Polyphenol polymerization by an alternative oxidative microbial enzyme and characterization of the biological activity of oligomers
Articolo
Data di Pubblicazione:
2018
Citazione:
Polyphenol polymerization by an alternative oxidative microbial enzyme and characterization of the biological activity of oligomers / P. Di Gennaro, V. Sabatini, S. Fallarini, R. Pagliarin, G. Sello. - In: BIOMED RESEARCH INTERNATIONAL. - ISSN 2314-6141. - 2018(2018 Apr 27), pp. 3828627.1-3828627.10. [10.1155/2018/3828627]
Abstract:
The recombinant catalase-peroxidase HPI from E. coli was used as an alternative enzyme in polymerization reactions for the
production of (−) epicatechin oligomers and their biological activity was characterized.The enzyme was prepared in two forms: a
purified and an immobilized form. Both were tested for their activity in oxidative polymerization reactions, and their stability and
reusability were assessed. The polymerization reactions were followed by SEC-HPLC analyses, and the substrate was completely
converted into one or more polymerization products depending on the reactions conditions. Results showed that the utilized
conditions allowed for the isolation of some oligomers of different molecular weight: the oligomers containing 6 and 7 units of
epicatechin substrate are the heaviest ones. Epicatechin was also used in reactions catalyzed by HRP in the same reaction conditions
for comparison. In addition, one selected oligomer obtained by HPI enzyme catalysis was shown to act as in vitro inhibitor of tumor
cell growth, like one oligomer deriving from epicatechin by HRP catalysis. These data confirm that epicatechin oligomeric form
is more effective than its monomer in biological activity and suggest the use of HPI as an alternative enzyme in reactions for the
production of epicatechin oligomers.
Tipologia IRIS:
01 - Articolo su periodico
Elenco autori:
P. Di Gennaro, V. Sabatini, S. Fallarini, R. Pagliarin, G. Sello
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