Using proteins in their natural environment: potential and limitations of microbial whole-cell hydroxylations in applied biocatalysis.
The unique catalytic properties of oxygenases (the regio-specific and/or enantio-specific hydroxylation of non-activated carbons) are of undisputed biosynthetic value. Factors that govern the economics of their industrial use include a low k(cat), a frequently decreased k(cat) in recombinant strains, limiting oxygen transfer rates in bioreactors, product inhibition, and the demanding discovery (screening) process.
Duetz
W A
WA
Institute of Biotechnology, ETH Hönggerberg, HPT, CH 8093, Zürich, Switzerland. duetz@biotech.biol.ethz.ch
van Beilen
J B
JB
Witholt
B
B
D001419:Bacteria / Q000166:cytology* / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D019149:Bioreactors; D001711:Biotransformation; D002384:Catalysis; D006900:Hydroxylation; D007700:Kinetics; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D010100:Oxygen / Q000378:metabolism; D010105:Oxygenases / Q000302:isolation & purification / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*
D001426:Bacterial Proteins; D011506:Proteins; D009243:NAD; D009249:NADP; D010105:Oxygenases; D010100:Oxygen