Enhanced Performance of Immobilized Xylanase/Filter Paper-ase on a Magnetic Chitosan Support
| Autor: | Teresita Arredondo-Ochoa, Monserrat Escamilla-García, Carlos Regalado, Jorge Gracida, Aldo Amaro-Reyes, Blanca E. García-Almendárez, Azariel Díaz-Hernández |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Immobilized enzyme
02 engineering and technology lcsh:Chemical technology 01 natural sciences Catalysis Chitosan lcsh:Chemistry Hydrolysis chemistry.chemical_compound catalytic efficiency Thermal stability lcsh:TP1-1185 Physical and Theoretical Chemistry nanobiocatalyst Filter paper 010405 organic chemistry Chemistry 021001 nanoscience & nanotechnology 0104 chemical sciences lcsh:QD1-999 Yield (chemistry) hydrolytic enzymes Xylanase Genipin nanoparticles 0210 nano-technology Nuclear chemistry |
| Zdroj: | Catalysts, Vol 9, Iss 11, p 966 (2019) |
| ISSN: | 2073-4344 |
| Popis: | Enzyme immobilization on different supports has emerged as an efficient and cost-effective tool to improve their stability and reuse capacity. This work aimed to produce a stable immobilized multienzymatic system of xylanase and filter paper-ase (FPase) onto magnetic chitosan using genipin as a cross-linking agent and to evaluate its biochemical properties and reuse capacity. A mixture of chitosan magnetic nanoparticles, xylanase, and FPase was covalently bonded using genipin. Immobilization yield and efficiency were quantified. The activity of free and immobilized enzymes was quantified at different values of pH, temperature, substrate concentration (Km and Vmax), and reuse cycles. The immobilization yield, immobilization efficiency, and activity recovery were 145.3% ± 3.06%, 14.8% ± 0.81%, and 21.5% ± 0.72%, respectively, measured as the total hydrolytic activity. Immobilization confers resistance to acidic/basic conditions and thermal stability compared to the free form. Immobilization improved 3.5-fold and 78-fold the catalytic efficiency (Kcat/Km) of the xylanase and filter paper-ase activities, while immobilized xylanase and FPase could be reused for 34 min and 43 min, respectively. Cross-linking significantly improved the biochemical properties of immobilized enzymes, combined with their simplicity of reuse due to the paramagnetic property of the support. Multienzyme immobilization technology is an important issue for industrial applications. |
| Databáze: | OpenAIRE |
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