title: A novel method for the immobilization of tyrosinase to enhance stability.
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 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).
authors.affiliation: Division of Biochemistry, SKUAST-J, R.S. Pura, Jammu, India. ns_biochemist@yahoo.com
authors.forename: Neeru Munjal
authors.initials: NM
authors.lastname: Sharma
authors.forename: Sushil
authors.initials: S
authors.lastname: Kumar
authors.forename: Suriender Kumar
authors.initials: SK
authors.lastname: Sawhney
mesh_terms: D000327:Adsorption; D000364:Agaricus / Q000201:enzymology; D001709:Biotechnology / Q000379:methods*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D014442:Monophenol Monooxygenase / Q000737:chemistry*; D013696:Temperature
chemical_list: D004800:Enzymes, Immobilized; D014442:Monophenol Monooxygenase