Immobilization of D-allulose 3-epimerase into magnetic metal-organic framework nanoparticles for efficient biocatalysis
- PMID: 35748959
- DOI: 10.1007/s11274-022-03330-4
Immobilization of D-allulose 3-epimerase into magnetic metal-organic framework nanoparticles for efficient biocatalysis
Abstract
D-allulose is a rare low-calorie sugar that has many fundamental biological functions. D-allulose 3-epimerase from Agrobacterium tumefaciens (AT-DAEase) catalyzes the conversion of D-fructose to D-allulose. The enzyme has attracted considerable attention because of its mild catalytic properties. However, the bioconversion efficiency and reusability of AT-DAEase limit its industrial application. Magnetic metal-organic frameworks (MOFs) have uniform pore sizes and large surface areas and can facilitate mass transport and enhance the capacity for enzyme immobilization. Here, we successfully encapsulated cobalt-type AT-DAEase into the cobalt-based magnetic MOF ZIF-67@Fe3O4 using a self-assembly strategy. We confirmed the immobilization of enzyme AT-DAEase and characterized the enzymatic properties of the MOF-immobilized AT-DAEase@ZIF-67@Fe3O4. The AT-DAEase@ZIF-67@Fe3O4 nanoparticles had higher catalytic activity (65.1 U mg-1) and bioconversion ratio (38.1%) than the free AT-DAEase. The optimal conditions for maximum enzyme activity of the AT-DAEase@ZIF-67@Fe3O4 nanoparticles were 55 °C and pH 8.0, which were significantly higher than those of the free AT-DAEase (50 °C and pH 7.5). The AT-DAEase@ZIF-67@Fe3O4 nanoparticles displayed significantly improved thermal stability and excellent recycling performance, with 80% retention of enzyme activity at a temperature range of 45-70 °C and > 45% of its initial activity after eight cycles of enzyme use. The AT-DAEase@ZIF-67@Fe3O4 nanoparticles have great potential for large-scale industrial preparation of D-allulose by immobilizing cobalt-type AT-DAEase into magnetic MOF ZIF-67@Fe3O4.
Keywords: D-allulose; D-allulose 3-epimerase; D-fructose; Immobilization; Magnetic metal–organic frameworks.
© 2022. The Author(s), under exclusive licence to Springer Nature B.V.
References
-
- Dedania SR, Patel MJ, Patel DM, Akhani RC, Patel DH (2017) Immobilization on graphene oxide improves the thermal stability and bioconversion efficiency of D-psicose 3-epimerase for rare sugar production. Enzyme Microb Technol 107:49–56. https://doi.org/10.1016/j.enzmictec.2017.08.003 - DOI - PubMed
-
- Dicosimo R, Mcauliffe JC, Poulose AJ, Bohlmann G (2013) Industrial use of immobilized enzymes. Chem Soc Rev 42(15):6437–6474. https://doi.org/10.1039/C3CS35506C - DOI - PubMed
-
- Franssen MC, Steunenberg P, Scott EL, Zuilhof H, Sanders JP (2013) Immobilised enzymes in biorenewables production. Chem Soc Rev 42(15):6491–6533. https://doi.org/10.1039/C3CS00004D - DOI - PubMed
-
- Hammes GG, Wu CW (1971) Regulation of enzyme activity. The activity of enzymes can be controlled by a multiplicity of conformational equilibria. Science 172(3989):1205–1211. https://doi.org/10.1126/science.172.3989.1205 - DOI - PubMed
-
- Itoh H, Okaya H, Khan AR, Tajima S, Hayakawa S, Izumori K (1994) Purification and characterization of D-tagatose 3-epimerase from Pseudomonas sp. ST-24. Biosci Biotech Bioch 58(12):2168–2171. https://doi.org/10.1271/bbb.58.2168 - DOI
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources