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Extracellular peroxidases from cell suspension cultures of Vaccinium myrtillus . Purification and characterization of two cationic enzymes

Plant Science, ISSN: 0168-9452, Vol: 106, Issue: 2, Page: 177-184
1995
  • 24
    Citations
  • 0
    Usage
  • 10
    Captures
  • 0
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    24
    • Citation Indexes
      23
    • Patent Family Citations
      1
      • 1
  • Captures
    10

Article Description

Seven proteins with peroxidase activity, three cationic and four anionic and neutral, were identified from the medium of 9-day-old Vaccinium myrtillus (bilberry) cell suspension cultures. These cultures have a doubling time of about 50 h and extracellular peroxidase activity seems to be strongly correlated with the biomass growth profile. The two major cationic enzymes (VMP×C1 and VMP×C2), were purified to apparent homogeneity with final RZ values of 3.4 and 3.7, respectively. These enzymes are heme-containing glycoproteins with isoelectric points close to 9 and a molecular weight of approximately 34 000 Da for VMP×C1 and 38 000 Da for VMP×C2. The effect of pH on the activity of the purified enzymes was studied using three substrates: guaiacol, ABTS and syringaldazine. These studies revealed different activity profiles and pH optima. Temperature stability experiments were performed at 37, 50 and 65°C.

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