Immobilization of Agrobacterium tumefaciensd-psicose 3-epimerase onto titanium dioxide for bioconversion of rare sugar.
Enzyme Microb Technol
; 140: 109605, 2020 Oct.
Article
em En
| MEDLINE
| ID: mdl-32912676
ABSTRACT
d-Psicose (d-ribo-2-hexulose or d-allulose) is the Carbon-3 epimer of d-fructose sugar and considered as an unnatural (rare) sugar found in low amount in nature. It has about 70% of the relative sweetness but 0.3% of the energy of sucrose, which is suggested as the most suitable sucrose substitute for food additives. Enzymatic biosynthesis using ketose 3-epimerases is a necessary procedure for the production of d-Psicose from d-fructose. However, significant drawbacks in the application of ketose 3-epimerases at industrial scale observe lower thermal stability as well as bioconversion efficiency, reusability and recovery of the enzyme. We have attempted immobilization of ketose 3-epimerases from Agrobacterium tumefaciens (agtu) d-psicose 3-epimerase (DPEase) on titanium dioxide. Further, Scanning electron microscopy (SEM), inverted microscopy, Fourier transform infrared spectroscopy (FTIR) and UV-vis spectroscopy showed that the enzyme was successfully immobilized on the titanium dioxide (TiO2) surface. Titanium dioxide immobilized agtu-DPEase (TiO2-agtu-DPEase) shows pH optima at 6.0 and 60⯰C as a higher working temperature. TiO2-agtu-DPEase showed a half-life of 180â¯min at 60⯰C, which is higher as compared to Agrobacterium tumefaciens (agtu) DPEase (3.99â¯min at 50⯰C). At equilibrium, 3664 (D-psicose d-fructose), the bioconversion efficiency was accounted for titanium dioxide immobilized DPEase, which is higher than the agtu-DPEase. Titanium dioxide immobilized DPEase showed bioconversion efficiency up to 9 cycles of reusability.
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MEDLINE
Assunto principal:
Titânio
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Carboidratos Epimerases
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Agrobacterium tumefaciens
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Enzimas Imobilizadas
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article