IMMOBILIZATION OF LACCASE FROM PHLEBIA-RADIATA ON CONTROLLED POROSITY GLASS

被引：57

作者：

ROGALSKI, J ^{[1
]}

JOZWIK, E ^{[1
]}

HATAKKA, A ^{[1
]}

LEONOWICZ, A ^{[1
]}

机构：

[1] HELSINKI UNIV, DEPT APPL CHEM & MICROBIOL, SF-00014 HELSINKI, FINLAND

来源：

JOURNAL OF MOLECULAR CATALYSIS A-CHEMICAL | 1995年 / 95卷 / 01期

关键词：

CONTROLLED POROSITY GLASS; ENZYMES; IMMOBILIZATION; INHIBITORS; KINETICS; LACCASE; ORGANIC SOLVENTS; PHLEBIA RADIATA; PROTEIN PURIFICATION;

D O I：

10.1016/1381-1169(94)00165-0

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Laccase from the white-rot fungus Phlebia radiata was immobilized on glass beads which were activated by gamma-aminopropyl-triethoxysilane. 98% of the protein and 96% of the laccase activity were coupled to the support. The final preparation contained ca. 1 mg of protein per gram of glass beads. The activity of the immobilized enzyme retained after two weeks preservation at + 4 degrees C was 100% and at + 25 degrees C over 90%. The activity in the presence of organic solvents was rather similar irrespective of the form of the enzyme, free or bound. However, the catalytic activity of the immobilized laccase was less vulnerable against inhibitors such as Cu-chelators and 2,6-dimethoxy-1,4-benzoquinone.

引用

页码：99 / 108

页数：10