Immobilization of trypsin in polycation-polyanion complexes

被引：25

作者：

Dautzenberg, H ^{[1
]}

Karibyants, N ^{[1
]}

Zaitsev, SY ^{[1
]}

机构：

[1] RUSSIAN ACAD SCI,INST BIOORGAN CHEM,MOSCOW 117871,RUSSIA

来源：

MACROMOLECULAR RAPID COMMUNICATIONS | 1997年 / 18卷 / 02期

关键词：

D O I：

10.1002/marc.1997.030180216

中图分类号：

O63 [高分子化学（高聚物）];

学科分类号：

070305 ; 080501 ; 081704 ;

摘要：

Trypsin was immobilized in quasi-soluble polyanion-polycation complexes with retention of the enzyme activity. The activity of the immobilized enzyme strongly depends on pH of the prepared solution, Composition, relative concentrations and molar masses of the polyelectrolytes. The highest activity of trypsin (about 93%) was found in the case of the complexes Na-poly(styrenesulfonate)-poly (diallyldimethylammonium chloride): trypsin = 10:1, prepared at pH 3.0, with high molar mass of the polyanion (about one million). This method can be proposed for immobilization of various serine proteases.

引用

页码：175 / 182

页数：8

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