Purification and characterization of thermostable pectate lyase with protopectinase activity from thermophilic bacillus sp. TS 47

Bioscience, Biotechnology and Biochemistry

Volumn 64, Issue 11, 2000, Pages 2360-2367

  Takao, Makoto ^a   Nakaniwa, Tetsuko ^a   Yoshikawa, Kentaro ^a   Terashita, Takao ^a   Sakai, Takuo ^a  

^a KINKI UNIVERSITY   (Japan)

Author keywords

Bacillus; Pectate lyase; Thermophili; Thermostable enzyme

Indexed keywords

GLYCOSIDASE; METAL; PECTATE LYASE; POLYGALACTURONASE; POLYSACCHARIDE LYASE;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS; CHEMISTRY; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; PH; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; TEMPERATURE;

AMINO ACID SEQUENCE; BACILLUS; ENZYME STABILITY; GLYCOSIDE HYDROLASES; HYDROGEN-ION CONCENTRATION; METALS; MOLECULAR SEQUENCE DATA; POLYSACCHARIDE-LYASES; SEQUENCE ANALYSIS, PROTEIN; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 0034328744     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.64.2360     Document Type: Article

References (32)

1. Brinton, C. S., Wichmann, H. J., Willaman, J. J., Wilson, C. P., and Dore, W. H., Definitions written by the committee on nomenclature of pectin of the agriculture-food division. J. Am. Chem. Soc., 49, 37-39 (1927).
2. Sakai, T., Protopectinase from yeasts and a yeastlike fungus. In “Methods in Enzymology”, eds. Wood, W. A. and Kellogg, S. T., Academic Press, San Diego, 161, pp. 335-350 (1988).
3. Sakai, T. and Okushima, M., Protopectin-solubiliz-ing enzyme from Trichosporon penicillatum. Agric. Biol. Chem., 42, 2427-2429 (1978).
4. Sakai, T. and Okushima, M., Purification and crystallization of a protopectin-solubilizing enzyme from Trichosporon penicillatum. Agric. Biol. Chem., 46, 667-676 (1982).
5. Sakai, T., Okushima, M., and Sawada M., Some properties of endo-polygalacturonase from Trichosporon penicillatum SNO-3. Agric. Biol. Chem., 46, 2223-2231 (1982).
6. Sakai, T. and Yoshitake, S., Purification and some properties of a protopectin-solubilizing enzyme from Galactomyces reessii strain L. Agric. Biol. Chem., 48, 1941-1950 (1984).
7. Sakai, T., Okushima, M., and Yoshitake, S., Purification, crystallization and some properties of endo-polygalacturonase from Kluyveromyces fragilis. Agric. Biol. Chem., 48, 1951-1961 (1984).
8. Sakai, T. and Sakamoto, T., Purification and some properties of a protopectin-solubilizing enzyme that has potent activity on sugar beet protopectin. Agric. Biol. Chem., 54, 879-889 (1990).
9. Sakamoto, T., Hours, R. A., and Sakai, T., Purification, characterization, and production of two pectic transeliminases with protopectinase activity from Bacillus subtilis. Biosci. Biotechnol. Biochem., 58, 353-358 (1994).
10. Sakamoto, T., Yoshinaga, J., Shogaki, T., and Sakai, T., Studies on protopectinase-C mode of action: analysis of the chemical structure of the specific substrate in sugar beet protopectin and characterization of the enzyme activity. Biosci. Biotechnol. Biochem., 57, 1832-1837 (1993).
11. Sakai, T., Biotechnological cotton scouring. Sen-shoku Kogyo (in Japanese), 43, 162-173 (1995).
12. Starr, M. P. and Chatterjee, A. K., The genus Er-winia\ enterobacteria pathogenic to plants and animals. Annu. Rev. Microbiol., 26, 389-426 (1972).
13. Nasser, W., Chalet, F., and Robert-Baudouy, J., Purification and characterization of extracellular pec-tate lyase from Bacillus subtilis. Biochimie, 72, 689-695 (1990).
14. Macmillan, J. D. and Vaughan, R. H., Purification and properties of polygalacturonic acid trans-eliminase produced by Clostridium multifermentas. Biochemistry, 3, 564-572 (1964).
15. Nasuno, S. and Starr, M. P., Polygalacturonic acid tram-eliminase of Xanthomonas campestris. Biochem. J., 104, 178-185 (1967).
16. Fuchs, A., The trans-eliminative breakdown of Na-polygalacturonate by Pseudomonas fluorecens. Antonie van Leeuwenhoek, 31, 323-340 (1965).
17. Karbassi, A. and Luh, B. S., Some characteristics of an endo-pectate lyase produced by a thermophilic Bacillus isolated from olives. J. Food Sci., 44, 1156-1161 (1979).
18. Karbassi, A. and Vaughn, R. H., Purification and properties of polygalacturonic acid frans-eliminase from Bacillus stearothermophilus. Can. J. Microbiol., 26, 377-384 (1980).
19. Gibson, T. and Gordon, R. E., Genus I. Bacillus. In “Bergey’s Manual of Determinative Microbiology”, eds. Buchanan, R. E. and Gibbons, N. E., The Williams and Wilkins Co., Baltimore, pp. 529-550 (1974).
20. Tanabe, H., Kobayashi, Y., Matuo, Y., Nishi, N., and Wada, F., Isolation and fundamental properties of endo-pectate lyase pI-isozymes from Erwinia carotovora. Agric. Biol. Chem., 48, 2113-2120 (1984).
21. Seibert, F. B. and Anto, J., Determination of polysaccharide in serum. J. Biol. Chem., 163, 511-522 (1946).
22. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
23. Nasser, W., Awade, A. C., Reverchon, S., and Robert-Baudouy, J., Pectate lyase from Bacillus subtilis: molecular characterization of the gene, and properties of the cloned enzyme. FEBS Lett., 335, 319-326 (1993).
24. Tamaki, S. J., Gold, S., Robeson, M., Manulis, S. and Keen, N. T., Structure and organization of the pel genes from Erwinia chrysanthemi EC 16. J. Bacteriol., 170, 3468-3478 (1988).
25. Keen, N. T. and Tamaki, S., Structure of two pectate lyase genes from Erwinia chrysanthemi EC 16 and their high-level expression in Escherichia coli. J. Bacteriol., 168, 595-606 (1986).
26. Davé, B. A. and Vaughn, R. H., Purification and properties of a polygalacturonic acid frans-eliminase produced by Bacillus pumilus. J. Bacteriol., 108, 166-174 (1971).
27. Nagel, C. W. and Vaughn, R. H., The characteristics of a polygalacturonase produced by Bacillus polγ-myxa. Arch. Biochem. Biophys., 93, 344-352 (1961).
28. Favey, S., Bourson, C., Bertheau, Y., Kotoujansky, A., and Boccara, M., Purification of the acidic pectate lyase and nucleotide sequence of the corresponding gene (pelA) of Erwinia chrysanthemi strain 3937. J. Gen. Microbiol., 138, 499-508 (1992).
29. Iguchi, K., Kishida, M., and Sakai, T., Purification and characterization of three extracellular protopec-tinases with polygalacturonase activities from Trichosporon penicillatum. Biosci. Biotechnol. Biochem., 60, 603-607 (1996).
30. Yoder, M. D., Keen, N. T., and Jurnak, F., New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science, 260, 1503-1507 (1993).
31. Yoder, M. D. and Jurnak, F., The refined three-dimensional structure of pectate lyase C from Erwinia chrysanthemi at 2.2 angstrom resolution. Implication for an enzymatic mechanism. Plant Physiol., 107, 349-364 (1995).
32. Pickersgill, R., Jenkins, J, Harris, G., Nasser, W., and Robert-Baudouy, J., The structure of Bacillus subtilis pectate lyase in complex with calcium. Nat. Struct. Biol., 1, 717-723 (1994).