In vitro polymerization of mussel polyphenolic proteins catalyzed by mushroom tyrosinase

Luis A. Burzio, Veronica A. Burzio, Joel Pardo, Luis O. Burzio

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)


The in vitro enzymatic polymerization of the polyphenolic protein purified from the mussels Aulacomya ater, Mytilus edulis chilensis and Choromytilus chorus was studied. Mushroom tyrosinase was used to oxidize the dopa residues present in these proteins, and polymerization was monitored by acid-urea polyacrylamide gel electrophoresis. The protein from A. ater polymerized at a faster rate than the other two. Amino acid analysis of the crosslinked protein showed a notable decrease in the content of dopa, but no significant change of other amino acids. This suggests that crosslink formation may be limited to the oxidized dopa derivatives of the protein molecules. (C) 2000 Elsevier Science Inc.

Original languageEnglish
Pages (from-to)383-389
Number of pages7
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Issue number3
Publication statusPublished - 30 Aug 2000


  • Adhesive proteins
  • Byssus
  • Catechol oxidase
  • Cross- linking
  • Dopa
  • Mussel
  • Polyphenolic protein
  • Sclerotization
  • Tyrosinase

ASJC Scopus subject areas

  • Physiology
  • Biochemistry
  • Molecular Biology


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