Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1967 Nov;105(2):577–583. doi: 10.1042/bj1050577

The glucoamylase of Coniophora cerebella

N J King 1
PMCID: PMC1198347  PMID: 5584000

Abstract

1. The major amylolytic enzyme in culture filtrates of Coniophora cerebella grown in starch-containing media has been purified and characterized as a glucoamylase (EC 3.2.1.3). 2. The activity/unit wt. of protein was increased 11-fold and the enzyme showed one major component on polyacrylamide-gel electrophoresis. 3. The glucoamylase had optimum pH4·0–4·5. 4. Hg2+ completely inhibited the enzyme, but other ions tested had little effect on the activity at the concentration of ions used (5mm). 5. The action of the enzyme on amylopectin, amylose and maltose was studied. Hydrolysis proceeded by the stepwise removal of glucose units from the non-reducing ends of the polymer chains, and the enzyme was able to bypass or to hydrolyse the α-(1→6)-glucosidic linkages at branch points in the amylopectin molecule. Glucose was the only product found in digests of these substrates. 6. At the same substrate concentration (0·1%, w/v) and enzyme concentration, the initial rates of glucose production from amylopectin, amylose and maltose were in the proportions 40:10:1. 7. Km values at 40° and pH4·0 were calculated for the enzyme acting on amylopectin, amylose and maltose.

Full text

PDF
577

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BROOME J. A RAPID METHOD OF DISK ELECTROPHORESIS. Nature. 1963 Jul 13;199:179–180. doi: 10.1038/199179b0. [DOI] [PubMed] [Google Scholar]
  2. DAHLQVIST A. Determination of maltase and isomaltase activities with a glucose-oxidase reagent. Biochem J. 1961 Sep;80:547–551. doi: 10.1042/bj0800547. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  4. HJERTEN S., LEVIN O., TISELIUS A. Protein chromatography on calcium phosphate columns. Arch Biochem Biophys. 1956 Nov;65(1):132–155. doi: 10.1016/0003-9861(56)90183-7. [DOI] [PubMed] [Google Scholar]
  5. HUGGETT A. S., NIXON D. A. Use of glucose oxidase, peroxidase, and O-dianisidine in determination of blood and urinary glucose. Lancet. 1957 Aug 24;273(6991):368–370. doi: 10.1016/s0140-6736(57)92595-3. [DOI] [PubMed] [Google Scholar]
  6. Hiromi K., Takahashi K., Hamauzu Z. I., Ono S. Kinetic studies on gluc-amylase. 3. The influence of pH on the rates of hydrolysis of maltose and panose. J Biochem. 1966 May;59(5):469–475. doi: 10.1093/oxfordjournals.jbchem.a128329. [DOI] [PubMed] [Google Scholar]
  7. King N. J. The extracellular enzymes of Coniophora cerebulla. Biochem J. 1966 Sep;100(3):784–792. doi: 10.1042/bj1000784. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. LYR H. [Formation of ectoenzymes by wood-destroying and wood-inhabiting fungi on various culture media. IV. (Xylan and glucose as carbon sources)]. Arch Mikrobiol. 1959;34:418–433. [PubMed] [Google Scholar]
  10. PAZUR J. H., ANDO T. The hydrolysis of glucosyl oligosaccharides with alpha-D-(1-4) and alpha-D-(1-6) bonds by fungal amyloglucosidase. J Biol Chem. 1960 Feb;235:297–302. [PubMed] [Google Scholar]
  11. PAZUR J. H., KLEPPE K. The hydrolysis of alpha-D-glucosides by amyloglucosidase from Aspergillus niger. J Biol Chem. 1962 Apr;237:1002–1006. [PubMed] [Google Scholar]
  12. SMOGYI M. Notes on sugar determination. J Biol Chem. 1952 Mar;195(1):19–23. [PubMed] [Google Scholar]
  13. TREVELYAN W. E., PROCTER D. P., HARRISON J. S. Detection of sugars on paper chromatograms. Nature. 1950 Sep 9;166(4219):444–445. doi: 10.1038/166444b0. [DOI] [PubMed] [Google Scholar]
  14. TSUJISAKA Y., FUKUMOTO J., YAMAMCTO T. Specificity of crystalline saccharogenic amylase of moulds. Nature. 1958 Mar 15;181(4611):770–771. doi: 10.1038/181770a0. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES