Amino-silane modified superparamagnetic particles with surface-immobilized enzyme

Hideki Kobayashi, Tadashi Matsunaga

研究成果: Article

48 引用 (Scopus)

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Microfine magnetic particles of magnetite with a mean diameter of 10-15 nm, which is in the range of superparamagnetism, were prepared by coprecipitation from ferrous and ferric electrolyte solution and applied to the enzyme immobilization support. The surface of the particles was treated by a series of amino-functional silane coupling agents capable of covalently bonding with enzyme. A protease, thermolysin, was immobilized on the particles and transferred to ethyl acetate solution containing N-Cbz-l-aspartic acid and l-phenylalanine methyl ester. The dipeptide, aspartame precursor synthetic reaction was then carried out. Higher enzyme activity was found when the silane coupling agents with long spacer arms between the silane functionality and amino functionality were used such as N-(6-aminohexyl)-3-aminopropyltrimethyoxysilane, compared to conventional 3-aminopropyltrichoxysilane. Magnetic recovery of the immobilized enzyme was also demonstrated upon the application of an external magnetic field.

元の言語English
ページ(範囲)505-511
ページ数7
ジャーナルJournal of Colloid and Interface Science
141
発行部数2
DOI
出版物ステータスPublished - 1991
外部発表Yes

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ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Biomaterials
  • Surfaces, Coatings and Films
  • Colloid and Surface Chemistry

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