A Modified Simulated Moving Bed Separating α-Arbutin from a Ternary Mixture with High Purity and High Productivity
α-Arbutin, obtained from the related fermentation processes, has several exceptional physiological functions, making it highly suitable for applications in the fine chemical and pharmaceutical industries. This has sparked interest in the production of high-purity α-arbutin in those industries. To address this issue, this study developed a chromatographic method to separate α-arbutin with high purity and high productivity. As a first step for this work, the optimal adsorbent for the separation of α-arbutin was identified through a comprehensive assessment of the molecular dimension, electrostatic potential distribution, binding energy, and resolution. For the chosen K-type resin, the frontal analysis experiments were conducted to determine the intrinsic parameters of the components, which were used in the optimal design of the α-arbutin separation process employing a simulated moving bed (SMB) method. Finally, the validity of the designed SMB process was investigated with the model simulation, followed by continuous α-arbutin separation experiments using self-assembled SMB equipment, which confirmed that the process developed in this study (column distribution 1–1–2–1–2, switching time 9 min; flow rates for the respective zones were QI = 5.18 mL/min, QII = 4.36 mL/min, QIII = 4.75 mL/min, QIV = 5.05 mL/min, QV = 5.87 mL/min) was capable of separating α-arbutin from feed solution with purity over 98% and the recovery rate exceeding 93%. These findings are beneficial in enabling the large-scale production of high-purity α-arbutin.
Authors
- Yuhao Liu (ORCID: https://orcid.org/0009-0005-3718-7272)
- Qi Wei (ORCID: https://orcid.org/0000-0002-5322-3692)
- Junwei Zhang (ORCID: https://orcid.org/0000-0002-4220-4496)
Institutions
- Jiangnan University (CN)
- Ministry of Education of the People's Republic of China (CN)
Publication Details
- Journal
- Industrial & Engineering Chemistry Research
- Published
- 2025-07-16
- DOI
- https://doi.org/10.1021/acs.iecr.5c00881
- Primary Topic
- Protein purification and stability
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Natural Science Foundation of China
- National Key Research and Development Program of China