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- W4295957531 abstract "Icariin, the most effective bioactive component in Epimedium, is also the index component of Epimedium quality control in Pharmacopoeia. It was a very attractive approach for bioconversion from epimedin C to icariin. However, its potential was impeded by poor stability and non-recyclable properties of free enzymes. In this study, we have fused the linker (4LP) to α-L-rhamnosidase BtRha and successfully prepared the immobilized enzyme (incubated 4LP-BtRha@Na-Y) to produce icariin from epimedin C. The activity recovery of 4LP-BtRha@Na-Y was 79.6 %, and enzyme activity was 209.8 U/g, which was 1.75-fold and 1.6-fold higher than that of immobilized BtRha (BtRha@Na-Y), respectively. The optimal reaction temperature and pH of 4LP-BtRha@Na-Y was 55 °C and 6.5, respectively. The thermal stability of immobilized enzyme was significantly improved by incubation in phosphate buffer containing 20 % glycerol and 10 % fructose. The kcat/Km value of incubated 4LP-BtRha@Na-Y was 7.98 × 105 s−1M−1, which increased by 8 % compared with free BtRha. Finally, under suitable conditions, 1 g/L epimedin C was transformed into icariin with icariin yield 75.1 %, and the relative conversion rate retained 74.9 % after reused 13 cycles. This experiment provides a new idea for one-step purification and immobilization of α-L-rhamnosidase for direct biotransformation from epimedin C to icariin, which will have great prospects in food and pharmaceutical production." @default.
- W4295957531 created "2022-09-16" @default.
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- W4295957531 date "2023-01-01" @default.
- W4295957531 modified "2023-09-23" @default.
- W4295957531 title "Linker-peptide-mediated one-step purification and immobilization of α-L-rhamnosidase from Bacteroides thetaiotaomicron for direct biotransformation from epimedin C to icariin" @default.
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- W4295957531 doi "https://doi.org/10.1016/j.enzmictec.2022.110131" @default.
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