Hyperthermophilic enzymes--stability, activity and implementation strategies for high temperature applications.
Current theories agree that there appears to be no unique feature responsible for the remarkable heat stability properties of hyperthermostable proteins. A concerted action of structural, dynamic and other physicochemical attributes are utilized to ensure the delicate balance between stability and functionality of proteins at high temperatures. We have thoroughly screened the literature for hyperthermostable enzymes with optimal temperatures exceeding 100 degrees C that can potentially be employed in multiple biotechnological and industrial applications and to substitute traditionally used, high-cost engineered mesophilic/thermophilic enzymes that operate at lower temperatures. Furthermore, we discuss general methods of enzyme immobilization and suggest specific strategies to improve thermal stability, activity and durability of hyperthermophilic enzymes.
Department of Chemical and Materials Engineering, University of Alberta, Edmonton, Canada.
Larry D
LD
Unsworth
John
J
van der Oost
Sotirios
S
Koutsopoulos
D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D023281:Genomics / Q000379:methods; D006358:Hot Temperature; D007218:Industrial Microbiology / Q000379:methods; D015202:Protein Engineering / Q000379:methods; D040901:Proteomics / Q000379:methods
D004798:Enzymes; D004800:Enzymes, Immobilized