In vitro polymerization of mussel polyphenolic proteins catalyzed by mushroom tyrosinase.
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.
Burzio
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LA
BiosChile Ingerinería Genetica S.A. and Fundación Ciencia para la Vida, Nuñoa, Santiago, Chile.
Burzio
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VA
Pardo
J
J
Burzio
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LO
D000363:Agaricales / Q000201:enzymology*; D000818:Animals; D049872:Bivalvia / Q000378:metabolism*; D003432:Cross-Linking Reagents / Q000378:metabolism; D019281:Dimerization; D014442:Monophenol Monooxygenase / Q000737:chemistry* / Q000378:metabolism*; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity
D003432:Cross-Linking Reagents; D011506:Proteins; C037403:adhesive protein, mussel; D014442:Monophenol Monooxygenase