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 language | English (US) |
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Pages (from-to) | 137-141 |
Number of pages | 5 |
Journal | Biotechnology and Applied Biochemistry |
Volume | 38 |
Issue number | 2 |
DOIs | |
State | Published - Oct 2003 |
Externally published | Yes |
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