Medline/PubMed Citation | Related Articles in PubMed | Download to Citation Manager

Biotechnology and Applied Biochemistry (2003) 38, (137–141) (Printed in Great Britain)

PDF

Legacy HTML

A novel method for the immobilization of tyrosinase to enhance stability

Neeru Munjal Sharma*¹, Sushil Kumar* and Suriender Kumar Sawhney†

*Division of Biochemistry, SKUAST-J, R.S. Pura, Jammu, India, and †Division of Biochemistry, College of Basic Sciences and Humanities, CCSHAU, Hisar, Haryana, India

Key words: L-DOPA, polyphenoloxidase, reactor.

Abbreviations used: L-DOPA, 3,4-dihydroxyphenylalanine; GE, gelatin-entrapped; FEAGE, Fuller's-earth-adsorbed gelatin-entrapped.

¹To whom correspondence should be addressed (e-mail ns_biochemist@yahoo.com).

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 40 °C 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).

Received 25 November 2002/24 March 2003; accepted 21 May 2003

Published as Immediate Publication 21 May 2003, DOI 10.1042/BA20020112

© 2003 Portland Press Ltd