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2-(N-morpholine) ethanesulfonic acid(cas 4432-31-9, pH 6.2) buffer

In the presence of MES(4432-31-9), pH 6.2, N-hydroxysuccinimide (NHS) and 1- (3-dimethylaminopropyl) (EDC HC1) was used as a crosslinking agent to activate the carrier material. Candida.sp99-125 lipase was cross-linked to magnetized multi-walled carbon nanotubes in phosphate buffer (PBS, pH 8.0) (Magnetic-MWCNTs). The vector and immobilized enzyme were characterized by UV, XRD, XPS, Raman spectrum, IR and FTIR, TEM. The maximum loading of magnetized immobilized enzyme was 1.45 mg lipase / mg. Magnetic-MWCNTs by BCA method. Determination of relative enzyme activity of immobilized enzyme according to copper soap method. The effect of enzymatic resolution of α-phenylethyl alcohol in the two phases of n-heptane, ionic liquid and n-heptane-ionic liquid was investigated in a variety of aspects using vinyl acetate as the acyl donor. The corresponding enantiomeric excess e.e and substrate conversion C were calculated by high performance liquid chromatography (HPLC) to quantitatively analyze the changes in substrate and product of the reaction process. 

The results show that in the n-heptane, the application of magnetized solid enzyme, the reaction temperature of 55 ℃ conversion rate of up to 50%, e.e.s reached 98.5%. The optimum reaction temperature of free enzyme and magnetized solid enzyme in n - heptane - ionic liquid two - phase system is 55 ℃. At 50 ℃ -60 ℃, the two-phase reaction system is more effective than single-phase reaction system. The results also showed that the magnetization immobilized enzyme had better anti - ultrasound ability than free enzyme, and the magnetization separation effect was good.



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