Protein engineering of bacterial alpha-amylases

Citation
Je. Nielsen et Tv. Borchert, Protein engineering of bacterial alpha-amylases, BBA-PROT ST, 1543(2), 2000, pp. 253-274
Citations number
88
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
ISSN journal
01674838 → ACNP
Volume
1543
Issue
2
Year of publication
2000
Pages
253 - 274
Database
ISI
SICI code
0167-4838(200012)1543:2<253:PEOBA>2.0.ZU;2-8
Abstract
alpha -Amylases constitute a very diverse family of glycosyl hydrolases tha t cleave alpha1 --> 4 linkages in amylose and related polymers. Recent stru ctural and mutagenic studies of archeael, mammalian and bacterial alpha -am ylases 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 th ese enzymes for the very harsh conditions encountered there. Stability has been a major area of focus in this respect, and several remarkably stable b acterial alpha -amylases have been produced by bioengineering techniques. P rotein engineering studies of pH-activity profiles and of substrate specifi cities have also been initiated, although without much success. In the comi ng years it is likely, however, that the focus of alpha -amylase engineerin g will shift from engineering stability to these new areas. (C) 2000 Elsevi er Science B.V. All rights reserved.