Chitopearl beads were used as immobilization supports for D-tagatose production by L-arabinose isomerase from Thermotoga neapolitana because chitopearl beads were more stable than alginate beads at temperatures above 60°C. The optimal pH and temperature for the isomerization of D-galactose were 7.5 and 90ºC, respectively. The half-life of immobilized L-arabinose isomerase was 11 times higher than that of free enzyme at 90°C. The pH of a mixture containing partially purified enzyme and galactose decreased as the reaction time, galactose concentration, and temperature increased, resulting in decreased tagatose production. When the pH was maintained at 7.5 in a stirred tank reactor containing immobilized enzyme, 138 g/L tagatose was produced at 70°C from 300 g/L galactose, while only 70 g/L was produced without pH control.
키워드
L-Arabinose isomeraseTagatoseImmobilizationThermotoga neapolitanaStirred tank reactorpH control
저자
Byung-Chul Lim [ Department of Bioscience and Biotechnology, Konkuk University ]
Hye-Jung Kim [ Department of Bioscience and Biotechnology, Konkuk University ]
Deok-Kun Oh [ Department of Bioscience and Biotechnology, Konkuk University ]
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
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