Enzymatic degradation of ginkgolic acids by laccase immobilized on core/shell Fe 3 O 4 /nylon composite nanoparticles using novel coaxial electrospraying process

• Published in: International journal of biological macromolecules 2021-03, Vol.172, p.270
• Main Authors: Chen, Hung-Yueh, Ting, Yuwen, Kuo, Hsing-Chun, Hsieh, Chang-Wei, Hsu, Hsien-Yi, Wu, Chun-Nan, Cheng, Kuan-Chen
• Format: Article
• Language: English
• Subjects: Cross-Linking Reagents - chemistry; Electrochemical Techniques; Enzymes, Immobilized - chemistry; Enzymes, Immobilized - isolation & purification; Equipment Reuse; Ferrosoferric Oxide - chemistry; Fungal Proteins - chemistry; Fungal Proteins - isolation & purification; Ginkgo biloba - chemistry; Glutaral - chemistry; Hydrolysis; Kinetics; Laccase - chemistry; Laccase - isolation & purification; Magnetite Nanoparticles - chemistry; Magnetite Nanoparticles - ultrastructure; Nylons - chemistry; Plant Extracts - chemistry; Plant Leaves - chemistry; Polyporaceae - chemistry; Polyporaceae - enzymology; Salicylates - chemistry
• ISSN: 1879-0003

Enzyme immobilization can increase enzyme reusability to reduce cost of industrial production. Ginkgo biloba leaf extract is commonly used for medical purposes, but it contains ginkgolic acid, which has negative effects on human health. Here, we report a novel approach to solve the problem by degrading the ginkgolic acid with immobilized-laccase, where core/shell composite nanoparticles prepared by coaxial electrospraying might be first applied to enzyme immobilization. The core/shell Fe O /nylon 6,6 composite nanoparticles (FNCNs) were prepared using one-step coaxial electrospraying and can be simply recovered by magnetic force. The glutaraldehyde-treated FNCNs (FNGCNs) were used to immobilize laccase. As a result, thermal stability of the free laccase was significantly improved in the range of 60-90 °C after immobilization. The laccase-immobilized FNGCNs (L-FNGCNs) were applied to degrade the ginkgolic acids, and the rate constants (k) and times (τ ) were ~0.02 min and lower than 39 min, respectively, showing good catalytic performance. Furthermore, the L-FNGCNs exhibited a relative activity higher than 0.5 after being stored for 21 days or reused for 5 cycles, showing good storage stability and reusability. Therefore, the FNGCNs carrier was a promising enzyme immobilization system and its further development and applications were of interest.