Asian Journal of Research in Chemistry
  • Year: 2014
  • Volume: 7
  • Issue: 11

Kinetics of o-diphenol oxidase Immobilized on Agar-Abelmoschus esculentus Polymer

  • Author:
  • Anita S. Goswami Giri
  • Total Page Count: 6
  • Page Number: 919 to 924

Chemistry Research Laboratory, Department of Chemistry, B. N. Bandodkar College of Science, Chendani Bunder Road, Thane-400 601. Maharashtra, India

*Corresponding Author E-mail: anitagoswami@yahoo.com

Online published on 10 February, 2015.

Abstract

DOPA is a precursor of dopamine and acts as a neuro transmitter. Oxidation of it to dopaquinone is a fast reaction by o-diphenol oxidase. Discrepancies in this reaction are responsible for diverse type of disease and disorders. o-diphenol oxidase was purified on natural column and immobilized on agar-Abelmoschus esculentus polymer. Its immobilized o-diphenol oxidase activity showed Vmax =167μmol/lit/min, Km= 2X10−3, Optimum PH = 6.8, Optimum temperature 80°C, Ea = 160.45Kcal/mol and observed highest activity at 45min. behavior of encapsulated activity was compared with free o-diphenol oxidase.

Keywords

Enzyme-catalyzed reaction, Activation energy of PPO, onion leaves