Starch-hydrolyzing enzymes from thermophilic archaea and bacteria.
Extremophlic microorganisms have developed a variety of molecular strategies in order to survive in harsh conditions. For the utilization of natural polymeric substrates such as starch, a number of extremophiles, belonging to different taxonomic groups, produce amylolytic enzymes. This class of enzyme is important not only for the study of biocatalysis and protein stability at extreme conditions but also for the many biotechnological opportunities they offer. In this review, we report on the different molecular properties of thermostable archaeal and bacterial enzymes including alpha-amylase, alpha-glucosidase, glucoamylase, pullulanase, and cyclodextrin glycosyltransferase. Comparison of the primary sequence of the pyrococcal pullulanase with other members of the glucosyl hydrolase family revealed that significant differences are responsible for the mode of action of these enzymes.
Bertoldo
Costanzo
C
Technical University Hamburg-Harburg, Institute of Technical Microbiology, Kasernenstrasse 12, 21073, Hamburg, Germany.
Antranikian
Garabed
G
D001105:Archaea / Q000201:enzymology*; D019843:Archaeal Proteins / Q000235:genetics / Q000378:metabolism; D001709:Biotechnology; D017124:Conserved Sequence; D006026:Glycoside Hydrolases / Q000235:genetics / Q000378:metabolism*; D013213:Starch / Q000378:metabolism; D013696:Temperature; D013824:Thermus / Q000201:enzymology*
D019843:Archaeal Proteins; D013213:Starch; D006026:Glycoside Hydrolases