Immobilization of laccase via cross-linked enzyme aggregates prepared using genipin as a natural cross-linker
Autor: | Kyeong Keun Oh, Dahun Jung, Jiyeon Hong, Saerom Park, Sang Hyun Lee, Yujin Oh |
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Rok vydání: | 2021 |
Předmět: |
Cross-linked enzyme aggregate
02 engineering and technology Biochemistry Polyporaceae 03 medical and health sciences chemistry.chemical_compound Structural Biology Enzyme Stability Iridoids Thermal stability Bovine serum albumin Molecular Biology 030304 developmental biology Trametes versicolor Trametes Laccase 0303 health sciences biology Chemistry Temperature Substrate (chemistry) Serum Albumin Bovine General Medicine Hydrogen-Ion Concentration Enzymes Immobilized 021001 nanoscience & nanotechnology biology.organism_classification Kinetics Cross-Linking Reagents Glutaral Genipin biology.protein Glutaraldehyde 0210 nano-technology Nuclear chemistry |
Zdroj: | International Journal of Biological Macromolecules. 169:541-550 |
ISSN: | 0141-8130 |
DOI: | 10.1016/j.ijbiomac.2020.12.136 |
Popis: | Genipin is a nontoxic natural cross-linker that was successfully used to prepare cross-linked enzyme aggregates (CLEAs) of Trametes versicolor laccase. The recovered activity of CLEAs was influenced by the co-solvent type, genipin concentration, cross-linking time, preparation pH, and bovine serum albumin (BSA; amino group feeder) concentration. The characteristics of CLEAs prepared using genipin under optimal conditions (genipin-BSA-CLEAs) were compared with those of typical CLEAs prepared using glutaraldehyde or dextran polyaldehyde. Genipin-BSA-CLEAs were nano-sized (average diameter, approximately 700 nm), had a ball-like shape, showed a narrow size distribution, and exhibited the highest substrate affinity among the prepared CLEAs. The thermal stability of genipin-BSA-CLEAs was 6.8-fold higher than that of free laccase, and their pH stability was also much higher than that of free laccase in the tested range. Additionally, genipin-BSA-CLEAs retained 85% of their initial activity after 10 cycles of reuse. Particularly, genipin-BSA-CLEAs showed higher thermal and pH stability than CLEAs that were cross-linked using glutaraldehyde. Therefore, genipin represents an alternative to toxic compounds such as glutaraldehyde during cross-linking to prepare CLEAs. |
Databáze: | OpenAIRE |
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