1887

Abstract

Summary: The mushroom produces a single endoxylanase (1,4-β-D-xylan xylano-hydrolase, EC 3.2.1.8) in the presence of either dextrin or xylan as sole source of carbon. The enzymes produced in the two conditions are different. The enzyme induced by xylan has been purified 67-fold from the culture filtrate of . The enzyme preparation gave a single protein band on SDS-PAGE, corresponding to a molecular weight of about 24000. The enzyme has an isoelectric point at pH 4·0 and acts on arabinoxylan and arabinogalactan, but not amylopectin or galactomannan. It shows maximum activity on xylan (1,4-β-linked D-xylopyranose units) at pH 3·5 and 55°C and is fairly stable up to 60°C. The for xylan is 4 mg ml. Hg, Fe and Ag are the most potent inhibitors of the enzyme. The pH optimum and molecular weight of this inducible xylanase differ from those of the enzyme produced by the same organism grown in dextrin medium.

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/content/journal/micro/10.1099/00221287-131-8-1881
1985-08-01
2021-08-06
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References

  1. Cisar J., Kabat E. A., Dorner M. M., Liao J. 1975; Binding properties of immunoglobulin combining sites specific for terminal or nonterminal antigen determinants in dextran. Journal of Experimental Medicine 142:435–458
    [Google Scholar]
  2. Comtat J. 1983; Isolation, properties and postulated role of some xylanases from the basidiomycete Sporotrichum dimorphosporium . Carbohydrate Research 118:215–223
    [Google Scholar]
  3. Davis B. J. 1964; Disk electrophoresis. II. Method and application to human serum proteins. Annals of the New York Academy of Sciences 121:404–427
    [Google Scholar]
  4. Dekker R. F. H., Richards G. N. 1976; Hemicellulases: their occurrence, purification, properties and mode of action. Advances in Carbohydrate Chemistry and Biochemistry 22:227–252
    [Google Scholar]
  5. Ghosh A. K., Sengupta S. 1978; Studies on biochemistry of higher fungi. II. Submerged growth of a few mushrooms in synthetic media. Journal of Food Science and Technology 15:237–242
    [Google Scholar]
  6. Ghosh A. K., Banerjee P. C., Sengupta S. 1980; Purification and properties of xylan hydrolase from mushroom Termitomyces clypeatus . Biochimica et biophysica acta 612:143–152
    [Google Scholar]
  7. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4 . Nature, London 227:680–685
    [Google Scholar]
  8. Nelson N. 1944; A photometric adaption of the Somogyi method for the determination of glucose. Journal of Biological Chemistry 153:375–380
    [Google Scholar]
  9. Rufo G. A. Jr, Singh J. P., Babcock D. F., Lardy H. A. 1982; Purification and characterization of a calcium transport inhibitor protein from bovine seminal plasma. Journal of Biological Chemistry 257:4627–4632
    [Google Scholar]
  10. Somogyi M. 1952; Notes on sugar determination. Journal of Biological Chemistry 195:19–23
    [Google Scholar]
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