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. 1981 Apr;41(4):857–866. doi: 10.1128/aem.41.4.857-866.1981

Formation and Location of 1,4-β-Glucanases and 1,4-β-Glucosidases from Penicillium janthinellum

Peter Rapp 1, Elisabeth Grote 1, Fritz Wagner 2
PMCID: PMC243824  PMID: 16345751

Abstract

Formation and location of 1,4-β-glucanases and 1,4-β-glucosidases were studied in cultures of Penicillium janthinellum grown on Avicel, sodium carboxymethyl cellulose, cellobiose, glucose, mannose, and maltose. Endo-1,4-β-glucanases were found to be cell free, and their formation was induced by cellobiose. 1,4-β-Glucosidases, on the other hand, were formed constitutively and were primarily cell free, but with a small amount strongly associated with the cell wall. Low 1,4-β-glucosidase activities of periplasmic or intracellular origin were also found. A rotational viscosimetric method was developed to measure the total endo-1,4-β-glucanase activity of the culture (broth and solids). By this method, it was possible to determine the endo-1,4-β-glucanase activity not only in the supernatant of the culture but also on the surface of the mycelium or absorbed on residual Avicel. During a 70-liter batch cultivation of P. janthinellum, the adsorption of endo-1,4-β-glucanases by residual and newly added 10% Avicel was measured. The adsorption of soluble protein and endo-1,4-β-glucanases by Avicel was found to be largely independent of the pH value but dependent on temperature.

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Selected References

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  1. Almin K. E., Eriksson K. E. Enzymic degradation of polymers. I. Viscometric method for the determination of enzymic activity. Biochim Biophys Acta. 1967 Jul 11;139(2):238–247. doi: 10.1016/0005-2744(67)90028-9. [DOI] [PubMed] [Google Scholar]
  2. Almin K. E., Eriksson K. E. Influence of carboxymethyl cellulose properties on the determination of cellulase activity in absolute terms. Arch Biochem Biophys. 1968 Mar 20;124(1):129–134. doi: 10.1016/0003-9861(68)90311-1. [DOI] [PubMed] [Google Scholar]
  3. Almin K. E., Eriksson K. E., Jansson C. Enzymic degradation of polymers. II. Viscometric determination of cellulase activity in absolute terms. Biochim Biophys Acta. 1967 Jul 11;139(2):248–253. doi: 10.1016/0005-2744(67)90029-0. [DOI] [PubMed] [Google Scholar]
  4. Berg B., Pettersson G. Location and formation of cellulases in Trichoderma viride. J Appl Bacteriol. 1977 Feb;42(1):65–75. doi: 10.1111/j.1365-2672.1977.tb00670.x. [DOI] [PubMed] [Google Scholar]
  5. Berghem L. E., Pettersson L. G. The mechanism of enzymatic cellulose degradation. Purification of a cellulolytic enzyme from Trichoderma viride active on highly ordered cellulose. Eur J Biochem. 1973 Aug 1;37(1):21–30. doi: 10.1111/j.1432-1033.1973.tb02952.x. [DOI] [PubMed] [Google Scholar]
  6. Boretti G., Garofano L., Montecucchi P., Spalla C. Cellulase production with Penicillium iriense (n.sp.). Arch Mikrobiol. 1973 Aug 21;92(3):189–200. doi: 10.1007/BF00411199. [DOI] [PubMed] [Google Scholar]
  7. Deshpande V., Eriksson K. E., Pettersson B. Production , purification and partial characterization of 1,4-beta-glucosidase enzymes from Sporotrichum pulverulentum. Eur J Biochem. 1978 Sep 15;90(1):191–198. doi: 10.1111/j.1432-1033.1978.tb12590.x. [DOI] [PubMed] [Google Scholar]
  8. Eriksson K. E., Hamp S. G. Regulation of Endo-1,4-beta-glucanase production in Sporotrichum pulverulentum. Eur J Biochem. 1978 Sep 15;90(1):183–190. doi: 10.1111/j.1432-1033.1978.tb12589.x. [DOI] [PubMed] [Google Scholar]
  9. Eriksson K. E., Hollmark B. H. Kinetic studies of the action of cellulase upon sodium carboxymethyl cellulose. Arch Biochem Biophys. 1969 Sep;133(2):233–237. doi: 10.1016/0003-9861(69)90450-0. [DOI] [PubMed] [Google Scholar]
  10. Eriksson K. E., Pettersson G. Studies on cellulolytic enzymes. V. Some structural properties of the cellulase from Penicillium notatum. Arch Biochem Biophys. 1968 Mar 20;124(1):160–166. doi: 10.1016/0003-9861(68)90316-0. [DOI] [PubMed] [Google Scholar]
  11. Hulme M. A. Viscometric determination of carboxymethylcellulase in standard international units. Arch Biochem Biophys. 1971 Nov;147(1):49–54. doi: 10.1016/0003-9861(71)90308-0. [DOI] [PubMed] [Google Scholar]
  12. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  13. Loewenberg J. R., Chapman C. M. Sophorose metabolism and cellulase induction in Trichoderma. Arch Microbiol. 1977 May 13;113(1-2):61–64. doi: 10.1007/BF00428581. [DOI] [PubMed] [Google Scholar]
  14. MANDELS M., PARRISH F. W., REESE E. T. Sophorose as an inducer of cellulase in Trichoderma viride. J Bacteriol. 1962 Feb;83:400–408. doi: 10.1128/jb.83.2.400-408.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. MANDELS M., REESE E. T. Induction of cellulase in fungi by cellobiose. J Bacteriol. 1960 Jun;79:816–826. doi: 10.1128/jb.79.6.816-826.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Nisizawa T., Suzuki H., Nakayama M., Nisizawa K. Inductive formation of cellulase by sophorose in Trichoderma viride. J Biochem. 1971 Sep;70(3):375–385. doi: 10.1093/oxfordjournals.jbchem.a129652. [DOI] [PubMed] [Google Scholar]
  17. Nisizawa T., Suzuki H., Nisizawa K. Catabolite repression of cellulase formation in Trichoderma viride. J Biochem. 1972 Jun;71(6):999–1007. doi: 10.1093/oxfordjournals.jbchem.a129872. [DOI] [PubMed] [Google Scholar]
  18. Olutiola P. O. A cellulase complex in culture filtrates of Penicillium citrinum. Can J Microbiol. 1976 Aug;22(8):1153–1159. doi: 10.1139/m76-167. [DOI] [PubMed] [Google Scholar]
  19. Peitersen N., Medeiros J., Mandels M. Adsorption of Trichoderma cellulase on cellulose. Biotechnol Bioeng. 1977 Jul;19(7):1091–1094. doi: 10.1002/bit.260190710. [DOI] [PubMed] [Google Scholar]
  20. Pettersson G., Eaker D. L. Studies on cellulolytic enzymes. IV. Chemical and physiochemical characterization of a cellulase for Penicillium notatum. Arch Biochem Biophys. 1968 Mar 20;124(1):154–159. doi: 10.1016/0003-9861(68)90315-9. [DOI] [PubMed] [Google Scholar]
  21. Pettersson G. Studies on cellulolytic enzymes. 3. Isolation of a cellulase from Penicillium notatum. Arch Biochem Biophys. 1968 Feb;123(2):307–311. doi: 10.1016/0003-9861(68)90139-2. [DOI] [PubMed] [Google Scholar]
  22. Smith M. H., Gold M. H. Phanerochaete chrysosporium beta-Glucosidases: Induction, Cellular Localization, and Physical Characterization. Appl Environ Microbiol. 1979 May;37(5):938–942. doi: 10.1128/aem.37.5.938-942.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Sternberg D., Mandels G. R. Induction of cellulolytic enzymes in Trichoderma reesei by sophorose. J Bacteriol. 1979 Sep;139(3):761–769. doi: 10.1128/jb.139.3.761-769.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Tsai H., Tsai J. H., Yu P. H. Effects of yeast proteinase and its inhibitor on the inactivation of tryptophan synthase from Saccharomyces cerevisiae and Neurospora crassa. Eur J Biochem. 1973 Dec 3;40(1):225–232. doi: 10.1111/j.1432-1033.1973.tb03190.x. [DOI] [PubMed] [Google Scholar]
  25. Updegraff D. M. Semimicro determination of cellulose in biological materials. Anal Biochem. 1969 Dec;32(3):420–424. doi: 10.1016/s0003-2697(69)80009-6. [DOI] [PubMed] [Google Scholar]

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