FOOD SCIENCE ›› 2013, Vol. 34 ›› Issue (9): 194-197.doi: 10.7506/spkx1002-6630-201309040

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Purification and Characterization of Recombinant EGCG-O-transferase from Tea Plant

LÜ Hai-peng,ZHANG Yue,FEI Dong-mei,LIN Zhi*   

  1. National Engineering Research Center for Tea Processing, Tea Research Institute, Chinese Academy of Agricultural Sciences,
    Hangzhou 310008, China
  • Received:2012-07-03 Revised:2013-03-15 Online:2013-05-15 Published:2013-05-07
  • Contact: LIN Zhi E-mail:lvhaipeng@caas.net.cn

Abstract:

Recombinant EGCG-O-transferase from tea plant was expressed in E.coli. The enzyme was then purified
from cell lysate using HisTMtrap affinity column and its enzymatic properties were investigated. After purification, a
pure protein with purity over 95%, recovery of 34.54% and specific enzyme activity of 0.0186 U/mg was obtained.
Further analysis showed that the recombinant protein had a molecular mass of 27.6 kD. It exhibited the highest
activity under the conditions of pH 7.5 and 35 ℃. Kinetic studies showed that Km and Vmax of EGCG-O-transferase
using EGCG as substrate were 0.100 mmol/L and 7.485 mg/(L·min), respectively.

Key words: tea plant, EGCG-O-transferase, purification, characterization

CLC Number: