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Acta Biomedica Scientia

Volume 1, Issue 2, 2013
Mcmed International
Acta Biomedica Scientia
Issn
2348 - 215X (Print), 2348 - 2168 (Online)
Frequency
bi-annual
Email
editorabs@mcmed.us
Journal Home page
http://mcmed.us/journal/abs
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Abstract
Title
MODELLING THREE-DIMENTIONAL STRUCTURE AND VALIDATION OF POLYPHENOL OXIDASE ENZYME FROM Camellia sinensis (L.) O. KUNTZE
Author
Ramkumar. S
Email
ramkumarbiochem007@gmail.com
keyword
Polyphenol oxidase (PPO), Sequence analysis, Homology modeling, Model validation.
Abstract
Polyphenol Oxidase (PPO), a major enzyme responsible for manufacture of black tea from tea leaves (Camellia sinensis (L) O. Kuntze). It is one of the oldest known beverages made from tender leaves of the plants. Polyphenol oxidase (PPO, EC.1.10.3.1) a key enzyme in tea processing, converts’ polyphenol (catechin) to its products by undergoing enzymatic oxidation to produce black tea pigments such as theflavins (TF) and thearubigis (TR). Therefore, in this study attempt to emphasize the structural relationship of PPO enzyme based on the homology modeling analysis from United Planters' Association of Southern India (UPASI) selected clone of Camellia sinensis (L.). The three-dimensional structure of PPO enzyme was constructed by molecular modeling studies. Further, the model was assessed by PROCHECK, ProSA, and ERRAT plot in order to analyze the quality and consistency of computed model. The overall quality of generated model showed that, 91.1% amino acid residues were under the favored region. The ERRAT value of 68.84 % indicates that the environment profile of the model is good. Based on the results it can be concluded that, the modeled PPO enzyme can be utilized for development of good beverage and production of black tea from the selected area.
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