Tagatose production with pH control in a stirred tank reactor containing immobilized L-arabinose rom Thermotoga neapolitana.
Chitopearl beads were used as immobilization supports for D-tagatose production from D-galactose by L-arabinose isomerase from Thermotoga neapolitana because chitopearl beads were more stable than alginate beads at temperatures above 60 degrees C. The pH and temperature for the maximum isomerization of galactose were 7.5 and 90 degrees C, respectively. In thermostability experiments, the half-lives of the immobilized enzyme at 70, 75, 80, 85, and 90 degrees C were 388, 106, 54, 36, and 22 h, respectively. The reaction temperature was determined to be 70 degrees C because the enzyme is highly stable up to 70 degrees C during the reaction. When the reaction time, galactose concentration, and temperature were increased, the pH of a mixture containing enzyme and galactose decreased by the Maillard reaction, resulting in decreased tagatose production. With pH control at 7.5, tagatose production (138 g/L) at 70 degrees C in a stirred tank reactor containing immobilized enzyme and 300 g/L galactose increased two times higher, comparing that without pH control.
Lim
Byung-Chul
BC
Department of Bioscience and Biotechnology, Konkuk University, Seoul 143-701, South Korea.
Kim
Hye-Jung
HJ
Oh
Deok-Kun
DK
D019747:Aldose-Ketose Isomerases / Q000378:metabolism*; D019149:Bioreactors; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006601:Hexoses / Q000096:biosynthesis*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D046949:Thermotoga neapolitana / Q000201:enzymology*
D004800:Enzymes, Immobilized; D006601:Hexoses; D019747:Aldose-Ketose Isomerases; C019715:L-arabinose isomerase; C030192:tagatose