| Autor: |
Salgın S; Department of Chemical Engineering, Faculty of Engineering, Sivas Cumhuriyet University, Sivas, Turkey., Çakal M; Department of Chemical Engineering, Faculty of Engineering, Sivas Cumhuriyet University, Sivas, Turkey., Salgın U; Department of Chemical Engineering, Faculty of Engineering, Sivas Cumhuriyet University, Sivas, Turkey. |
| Jazyk: |
angličtina |
| Zdroj: |
Preparative biochemistry & biotechnology [Prep Biochem Biotechnol] 2020; Vol. 50 (2), pp. 148-155. Date of Electronic Publication: 2019 Oct 24. |
| DOI: |
10.1080/10826068.2019.1679178 |
| Abstrakt: |
In this study, the non-magnetic and the magnetic cross-linked enzyme aggregates (CLEAs) from Candida rugosa lipase were synthesized to catalyze the kinetic resolution reaction of naproxen methyl ester (NME). Magnetic iron oxide nanoparticles (MIONPs) were produced through co-precipitation method and their surfaces were modified by silanization reaction. The MIONPs were used as a platform to synthesize the magnetic CLEAs (M-CLEAs). The biocatalysts and MIONPs synthesized were characterized by FTIR spectroscopy and SEM analysis. The kinetic resolution of racemic NME was studied in aqueous buffer solution/isooctane biphasic system to compare the performance of M-CLEAs and CLEAs. The effects of reaction parameters such as temperature, pH, stirring rate on the enantiomeric excess of the substrate (ee s %) were investigated in a batch reactor system. The activity recovery of CRL enzyme in CLEAs was higher than M-CLEAs. Compared with M-CLEAs, CLEAs biocatalysts had previously reached ee s % values. Although both biocatalysts showed similar cavity structure from SEM analysis, the lower performance of M-CLEAs may be due to the different microenvironments of M-CLEAs from CLEAs. However, the reusability performance of M-CLEAs was higher than that of CLEAs. The optimal reaction conditions for M-CLEAs and CLEAs were found to be 37 °C, pH 7.5, and 300 rpm. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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