Abstract: In this study, an enzyme immobilization method effective for transformation of ginsenoside Rb1 and sufficiently robust as an immobilization enzyme reactor has been developed. Using a model hydrolase enzyme, β-glucosidase from Aspergillus Niger, immobilization within chemically cross-linked coating amino-based silica is achieved by multi-point biotinylation oriented linking by streptavidin. The optimum pH value for both free enzyme and immobilized enzyme was pH 5.5. The optimal reaction temperature of the immobilized enzyme was 45 ℃, which was a 5 ℃ increase from that of the free enzyme. The Michaelis constant (Km) values before and after immobilization were 0.482 mmol•L-1 and 0.387 mmol•L-1, respectively. The catalytic efficiency of the immobilized enzyme was three-fold higher than the free enzyme (57.52mM-1S-1). Under repeated batch conditions, the residual activity remained 97% of the initial after 45 times of reuse.

Rigid Immobilized Enzyme Reactor-Separator Design for Biotransformation of Ginsenoside Rb1

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