ISSN

0974-4150 (Online)
0974-4169 (Print)


Author(s): A. S. Goswami-Giri

Email(s): anitagoswami@yahoo.com

DOI: Not Available

Address: A. S. Goswami-Giri
Chemistry Research Laboratory, Department of Chemistry, B. N. Bandodkar College of Science.
Chendani Bunder Road, Thane – 400 601, MS (India).
*Corresponding Author

Published In:   Volume - 5,      Issue - 5,     Year - 2012


ABSTRACT:
To revaluates the catalytic mechanism of onion leaves tyrosinase and its behavioral study were performed by immobilized it in agar- Abelmoschus esculentus polymer. Soluble and immobilized tyrosinase exhibited Km 5µM and 8.33µM; Vmax 167µmol/lit/min and 90µmol/lit/min; optimum pH 7.2 ; Optimum pH 7.0, Optimum temperature 50oC and 60oC, Ea 108.35 Kcal/mol and 78.80 Kcal/mol respectively. Immobilized tyrosinase was more heat stable and longer stability than soluble tyrosinase. Immobilized activity maxima investigated at 35 min having storage stability 75-80% while 65% for soluble. Nevertheless, soluble tyrosinase had higher affinity for the substrate as compared to immobilize. Concluding, agar: Abelmoschus esculentus composite matrix provides natural ambient to enzyme; may be utilized for industrial purpose.


Cite this article:
A. S. Goswami-Giri. Immobilized onion leaves tyrosinase on agar- Abelmoschus esculentus. Asian J. Research Chem. 5(5): May 2012; Page 663-667.


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