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
- 24Citations
- 10Captures
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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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0168945295040789; http://dx.doi.org/10.1016/0168-9452(95)04078-9; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0029105156&origin=inward; https://linkinghub.elsevier.com/retrieve/pii/0168945295040789; https://api.elsevier.com/content/article/PII:0168945295040789?httpAccept=text/xml; https://api.elsevier.com/content/article/PII:0168945295040789?httpAccept=text/plain; http://dx.doi.org/10.1016/0168-9452%2895%2904078-9; https://dx.doi.org/10.1016/0168-9452%2895%2904078-9
Elsevier BV
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