Skip to main content
PMC home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1990 Jul;56(7):1985–1991. doi: 10.1128/aem.56.7.1985-1991.1990

Characterization of Amylolytic Enzyme Activities Associated with the Hyperthermophilic Archaebacterium Pyrococcus furiosus

Stephen H Brown 1, Henry R Costantino 1, Robert M Kelly 1,*
PMCID: PMC184549  PMID: 16348235

Abstract

The hyperthermophilic archaebacterium Pyrococcus furiosus produces several amylolytic enzymes in response to the presence of complex carbohydrates in the growth medium. These enzyme activities, α-glucosidase, pullulanase, and α-amylase, were detected in both cell extracts and culture supernatants. All activities were characterized by temperature optima of at least 100°C as well as a high degree of thermostability. The existence of this collection of activities in P. furiosus suggests that polysaccharide availability in its growth environment is a significant aspect of the niche from which it was isolated.

Full text

PDF
1989

Images in this article

1988Image
on p.1988
1988Image
on p.1988
1989Image
on p.1989

Selected References

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

  1. Antranikian G., Herzberg C., Gottschalk G. Production of Thermostable alpha-Amylase, Pullulanase, and alpha-Glucosidase in Continuous Culture by a New Clostridium Isolate. Appl Environ Microbiol. 1987 Jul;53(7):1668–1673. doi: 10.1128/aem.53.7.1668-1673.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Aono S., Bryant F. O., Adams M. W. A novel and remarkably thermostable ferredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus. J Bacteriol. 1989 Jun;171(6):3433–3439. doi: 10.1128/jb.171.6.3433-3439.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Blumentals I. I., Robinson A. S., Kelly R. M. Characterization of sodium dodecyl sulfate-resistant proteolytic activity in the hyperthermophilic archaebacterium Pyrococcus furiosus. Appl Environ Microbiol. 1990 Jul;56(7):1992–1998. doi: 10.1128/aem.56.7.1992-1998.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Brown S. H., Kelly R. M. Cultivation Techniques for Hyperthermophilic Archaebacteria: Continuous Culture of Pyrococcus furiosus at Temperatures near 100 degrees C. Appl Environ Microbiol. 1989 Aug;55(8):2086–2088. doi: 10.1128/aem.55.8.2086-2088.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bryant F. O., Adams M. W. Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus. J Biol Chem. 1989 Mar 25;264(9):5070–5079. [PubMed] [Google Scholar]
  6. Buonocore V., Caporale C., De Rosa M., Gambacorta A. Stable, inducible thermoacidophilic alpha-amylase from Bacillus acidocaldarius. J Bacteriol. 1976 Nov;128(2):515–521. doi: 10.1128/jb.128.2.515-521.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Corliss J. B., Dymond J., Gordon L. I., Edmond J. M., von Herzen R. P., Ballard R. D., Green K., Williams D., Bainbridge A., Crane K., van Andel T. H. Submarine thermal sprirngs on the galapagos rift. Science. 1979 Mar 16;203(4385):1073–1083. doi: 10.1126/science.203.4385.1073. [DOI] [PubMed] [Google Scholar]
  8. Costantino H. R., Brown S. H., Kelly R. M. Purification and characterization of an alpha-glucosidase from a hyperthermophilic archaebacterium, Pyrococcus furiosus, exhibiting a temperature optimum of 105 to 115 degrees C. J Bacteriol. 1990 Jul;172(7):3654–3660. doi: 10.1128/jb.172.7.3654-3660.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Fukusumi S., Kamizono A., Horinouchi S., Beppu T. Cloning and nucleotide sequence of a heat-stable amylase gene from an anaerobic thermophile, Dictyoglomus thermophilum. Eur J Biochem. 1988 May 16;174(1):15–21. doi: 10.1111/j.1432-1033.1988.tb14056.x. [DOI] [PubMed] [Google Scholar]
  10. Hyun H. H., Zeikus J. G. General Biochemical Characterization of Thermostable Extracellular beta-Amylase from Clostridium thermosulfurogenes. Appl Environ Microbiol. 1985 May;49(5):1162–1167. doi: 10.1128/aem.49.5.1162-1167.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hyun H. H., Zeikus J. G. General Biochemical Characterization of Thermostable Pullulanase and Glucoamylase from Clostridium thermohydrosulfuricum. Appl Environ Microbiol. 1985 May;49(5):1168–1173. doi: 10.1128/aem.49.5.1168-1173.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  13. Madi E., Antranikian G., Ohmiya K., Gottschalk G. Thermostable amylolytic enzymes from a new clostridium isolate. Appl Environ Microbiol. 1987 Jul;53(7):1661–1667. doi: 10.1128/aem.53.7.1661-1667.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Medda S., Chandra A. K. New strains of Bacillus licheniformis and Bacillus coagulans producing thermostable alpha-amylase active at alkaline pH. J Appl Bacteriol. 1980 Feb;48(1):47–58. doi: 10.1111/j.1365-2672.1980.tb05205.x. [DOI] [PubMed] [Google Scholar]
  15. Melasniemi H. Characterization of alpha-amylase and pullulanase activities of Clostridium thermohydrosulfuricum. Evidence for a novel thermostable amylase. Biochem J. 1987 Aug 15;246(1):193–197. doi: 10.1042/bj2460193. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Pihl T. D., Schicho R. N., Kelly R. M., Maier R. J. Characterization of hydrogen-uptake activity in the hyperthermophile Pyrodictium brockii. Proc Natl Acad Sci U S A. 1989 Jan;86(1):138–141. doi: 10.1073/pnas.86.1.138. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Rinderknecht H., Wilding P., Haverback B. J. A new method for the determination of alpha-amylase. Experientia. 1967 Oct 15;23(10):805–805. doi: 10.1007/BF02146851. [DOI] [PubMed] [Google Scholar]
  18. Saha B. C., Mathupala S. P., Zeikus J. G. Purification and characterization of a highly thermostable novel pullulanase from Clostridium thermohydrosulfuricum. Biochem J. 1988 Jun 1;252(2):343–348. doi: 10.1042/bj2520343. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES