TY - JOUR
T1 - Sustainable chiral separation using chitin nanofibrous microspheres for enhanced catalysis and reusability
AU - Wang, Huiqing
AU - Zhou, Xiaoyue
AU - Wu, Ke
AU - Tang, Longxiang
AU - Duan, Xiaorui
AU - Li, Wei
N1 - Publisher Copyright:
© 2025 Elsevier Ltd
PY - 2025/12/15
Y1 - 2025/12/15
N2 - The inefficiency and instability of free enzymes in the chiral separation of high-purity D-pantolactone, a crucial intermediate in vitamin B5 synthesis, pose significant challenges, with nanostructured materials offering promising solutions. In this study, D-Lactonohydrolase (D-lacs) was immobilized in crab-derived chitin nanofibrous microspheres (ChNFM), achieving high enzyme loading and excellent reusability. By combining physical absorption and chemical cross-linking, stable immobilization of D-lacs was realized. The enzyme loading capacity of D-Lacs on ChNFM was gradually increased as the particle size of ChNFM decreased. Batch hydrolysis using D-Lacs@ChNFM was conducted for 50 consecutive times, maintaining an average degree of hydrolysis of 30.0%, with stable enzyme activity throughout. Compared to the commercial immobilized D-lacs carrier, D-Lacs@ChNFM exhibited superior hydrolytic efficiency, higher batch stability, and excellent biodegradability. This work highlights the potential of ChNFM as an efficient and eco-friendly carrier for enzyme immobilization, offering a promising platform for scalable DL-pantolactone separation and greener vitamin B5 production.
AB - The inefficiency and instability of free enzymes in the chiral separation of high-purity D-pantolactone, a crucial intermediate in vitamin B5 synthesis, pose significant challenges, with nanostructured materials offering promising solutions. In this study, D-Lactonohydrolase (D-lacs) was immobilized in crab-derived chitin nanofibrous microspheres (ChNFM), achieving high enzyme loading and excellent reusability. By combining physical absorption and chemical cross-linking, stable immobilization of D-lacs was realized. The enzyme loading capacity of D-Lacs on ChNFM was gradually increased as the particle size of ChNFM decreased. Batch hydrolysis using D-Lacs@ChNFM was conducted for 50 consecutive times, maintaining an average degree of hydrolysis of 30.0%, with stable enzyme activity throughout. Compared to the commercial immobilized D-lacs carrier, D-Lacs@ChNFM exhibited superior hydrolytic efficiency, higher batch stability, and excellent biodegradability. This work highlights the potential of ChNFM as an efficient and eco-friendly carrier for enzyme immobilization, offering a promising platform for scalable DL-pantolactone separation and greener vitamin B5 production.
KW - Chitin nanofibrous microspheres
KW - D-Lactonohydrolase
KW - Enzyme immobilization
UR - https://www.scopus.com/pages/publications/105016015320
U2 - 10.1016/j.carbpol.2025.124289
DO - 10.1016/j.carbpol.2025.124289
M3 - Article
AN - SCOPUS:105016015320
SN - 0144-8617
VL - 370
JO - Carbohydrate Polymers
JF - Carbohydrate Polymers
M1 - 124289
ER -