Affordable Access

Publisher Website

Biotransformation of tea catechins into theaflavins with immobilized polyphenol oxidase

Authors
Journal
Journal of Molecular Catalysis B Enzymatic
1381-1177
Publisher
Elsevier
Publication Date
Volume
56
Issue
4
Identifiers
DOI: 10.1016/j.molcatb.2008.05.016
Keywords
  • Biotransformation
  • Bioprocessing
  • Theaflavins
  • Catechins
  • Immobilization
  • Immobilized Enzyme
  • Matrix
  • Substrate
  • Polyphenol Oxidase
Disciplines
  • Biology
  • Pharmacology

Abstract

Abstract Theaflavins, an active antioxidant, a natural pigment and pharmacologically active molecule obtained from black tea were bioprocessed on an immobilized tea polyphenol oxidase (PPO) system by the conversion of tea catechins extracted from green tea leaves with an overall conversion efficiency of 85% about 14-fold increase over maximum achievable in normal black teas. The immobilized enzyme (IE) system consists of activated cellulose matrix on to which the freshly extracted tea leaf polyphenol oxidase was covalently linked. Cellulose as a matrix of choice was considered primarily for its non-toxic nature, natural origin, low cost and easy availability. The kinetic parameters of the IE system were; protein loading capacity 11.8 mg/g; pH optimum 5.9; temperature optimum 37.5 °C; K m 4.76 ± 0.08 mM; V max 20 ± 1.80 nmol/min; enzyme activity retention (83.58%) and number of batches per turnover without loss of activity was 14. The product from IE system was identified by HPLC and ESI-QTOF-MS spectrometry.

There are no comments yet on this publication. Be the first to share your thoughts.