One-pot synthesis of L-Fructose using coupled multienzyme systems based on rhamnulose-1-phosphate aldolase.
Two methods have been developed for the highly efficient enzymatic synthesis of L-fructose: one is based on rhamnulose-1-phosphate aldolase and acid phosphatase using racemic glyceraldehyde and dihydroxyacetone phosphate as substrates; the other is to generate enantiomerically pure L-glyceraldehyde in situ from glycerol for the aldol reaction, using galactose oxidase catalyzed oxidation of glycerol in the presence of catalase. Using this four-enzyme system, enantiomerically pure L-fructose was obtained. Using the more expensive dihydroxyacetone phosphate, the yield was 55% after purification.
Franke
Dirk
D
Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
Machajewski
Timothy
T
Hsu
Che-Chang
CC
Wong
Chi-Huey
CH
D000135:Acid Phosphatase; D000446:Aldehyde-Lyases; D002374:Catalase; D005632:Fructose / Q000138:chemical synthesis* / Q000737:chemistry*; D007202:Indicators and Reagents; D010766:Phosphorylation; D013237:Stereoisomerism
D007202:Indicators and Reagents; D005632:Fructose; D002374:Catalase; D000135:Acid Phosphatase; D000446:Aldehyde-Lyases; C022526:rhamnulose-1-phosphate adolase