A novel method for the immobilization of tyrosinase to enhance stability

被引：13

作者：

Sharma, NM ^{[1
]}

Kumar, S

Sawhney, SK

机构：

[1] RS Pura, SKUAST J, Div Biochem, Jammu, India

[2] CCSHAU, Coll Basic Sci & Humanities, Div Biochem, Hisar, Haryana, India

来源：

BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY | 2003年 / 38卷

关键词：

L-DOPA; polyphenoloxidase; reactor;

D O I：

10.1042/BA20020112

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A new method of tyrosinase immobilization by Fuller's-earth adsorption followed by entrapment in gelatin has been developed with 98% activity immobilization yield. An appreciable increase in operational and thermal stability was observed for FEAGE (Fuller's earth-adsorbed gelatin-entrapped) tyrosinase compared with GE (gelatin-entrapped) native enzyme. FEAGE tyrosinase could be used repeatedly after intermittent storage and retained 70% of its initial activity after eight cycles. The half-life of the GE enzyme at 40degreesC was less than 2 h, whereas the FEAGE enzyme retained about 75 % of its initial activity after 2 h. Taken together our data demonstrate clearly that the technique of immobilizing tyrosinase via adsorption followed by entrapment appears promising and is hence recommended for tyrosinase immobilization for commercial production Of L-DOPA (3,4-dihydroxyphenylalanine).

引用

页码：137 / 141

页数：5

共 19 条

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