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Dergiler / Turkish Journal of Chemistry / 2014 / Cilt: 38 - Sayı: 1

Immobilized metal ion affinity nanospheres for a-amylase immobilization

Tülden KALBURCU
Münire Nalan TÜZMEN
Sayfa
28–40
Yayın Tarihi
2014-05-18
DOI
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It was also observed that p(HEMA-MAT)-Ni2+ nanospheres can be repeatedly used for a-amylase immobilization.

📌 3 Maddede Bu Makale

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Amaç & Hipotez:Immobilized metal chelate affinity chromatography (IMAC) support was practiced for a-amylase immobilization.
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Temel Bulgular & Veri:Poly(hydroxyethylmethacrylate-methacryloylamidotryptophan)-Ni2+ [p(HEMA-MAT)-Ni2+] nanospheres, average diameter 100 nm, were produced by surfactant free emulsion polymerization.
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Sonuç & Katkı:It was also observed that p(HEMA-MAT)-Ni2+ nanospheres can be repeatedly used for a-amylase immobilization.
🔬Tür:Araştırma Makalesi
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:a-Amylase · nanospheres · IMAC

Özet

Immobilized metal chelate affinity chromatography (IMAC) support was practiced for a-amylase immobilization. Poly(hydroxyethylmethacrylate-methacryloylamidotryptophan)-Ni2+ [p(HEMA-MAT)-Ni2+] nanospheres, average diameter 100 nm, were produced by surfactant free emulsion polymerization. Characterizations of p(HEMA-MAT)-Ni2+ nanospheres were carried out by Fourier transform infrared (FTIR) spectroscopy and scanning electron microscope (SEM). In addition, average particle size, size distribution, and surface charge were specified. The amount of N-methacryloylamidotryptophan (MAT) incorporated to polymer was determined as 1.95 mmol/g polymers by using nitrogen stoichiometry. The specific surface areas of poly(hydroxyethylmethacrylate) [p(HEMA)] and p(HEMA-MAT) nanospheres were calculated as 1856 m2/g and 1914 m2/g, respectively. Protein adsorption increased with increasing initial protein concentration and maximum a-amylase adsorption on p(HEMA-MAT)-Ni2+ nanospheres was observed at pH 4.0. Both free and immobilized a-amylase showed pH optimum at pH 7.0. It was determined that the immobilized a-amylase had better thermostability than the free one. Immobilization of the enzyme did not significantly change the kinetic parameters. The storage stability of a-amylase increased upon immobilization. It was also observed that p(HEMA-MAT)-Ni2+ nanospheres can be repeatedly used for a-amylase immobilization.

Abstract

Immobilized metal chelate affinity chromatography (IMAC) support was practiced for a-amylase immobilization. Poly(hydroxyethylmethacrylate-methacryloylamidotryptophan)-Ni2+ [p(HEMA-MAT)-Ni2+] nanospheres, average diameter 100 nm, were produced by surfactant free emulsion polymerization. Characterizations of p(HEMA-MAT)-Ni2+ nanospheres were carried out by Fourier transform infrared (FTIR) spectroscopy and scanning electron microscope (SEM). In addition, average particle size, size distribution, and surface charge were specified. The amount of N-methacryloylamidotryptophan (MAT) incorporated to polymer was determined as 1.95 mmol/g polymers by using nitrogen stoichiometry. The specific surface areas of poly(hydroxyethylmethacrylate) [p(HEMA)] and p(HEMA-MAT) nanospheres were calculated as 1856 m2/g and 1914 m2/g, respectively. Protein adsorption increased with increasing initial protein concentration and maximum a-amylase adsorption on p(HEMA-MAT)-Ni2+ nanospheres was observed at pH 4.0. Both free and immobilized a-amylase showed pH optimum at pH 7.0. It was determined that the immobilized a-amylase had better thermostability than the free one. Immobilization of the enzyme did not significantly change the kinetic parameters. The storage stability of a-amylase increased upon immobilization. It was also observed that p(HEMA-MAT)-Ni2+ nanospheres can be repeatedly used for a-amylase immobilization.

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Bu Makaleye Atıf Yap

KALBURCU, T., TÜZMEN, M. N. (2014). Immobilized metal ion affinity nanospheres for a-amylase immobilization. Turkish Journal of Chemistry, Cilt: 38 - Sayı: 1, 28–40. https://ajindex.com/articles/184717

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