Purification and characterization of trehalose phosphorylase from catellatospora ferruginea

Bioscience, Biotechnology and Biochemistry

Volumn 62, Issue 4, 1998, Pages 782-787

  Aisaka, Kazuo ^a   Masuda, Tomomi ^a   Chikamune, Tadashi ^a   Kamitori, Kazuyo ^a,b  

^a KYOWA HAKKO KOGYO CO LTD   (Japan)

^b NATIONAL INSTITUTE OF NEUROSCIENCE   (Japan)

Author keywords

Catellatospora ferruqinea; Disaccharide; Phosphorylase; Trehalose phosphorylase

Indexed keywords

ALPHA,ALPHA TREHALOSE PHOSPHORYLASE; ALPHA,ALPHA-TREHALOSE PHOSPHORYLASE; CATION; FUNGAL PROTEIN; GLUCOSYLTRANSFERASE;

ACTINOMYCETACEAE; AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; CULTURE MEDIUM; ENZYME SPECIFICITY; ENZYMOLOGY; ISOELECTRIC FOCUSING; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; MOLECULAR WEIGHT; PH; TEMPERATURE;

ACTINOMYCETACEAE; AMINO ACID SEQUENCE; CATIONS; CULTURE MEDIA; FUNGAL PROTEINS; GLUCOSYLTRANSFERASES; HYDROGEN-ION CONCENTRATION; ISOELECTRIC FOCUSING; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 0032039313     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.62.782     Document Type: Article

References (26)

1. C. Colaco, S. Sen, M. Thangavelu, S. Pinder, and B. Roser, Bio/Technology, 10, 1007-1011 (1992).
2. B. Roser, Trends Food Sci. Technol., 2, 161-184 (1991).
3. S. L. Haynie and G. M. Whitesides, Appl. Biochem. Biotech., 23, 155-170 (1990).
4. K. Murata, T. Nakada, M. Kubota, H. Chaen, T. Sugimoto, M. Kurimoto, and Y. Tsujisaka, Biosci. Biotech. Biochem., 59, 1829-1834 (1995).
5. M. Kato, Y. Miura, M. Kettoku, K. Shindo, A. Iwamatsu, and K. Kobayashi, Biosci. Biotech. Biochem., 60, 546-550 (1996).
6. S. Murao, H. Nagano, S. Ogura, and T. Nishino, Agric. Biol. Chem., 49, 2113-2118 (1985).
7. I. Schick, J. Fleckenstein, H. Weber, and K. D. Kulbe, Proceedings of the International Symposium Biochem. Engineering, pp. 126-129 (1991).
8. E. Belocopitow and L. R. Marechal, Biochim. Biophys. Acta, 198, 151-154 (1970).
9. Y. Kitamoto, H. Akashi, H. Tanaka, and N. Mori, FEMS Microbiol. Lett., 55, 147-150 (1988).
10. S. O. Salminen and J. G. Streeter, Plant Physiol., 81, 538-541 (1986).
11. H. Kizawa, K. Miyagawa, and Y. Sugiyama, Biosci. Biotech. Biochem., 59, 1908-1912 (1995).
12. L. R. Marechal and E. Belocopitow, J. Biol. Chem., 247, 3223-3228 (1972).
13. K. Aisaka and T. Masuda, FEMS Microbiol. Lett., 131, 47-51 (1995).
14. M. M. Bradford, Anal. Biochem., 72, 248-254 (1976).
15. U. K. Laemmli, Nature, 227, 680-685 (1970).
16. M. Doudoroff, in “The Enzymes,” vol. 5, 2nd Ed. ed. by P. D. Boyer, H. Lardy, and K. Myrback, Academic Press, New York, 1961, pp. 229-236.
17. E. J. Vandamme, J. V. Loo, L. Machtelinckx, and A. de Laporte, Adv. Appl. Microbiol., 32, 163-201 (1987).
18. A. Kamogawa, K. Yokobayashi, and T. Fukui, Agric. Biol. Chem., 37, 2813-2819 (1973).
19. K. Aisaka, T. Masuda, and T. Chikamune, J. Ferment. Bioeng., 82, 171-173 (1996).
20. M. Kitaoka, T. Sasaki, and H. Taniguchi, Biosci. Biotech. Biochem., 56, 652-655 (1992).
21. K. Tanaka, T. Kawaguchi, Y. Imada, T. Ooi, and M. Arai, J. Ferment. Bioeng., 79, 212-216 (1995).
22. S. H. Goldemberg, L. R. Marechal, and B. C. DeSouza, J. Biol. Chem., 241, 45-50 (1966).
23. M. Kitaoka, T. Sasaki, and H. Taniguchi, Arch. Biochem. Biophys., 304, 508-514 (1993).
24. Z. Selinger and M. Schramm, J. Biol. Chem., 236, 2183-2185 (1961).
25. K. Morgan and W. J. Whelan, Nature, 196, 168-169 (1962).
26. J. K. Alexander, Arch. Biochem. Biophys., 123, 240-246 (1968).