Construction and Catalytic Performances of Fe-aminoclay Nanostructured Lipase †

doi:10.7503/cjcu20190444

Abstract

Abstract:

Lipase from Aspergillus oryzae was immobilized on Fe-aminoclay support via 1-(3-dimethylami-nopropyl)-3-ethylcarbodiimide hydrochloride(EDC) as covalent crosslinking agent. The nanocomposite structure of immobilized lipase(Feclay-lipase) was characterized by means of X-ray diffraction(XRD), transmission electron microscope(TEM) and Fourier transform infrared spectroscopy(FTIR). The enzymatic properties of free lipase and Feclay-lipase were studied by enzymatic kinetics. The results showed that the optimal immobilization efficiency of Feclay-lipase was 82.88%, immobilization capacity was 414.4 mg/g support, and the enzyme activity was 28.24 U/mg, which was three times higher than that of free lipase(8.21 U/mg). The optimum reaction temperature of Feclay-lipase increased from 45 ℃ to 55 ℃, the optimum pH shifted to alkalinity, and the catalytic activity of Feclay-lipase did not decrease significantly after storage at 4 ℃ for one month.

Key words: Fe-aminoclay, Lipase, Nanostructured support, Enzyme immobilization, Nanobiocatalyst

CLC Number:

O643.3

TrendMD:

Xiaoyu FAN,Ke WANG,Shiyong SUN,Biaobiao MA,Rui LÜ. Construction and Catalytic Performances of Fe-aminoclay Nanostructured Lipase ^†[J]. Chem. J. Chinese Universities, 2019, 40(12): 2512.

Figures/Tables 10

Fig.1 XRD patterns(A) and FTIR spectra(B) of Fe-aminoclay and Feclay-lipase with various lipase loadings (A) a. Fe-aminoclay; b. Feclay-10lipase; c. Feclay-50lipase; d. Feclay-100lipase; e. Feclay-150lipase; f. Feclay-200lipase. (B) a. Fe-aminoclay; b. lipase; c. Feclay-10lipase; d. Feclay-50lipase; e. Feclay-100lipase; f. Feclay-150lipase; g. Feclay-200lipase.

Fig.2 Schematic diagram of Fe-aminoclay dispersed in water and lipase immobilized on Fe-aminoclay

Fig.3 Zeta potentials(A) and average particle sizes(B) of Fe-aminoclay, lipase and Feclay-lipase a. Fe-aminoclay; b. lipase; c. Feclay-10lipase; d. Feclay-50lipase; e. Feclay-100lipase; f. Feclay-150lipase; g. Feclay-200lipase.

Fig.4 Photographs of as-prepared Fe-aminoclay powder(A) and Fe-aminoclay(a), Feclay-150lipase(b) and lipase(c) dispersed in water(B)

Fig.5 TEM images of Fe-aminoclay(A) and Feclay-lipase(B), SEM images of Fe-aminoclay(C), Feclay-150lipase(D) and the selected area in (D) image(E) and contact angle images of Fe-aminoclay(F), lipase(G) and Feclay-150lipase(H)

Fig.6 Effect of lipase loading on the catalytic acti-vity and immobilization efficiency for Feclay-lipase

Fig.7 Effect of reaction temperature(A) and pH(B) on catalytic activity of free lipase and Feclay-150lipase

Fig.8 Thermal stability at 60 ℃(A) and storage stability at 4 ℃(B) of free lipase and Feclay-150lipase

Fig.9 Lineweaver-Burk plots of the free lipase and Feclay-lipase(A), absorbance at the peak position for p-NP(410 nm) as a function of time for two different catalytic systems(B)

Sample	R²	K_m/mmol	V_max/(mmol·mL^-1·min^-1)
Free lipase	0.997	5.35	99
Feclay-50lipase	0.996	6.98	217.39
Feclay-150lipase	0.996	7.84	175.42

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