Characterization of amylolytic enzyme activities associated with the hyperthermophilic archaebacterium Pyrococcus furiosus
Journal Article
·
· Applied and Environmental Microbiology; (USA)
OSTI ID:5963717
- Johns Hopkins Univ., Baltimore, MD (USA) Univ. of Maryland, Baltimore (USA)
The hyperthermophilic archaebacterium Pyrococcus furiosus produces several amylolytic enzymes in response to the presence of complex carbohydrates in the growth medium. These enzyme activities, {alpha}-glucosidase, pullulanase, and {alpha}-amylase, were detected in both cell extracts and culture supernatants. All activities were characterized by temperature optima of at least 100{degree}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.
- OSTI ID:
- 5963717
- Journal Information:
- Applied and Environmental Microbiology; (USA), Journal Name: Applied and Environmental Microbiology; (USA) Vol. 56:7; ISSN 0099-2240; ISSN AEMID
- Country of Publication:
- United States
- Language:
- English
Similar Records
Thermostable amylolytic enzymes from a new Clostridium isolate
Characterization of the glycolytic enzyme enolase which is abundant in the hyperthermophilic archaeon, Pyrococcus furiosus
Role of polysulfides in reduction of elemental sulfur by the hyperthermophilic archaebacterium Pyrococcus furiosus
Journal Article
·
Wed Jul 01 00:00:00 EDT 1987
· Appl. Environ. Microbiol.; (United States)
·
OSTI ID:5625620
Characterization of the glycolytic enzyme enolase which is abundant in the hyperthermophilic archaeon, Pyrococcus furiosus
Technical Report
·
Thu Dec 30 23:00:00 EST 1993
·
OSTI ID:10124321
Role of polysulfides in reduction of elemental sulfur by the hyperthermophilic archaebacterium Pyrococcus furiosus
Journal Article
·
Tue May 01 00:00:00 EDT 1990
· Applied and Environmental Microbiology; (USA)
·
OSTI ID:6604934