULA GLUTINIS;

EID: 0031933242     PISSN: 0922338X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0922-338X(97)80353-4     Document Type: Article

References (16)

1. Komatsu, K.: Basic and applied aspects of cephalosporin C acylase. Bioscience & Industry, 49, 612-616 (1991). (in Japanese)
2. Isogai, T.: Gene engineering of cephalosporin- and penicillin-producing microorganisms. Bioscience & Industry, 50, 971-978 (1992). (in Japanese)
3. Sakai, Y., Abe, T., Ohbayashi, Y., Isaka, K., Yamamoto, K., Tani, Y., and Kato, N.: Bioconversion of 7-aminocephalosporanic acid by intact Rhodotorula glutinis cells. Appl. Environ. Microbiol., 62, 2669-2672 (1996).
4. Abraham, E.P. and Fawcett, P.: Cephalosporin acetylesterase (citrus). Methods Enzymol., 43, 728-731 (1975).
5. Abbott, B.J. and Fukuda, D.S.: Cephalosporin acetylesterase (Bacillus subtilis). Methods Enzymol., 43, 731-734 (1975).
6. Abbott, B.J. and Fukuda, D.: Physical properties of kinetic behavior of a cephalosporin acetylesterase produced by Bacillus subtilis. Appl. Microbiol., 30, 413-419 (1975).
7. Konecny, J. and Voser, W.: Effects of carrier morphology and buffer diffusion on the expression of enzymatic activity. Biochim. Biophys. Acta, 485, 367-378 (1977).
8. Takimoto, A., Mitsushima, K., Yagi, S., and Sonoyama, T.: Purification, characterization and partial amino acid sequences of a novel cephalosporin-C deacetylase from Bacillus subtilis. J. Ferment. Bioeng., 77, 17-22 (1994).
9. Demain, A.L., Walton, R.B., Newkirk, J.F., and Miller, I.M.: Microbial degradation of cephalosporin C. Nature (London), 199, 909-910 (1963).
10. Fujisawa, Y., Shirafuji, H., and Kanzaki, T.: Deacetyl-cephalosporin C formation by cephalosporin C acetylhydrolase induced in a Cephalosporium acremonium mutant. Agric. Biol. Chem., 39, 1303-1309 (1975).
11. Hinnen, A. and Nuesch, J.: Enzymatic hydrolysis of cephalosporin C by an extracellular acetylhydrolase of Cephalosporium acremonium. Antimicrob. Agents Chemother., 9, 824-830 (1976).
12. Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227, 680-685 (1970).
13. Ochiai, H. and Katagiri, Y.: Gel electrophoresis and gel blot methods, p. 31-40. In Suzuki, S., Yamashina, I., Osawa, T., Kowata, Y., and Nagai, K. (ed.), Shin-Seikagaku Jikken-Koza vol. 3. Tokyo Kagaku Dojin, Tokyo (1990). (in Japanese)
14. Yamamoto, K. and Osawa, T.: Affinity chromatography, p. 3- 29. In Suzuki, S., Yamashina, I., Osawa, T., Kowata, Y., and Nagai, K. (ed.), Shin-Seikagaku Jikken-Koza vol. 3. Tokyo Kagaku Dojin, Tokyo (1990). (in Japanese)
15. Takagi, M.: Isolation of organelles of yeasts and fungi, p. 208-228. In Beppu, T., Nomoto, A., and Ohta, T. (ed.), Shin-Seikagaku Jikken-Koza vol. 17. Tokyo Kagaku Dojin, Tokyo (1992). (in Japanese)
16. Mitsushima, K., Takimoto, A., Sonoyama, T., and Yagi, S.: Gene cloning, nucleotide sequence, and expression of a cephalosporin-C deacetylase from Bacillus subtilis. Appl. Environ. Microbiol., 61, 2224-2229 (1995).