Biotransformation of ginsenoside using covalently immobilized snailase enzyme onto activated carrageenan gel beads

Ginsenoside transformation has received significant attention from scientists. The main objective of this study is to use immobilized enzymes in ginsenoside transformation. Factors affecting immobilization process were studied; carrageenan beads treated with polyethyleneimine and then activated using glutaraldehyde (GA) were used for snailase enzyme immobilization. The functionalized gel beads were characterized using Fourier transform infrared spectroscopy to verify the modification process. Furthermore, the optimum conditions for biotransformation of ginsenoside were also deliberated and showed that optimum biotransformation pH is 4.5 and 5–5.5 and temperature 50 and $$60^\circ \hbox {C}$$ for free and immobilized snailase, respectively. Michaelis constants, $$K_{\mathrm{m}}$$ and $$V_\max $$ , were also studied. The immobilized enzyme retains 96% of its initial activity after being used 10 consecutive times. The results clearly suggested that ginsenoside transformation was performed using immobilized snailase; this process can reduce the transformation cost as the enzyme can be reused many times.