Protein engineering of bacterial alpha-amylases.
alpha-Amylases constitute a very diverse family of glycosyl hydrolases that cleave alpha1-->4 linkages in amylose and related polymers. Recent structural and mutagenic studies of archeael, mammalian and bacterial alpha-amylases have resulted in a wealth of information on the catalytic mechanism and on the structural features of this enzyme class. Because of their high thermo-stability, the Bacillus alpha-amylases have found widespread use in industrial processes, and much attention has been devoted to optimising these enzymes for the very harsh conditions encountered there. Stability has been a major area of focus in this respect, and several remarkably stable bacterial alpha-amylases have been produced by bioengineering techniques. Protein engineering studies of pH-activity profiles and of substrate specificities have also been initiated, although without much success. In the coming years it is likely, however, that the focus of alpha-amylase engineering will shift from engineering stability to these new areas.
Nielsen
J E
JE
EMBL, Meyerhofstrasse 1, 69117 Heidelber, Germany.
Borchert
T V
TV
D001407:Bacillus; D001419:Bacteria / Q000201:enzymology*; D001665:Binding Sites; D002384:Catalysis; D017124:Conserved Sequence; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007221:Industry; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D015202:Protein Engineering; D000516:alpha-Amylases / Q000737:chemistry* / Q000145:classification / Q000235:genetics
D000516:alpha-Amylases