| Autor: |
Sharma NM; Division of Biochemistry, SKUAST-J, R.S. Pura, Jammu, India. ns_biochemist@yahoo.com, Kumar S, Sawhney SK |
| Jazyk: |
angličtina |
| Zdroj: |
Biotechnology and applied biochemistry [Biotechnol Appl Biochem] 2003 Oct; Vol. 38 (Pt 2), pp. 137-41. |
| DOI: |
10.1042/BA20020112 |
| Abstrakt: |
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 degrees 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). |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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