Expression of psychrophilic genes in mesophilic hosts: assessment of the folding state of a recombinant alpha-amylase.
Alpha-Amylase from the antarctic psychrophile Altermonas haloplanktis is synthesized at 0 +/- 2 degrees C by the wild strain. This heat-labile alpha-amylase folds correctly when overexpressed in Escherichia coli, providing the culture temperature is sufficiently low to avoid irreversible denaturation. In the described expression system, a compromise between enzyme stability and E. coli growth rate is reached at 18 degrees C.
Feller
G
G
Laboratory of Biochemistry, University of Liège, Liège-Sart Tilman, Belgium. gfeller@ulg.ac.be
Le Bussy
O
O
Gerday
C
C
D004926:Escherichia coli / Q000235:genetics; D006090:Gram-Negative Bacteria / Q000201:enzymology*; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry; D000516:alpha-Amylases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D011994:Recombinant Proteins; D000516:alpha-Amylases