Oxidase Activity of the Barnacle Adhesive Interface Involves Peroxide-Dependent Catechol Oxidase and Lysyl Oxidase Enzymes.

Journal Article (Journal Article)

Oxidases are found to play a growing role in providing functional chemistry to marine adhesives for the permanent attachment of macrofouling organisms. Here, we demonstrate active peroxidase and lysyl oxidase enzymes in the adhesive layer of adult Amphibalanus amphitrite barnacles through live staining, proteomic analysis, and competitive enzyme assays on isolated cement. A novel full-length peroxinectin (AaPxt-1) secreted by barnacles is largely responsible for oxidizing phenolic chemistries; AaPxt-1 is driven by native hydrogen peroxide in the adhesive and oxidizes phenolic substrates typically preferred by phenoloxidases (POX) such as laccase and tyrosinase. A major cement protein component AaCP43 is found to contain ketone/aldehyde modifications via 2,4-dinitrophenylhydrazine (DNPH) derivatization, also called Brady's reagent, of cement proteins and immunoblotting with an anti-DNPH antibody. Our work outlines the landscape of molt-related oxidative pathways exposed to barnacle cement proteins, where ketone- and aldehyde-forming oxidases use peroxide intermediates to modify major cement components such as AaCP43.

Full Text

Duke Authors

Cited Authors

  • So, CR; Scancella, JM; Fears, KP; Essock-Burns, T; Haynes, SE; Leary, DH; Diana, Z; Wang, C; North, S; Oh, CS; Wang, Z; Orihuela, B; Rittschof, D; Spillmann, CM; Wahl, KJ

Published Date

  • April 2017

Published In

Volume / Issue

  • 9 / 13

Start / End Page

  • 11493 - 11505

PubMed ID

  • 28273414

Electronic International Standard Serial Number (EISSN)

  • 1944-8252

International Standard Serial Number (ISSN)

  • 1944-8244

Digital Object Identifier (DOI)

  • 10.1021/acsami.7b01185


  • eng