Abstract
In this paper, a recombinant catalase-peroxidase HPI from Escherichia coli was prepared, purified, and used in enzymatic polymerization reactions for the production of several oligomeric products. We tested the enzyme on four different substrates, chosen as representative of phenols and anilines: phenol, 3-methoxyphenol, catechol, and aniline. The polymerization reactions were followed by SEC-HPLC analysis, and except for aniline, all the other substrates were completely converted into one or more polymerization products. Results showed that reactions performed with phenol and 3-methoxyphenol allowed the isolation of some oligomers of different weight: a 27-monomeric unit oligomer and a 23-U oligomer are the heaviest ones. Experiments performed with catechol showed the formation of oligomers of 7 U in the reaction with HPI. HPI polymerization reactions performed with aniline allowed the identification of two different oligomers, one of 4 U and one of 10 U. All the substrates have been also used in reactions catalyzed by HRP in the same reaction conditions. Several products were common to the two enzymes. This work suggests the use of HPI as an alternative enzyme in peroxidatic reactions for the production of different oligomers from phenols and other compounds.
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Acknowledgements
The authors are particularly grateful to Dr. Anna Daghetti for MALDI-TOF analyses and Dr. Giovanni Crosta for helpful discussion. This work was partially supported by US-ARMY-Grant no. W911NF-10-1-0204.
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Di Gennaro, P., Bargna, A., Bruno, F. et al. Purification of recombinant catalase-peroxidase HPI from E. coli and its application in enzymatic polymerization reactions. Appl Microbiol Biotechnol 98, 1119–1126 (2014). https://doi.org/10.1007/s00253-013-4948-0
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DOI: https://doi.org/10.1007/s00253-013-4948-0