Purification of an extracellular D-(-)-3-hydroxybutyrate oligomer hydrolase from Pseudomonas sp. strain A1 and cloning and sequencing of its gene

Journal of Bacteriology

Volumn 179, Issue 1, 1997, Pages 72-77

  Zhang, Kai ^a   Shiraki, Mari ^a   Saito, Terumi ^a  

^a KANAGAWA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

3 HYDROXYBUTYRIC ACID; BACTERIAL ENZYME; HYDROLASE;

ARTICLE; ENZYME ANALYSIS; ENZYME PURIFICATION; GENE EXPRESSION; GENE SEQUENCE; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PSEUDOMONAS;

ALCALIGENES FAECALIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PSEUDOMONAS; PSEUDOMONAS SP.;

EID: 0031037703     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.1.72-77.1997     Document Type: Article

References (29)

1. Brenner, S. 1988. The molecular evolution of genes and proteins: a tale of two serines. Nature (London) 331:528-530.
2. Briese, B. H., B. Schmidt, and D. Jendrossek. 1994. Pseudomonas lemoignei has five poly(hydroxyalkanoic acid) (PHA) depolymerase genes: a comparative study of bacterial and eukaryotic PHA depolymerases. J. Environ. Polymer Degrad. 2:75-87.
3. Brucato, C. L., and S. S. Wang. 1991. Extracellular poly(3-hydroxybutyrate) depolymerase from Penicillium funiculosum:. general characteristics and active site studies. Arch. Bioehem. Biophys. 290:497-502.
4. Chowdhury, A. A. 1963. Poly-β-hydroxybuttersäure abbauende Bakterien unt Exoenzym. Arch. Mikrohiol. 47:169-200.
5. Dartois, V., A. Buulard, K. Schanck, and C. Colsaon. 1992. Cloning, nucleotide sequence and expression in Escherichia coli of a lipase gene from Bacillus subtilis. Biochim. Biophys. Acta 1131:253-260.
6. Dawes, E. A. 1964. Some aspects of the endogenous metabolism of bacteria. Bacteriol, Rev. 28:126-149.
7. Dawes, E. A. 1990, Novel microbial polymers: an introductory overview, p. 3-16, In E. A. Dawes (ed.). Novel biodegradable mierobial polymers, Kluwer Academic Publishers, Dordrecht. The Netherlands.
8. Delafield, F. P., K. E. Cooksey, and M. Doudoroff. 1965. β-Hydroxybutyric dehydrogenase and dimer hydrolase of Pseudomonas lemoignei. J. Biol. Chem. 240:4023-4028.
9. Doudoroff, M. 1966. Metabolism of poly-β-hydroxybutyrate in bacteria, p. 385-400. In N. O. Kaplan and E. P. Kennedy (ed.). Current aspects of biochemical energetics. Academic Press, Inc., New York, N.Y.
10. Jendrossek, D., A. Frisse, A. Behrends, M. Andermann, H. D. Krazin, T. Stanislawski, and H. G. Schlegel. 1995. Biochemical and molecular characterization of the Pseudomonas lemoignei polyhydroxyalkanoate depolymerase system. J. Bacteriol. 177:596-607.
11. Jendrossek, D., I, Knoke, R. B. Habibian, A. Steinbüchel, and H. G. Schlegel. 1993. Degradation of poly(3-hydroxybutyrate), PHB, by bacteria and purification of a novel PHB "depolymerase from Comamonas sp. J. Environ. Polymer Degrad. 1:53-63.
12. King, P. P. 1982. Biotechnology. An industrial view. J. Chem. Tech. Biotechnol. 32:2-8.
13. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
14. Lowry, O. H., N. J. Rosebruugh, A. L. Farr, and R. J. Randall. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265-275.
15. Lusty, C. J., and M. Doudoroff. 1966. Poly-β-hydroxybutyrate depolymerase of Pseudomonas lemoignei. Proc. Natl. Acad. Sci. USA 56:960-965.
16. Merrick, J. M., and C. I. Yu. 1966. Purification and properties of a D(-)β-hydnixybutyric dimer hydrolase from Rhodospirillum rubrum. Biochemistry 4:3563-3568.
17. Saito, H., and K. Miura. 1963. Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim. Biophys. Acta 72:617-629.
18. Saito, I., and G. R. Stark. 1986. Charomids: cosmid vectors for efficient cloning and mapping of large or small restriction fragments. Proc. Natl. Acad. Sci. USA 83:8664-8668.
19. Saito, T., K. Suzuki, J. Yamamoto, T. Fukui, K. Miwa, K. Tomita, S. Nakanishi, S. Oduni, J. Suzuki, and K. Ishikawa. 1989. Cloning, nucleotide sequence, and expression in Escherichia coli of the gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis. J. Bacteriol. 171:184-189.
20. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
21. Schirmer, A. D., and D. Jendrossek. 1994. Molecular characterization of the extracellular poly(3-hydroxyoctanoic acid) [P(3HO)] depolymerase gone of Pseudomonas fluorescens GK13 and of its gene product. J. Bactcriol. 176: 7065-7073.
22. Shirnki, M., T. Shtmada, M, Tatsumichi, and T. Saito. 1995. Purification and characterization of extracellular poly(3-hydroxybutyrate) depolymerases. J. Environ. Polymer Degnid. 3:13-21.
23. Shirakura, Y., T. Fukui, I. Tanio, K. Nakayama, R. Matsuno, and T. Tomita. 1983. An extracellular D(-)-3-hydroxybutyrate oligomer hydrolase from Alcaligenes faecalis. Biochim. Biophys. Acta 784:331-339.
24. Smibert, R. M., and N. R. Krieg. 1994. Phenotypic characterization, p. 650. In P. Gerhardt, R. G. E. Murray, W. A. Wood, and N. R. Krieg (ed.), Methods for general and molecular bacteriology. American Society for Microbiology, Washington, D.C.
25. Tanaka, Y., T. Saito, T. Fukui, T. Tanio, and K. Tomita. 1981. Purification and properties of D(-)-3-hydroxybutyrate-dimer hydrolase from Zoogloea ranimera I-16-M. Eur. J. Biochem. 118:177-182.
26. Tanio, T., T. Fukui, T. Shirakura, T. Saito, K. Tomita, T. Kaiho, and S. Masamune. 1982. An extracellular poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis. Eur. J. Biochem, 124:71-77.
27. Towbin, H., T. Staehelln, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc, Natl. Acad. Sci. USA 76:4350-4354.
28. Upton, C., and J. T. Buckley. 1995. A new family of lipolytic enzymes? Trends Biochem. Sci. Lett. 20:178-179.
29. Yamada, K., K. Mukai, and Y. Doi. 1993. Enzymatic degradation of poly(hydroxyalkanoates) by Pseudomonas pickettii. Int. J. Biol. Macromol. 15: 215-220.