1887

Abstract

A (1.3)---glucan glucanohydrolase (EC 3.2.1.6), capable of hydrolysing resistant curdlan, was purified chromatographically from the culture supernatant of complex YK9 on Toyopearl HW-55F and butyl-Toyopearl 650M columns. The purified enzyme had a specific activity of 190 units mg on regenerated curdlan. The molecular mass was estimated to be about 70 kDa as judged by SDS-PAGE. The enzyme had a pH optimum of approximately pH 6.0. It hydrolysed regenerated and resistant curdlans yielding predominantly laminari-biose, although the rate of hydrolysis of the former was much higher than the latter. This enzyme rapidly hydrolysed laminaran, curdlan and carboxymethyl-curdlan, but did not cleave schizophyllan and screloglucan, which have glucosyl side chains. The enzyme hydrolysed low molecular mass (1→3)---glucans (mean degree of polymerization,.DPTn = 131, 49 and 14) and laminari-heptaose more efficiently than curdlan. It also hydrolysed laminari-hexaose and -pentaose effectively, but laminari-tetraose only slightly and it did not hydrolyse laminari-triose or -biose. The enzyme is an exo-hydrolase of curdlan and various oligomers composed of (1→3)---glucosidic linkages, liberating laminari-biose from their non-reducing terminals. The laminari-biose generated was in the α-form.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-140-3-637
1994-03-01
2024-04-26
Loading full text...

Full text loading...

/deliver/fulltext/micro/140/3/mic-140-3-637.html?itemId=/content/journal/micro/10.1099/00221287-140-3-637&mimeType=html&fmt=ahah

References

  1. Aono R., Sato M., Yamamoto M., Horikoshi H. Isolation and partial characterization of an 87-kilodalton β-1,3-glucanase from bacillus circulans IMI 165. Appl "Environ Microbiol 1992; 58:520–524
    [Google Scholar]
  2. Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal biochem 1976; 72:248–254
    [Google Scholar]
  3. Harada T. The story of research into curdlan and the bacteria producing it. Trends Glycosci Glycotechnol 1992; 4:309–317
    [Google Scholar]
  4. Harada T., Misaki A., Saito H. Curdlan: bacterial gelforming β-1,3-glucan. Arch biochem biophys 1968; 124:292–298
    [Google Scholar]
  5. Harada T., Kanzawa Y., Kanenaga K., Koreeda A., Harada A. Electron microscopic studies on the ultrastructure of curdlan and other polysaccharides in gels used in foods. Food Struct 1991; 10:1–18
    [Google Scholar]
  6. Imura N., Ohshima T., Kurokawa M., Nagai Y., Miura K., Mizushima S. 1984 Handbook of biochemistry Tokyo: Maruzen;
    [Google Scholar]
  7. Kanzawa Y., Koreeda A., Harada A., Harada T. Electron microscopy of the gel-forming ability of polysaccharide food additives. Agric biol Chem 1989; 53:979–989
    [Google Scholar]
  8. Kanzawa Y., Harada A., Harada T. Production of an enzyme capable of hydrolyzing resistant curdlan by soil bacteria. Home Econ Jpn 1991; 42:703–709
    [Google Scholar]
  9. Kanzawa Y., Kanenaga K., Harada T., Harada A., Yokota A. Strains of bacillus circulans complex capable of hydrolyzing resistant curdlan to produce laminaribiose. Nippon Nogeikagaku Kaishi 1993; 67:319
    [Google Scholar]
  10. Kitamura K., Kaneko T., Yamamoto Y. Lysis of viable yeast cells by enzymes of Arthrobacter luteus. II. Purification and properties of an enzyme, Zymolyase, which lyses viable yeast cells. Gen Appl Microbiol 1974; 20:323–344
    [Google Scholar]
  11. Kobayashi Y., Tanaka H., Ogasawara N. Multiple β-1,3 glucanases in the lytic enzyme complex of Bacillus circulans WL-12. Agric Biol Chem 1974; 48:1433–1440
    [Google Scholar]
  12. Kusama S., Kusakabe I., Zama M., Murakami K., Yasui T. Enzymatic preparation of crystalline laminaribiose from curdlan. Agric Biol Chem 1984; 48:1433–1440
    [Google Scholar]
  13. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680–685
    [Google Scholar]
  14. Molina M., Cenamor R., Sanchez M., Nombela C. Purification and some properties of Candida albicans exo-1,3-β-glucanase. J Gen Microbiol 1989; 135:309–314
    [Google Scholar]
  15. Nagasaki N., Saito K., Yamamoto S. Purification and characterization of an exo-β-l,3-glucanase from a fungi imperfecti. Agric biol Chem 1977; 41:493–502
    [Google Scholar]
  16. Nelson T. E., Johnson J. Jr, Jantzen E., 8c Kirkwood S. Action pattern and specificity of an exo-β-(l→3)-o-glucanase from basidiomycetes species QM 806. J Biol Chem 1969; 244:5972–5980
    [Google Scholar]
  17. Okuyama K., Otsubo A., Fukuzawa Y., Ozawa K., Harada T., Kasai N. Single-helical structure of native curdlan and its aggregation state. J Carbohydr Chem 1991; 10:645–656
    [Google Scholar]
  18. Somogyi M. A new reagent for the determination of sugars. J Biol Chem 1952; 195:19–23
    [Google Scholar]
  19. Takahashi F., Harada T., Koreeda A., Harada A. Structure of curdlan that is resistant to (1→3)-β-d-glucanase. Carbohydr Polym 1986; 6:407–421
    [Google Scholar]
  20. Thoma J. A., Koshland D. E. Jr Competitive inhibition by substrate during enzyme action. Evidence for the induced-fit theory. J Am Chem Soc 1960; 82:3329–3333
    [Google Scholar]
  21. Yokota A., Sakano T. Taxonomic significance of fatty acid compositions in whole cells and lipopolysaccharides in Rhizobiaceae . IFO Res Commun 1991; 15:57–75
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-140-3-637
Loading
/content/journal/micro/10.1099/00221287-140-3-637
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error