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Updated: Jul 12, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Characterization of Amylolytic Enzyme Activities Associated with the Hyperthermophilic Archaebacterium Pyrococcus
S H Brown1, H R Costantino, R M Kelly
1Department of Chemical Engineering, The Johns Hopkins University, Baltimore, Maryland 21218, and Center of Marine Biotechnology, University of Maryland, Baltimore, Maryland 21202.
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, 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 degrees 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.
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