Open Access Open Access  Restricted Access Subscription Access
Open Access Open Access Open Access  Restricted Access Restricted Access Subscription Access

Isolation, Partial Purification and Characterization of Polyphenol Oxidase (PPO) from Musa Paradisiaca


Affiliations
1 Department of Biotechnology, Kumaraguru College of Technology, Coimbatore - 641 049, India
2 T. Stanes and Company Limited, Coimbatore – 641 018, India
     

   Subscribe/Renew Journal


Polyphenol oxidase or tyrosinase which is universally present in plants, animals, fungi and bacteria, catalyses two different oxidative reactions combining with molecular oxygen. It causes the hydroxylation of monophenols into odiphenols and further oxidation of o- diphenols into o- quinones. Subsequent polymerisation of o- quinones results in the discoloration of tissues and loss of nutrients from fruits and vegetables. In the present study, PPO (E.C number 1.14.18.1) was extracted from banana (Musa paradisiaca) and partially purified by acetone precipitation. The enzyme was found to have high affinity towards its substrate, catechol and the Michaelis Menten constant was observed as 1mM. The optimum pH and temperature of the enzyme were determined to be 5.0 and 50°C respectively. In this study, various plant extracts like Glycyrrhiza glabra, Rubia cordifolia, Hesperethusa crenulata and oil from the seeds of Hydnocarpus laurifolia and purified compounds like Curcumin, Psoralenwere observed to modulate the activity of PPO. These compounds can be used in skin care cosmetics and in the treatment of skin diseases like vitiligo, leucoderma etc.

Keywords

Polyphenol Oxidase, Characterization, Enzyme Activity.
Subscription Login to verify subscription
User
Notifications
Font Size


Abstract Views: 251

PDF Views: 0




  • Isolation, Partial Purification and Characterization of Polyphenol Oxidase (PPO) from Musa Paradisiaca

Abstract Views: 251  |  PDF Views: 0

Authors

M. Alamelumangai
Department of Biotechnology, Kumaraguru College of Technology, Coimbatore - 641 049, India
J. Dhanalakshmi
Department of Biotechnology, Kumaraguru College of Technology, Coimbatore - 641 049, India
M. Mathumitha
Department of Biotechnology, Kumaraguru College of Technology, Coimbatore - 641 049, India
R. Saranya Renganayaki
Department of Biotechnology, Kumaraguru College of Technology, Coimbatore - 641 049, India
N. Rajalakshmi
T. Stanes and Company Limited, Coimbatore – 641 018, India

Abstract


Polyphenol oxidase or tyrosinase which is universally present in plants, animals, fungi and bacteria, catalyses two different oxidative reactions combining with molecular oxygen. It causes the hydroxylation of monophenols into odiphenols and further oxidation of o- diphenols into o- quinones. Subsequent polymerisation of o- quinones results in the discoloration of tissues and loss of nutrients from fruits and vegetables. In the present study, PPO (E.C number 1.14.18.1) was extracted from banana (Musa paradisiaca) and partially purified by acetone precipitation. The enzyme was found to have high affinity towards its substrate, catechol and the Michaelis Menten constant was observed as 1mM. The optimum pH and temperature of the enzyme were determined to be 5.0 and 50°C respectively. In this study, various plant extracts like Glycyrrhiza glabra, Rubia cordifolia, Hesperethusa crenulata and oil from the seeds of Hydnocarpus laurifolia and purified compounds like Curcumin, Psoralenwere observed to modulate the activity of PPO. These compounds can be used in skin care cosmetics and in the treatment of skin diseases like vitiligo, leucoderma etc.

Keywords


Polyphenol Oxidase, Characterization, Enzyme Activity.