A novel method for the immobilization of tyrosinase to enhance stability

Neeru Munjal Sharma, Sushil Kumar, Suriender Kumar Sawhney

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

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).

Original languageEnglish (US)
Pages (from-to)137-141
Number of pages5
JournalBiotechnology and Applied Biochemistry
Volume38
Issue number2
DOIs
StatePublished - Oct 2003
Externally publishedYes

Keywords

  • L-DOPA
  • Polyphenoloxidase
  • Reactor

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Molecular Medicine
  • Biomedical Engineering
  • Applied Microbiology and Biotechnology
  • Drug Discovery
  • Process Chemistry and Technology

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