Kaetsu I, Kumakura M, Yoshida M
Biotechnol Bioeng. 1979 May;21(5):863-73. doi: 10.1002/bit.260210509.
Enzyme immobilization was studied by means of radiation-induced polymerization of hydrophobic glass-forming monomers at low temperatures. The polymerized hydrophobic composite was generally obtained in microspheric form. Enzymatic activity showed little decrease with repeated use in these systems. The particle size of the microsphere increased with increasing monomer concentration, and activity yield had a maximum at an optimum monomer concentration. Immobilization by copolymerization of hydrophilic and hydrophobic comonomers was also investigated and a maximum activity yield was found at a certain monomer concentration. A model scheme for immobilization at low temperatures was proposed and discussed.
通过在低温下辐射诱导疏水性玻璃形成单体聚合来研究酶固定化。聚合后的疏水性复合材料通常以微球形式获得。在这些系统中,酶活性在重复使用时几乎没有下降。微球的粒径随着单体浓度的增加而增大,活性产率在最佳单体浓度时达到最大值。还研究了亲水性和疏水性共聚单体的共聚固定化,发现在一定单体浓度下活性产率最高。提出并讨论了低温固定化的模型方案。