Versatile peroxidase as a valuable tool for generating new biomolecules by homogeneous and heterogeneous cross-linking

Davinia Salvachúa, Alicia Prieto, Maija Liisa Mattinen, Tarja Tamminen, Tiina Liitiä, Martina Lille, Stefan Willför, Angel T. Martínez, María Jesús Martínez*, Craig B. Faulds

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

29 Citations (Scopus)


The modification and generation of new biomolecules intended to give higher molecular-mass species for biotechnological purposes, can be achieved by enzymatic cross-linking. The versatile peroxidase (VP) from Pleurotus eryngii is a high redox-potential enzyme with oxidative activity on a wide variety of substrates. In this study, VP was successfully used to catalyze the polymerization of low molecular mass compounds, such as lignans and peptides, as well as larger macromolecules, such as protein and complex polysaccharides. Different analytical, spectroscopic, and rheological techniques were used to determine structural changes and/or variations of the physicochemical properties of the reaction products. The lignans secoisolariciresinol and hydroxymatairesinol were condensed by VP forming up to 8 unit polymers in the presence of organic co-solvents and Mn2+. Moreover, 11 unit of the peptides YIGSR and VYV were homogeneously cross-linked. The heterogeneous cross-linking of one unit of the peptide YIGSR and several lignan units was also achieved. VP could also induce gelation of feruloylated arabinoxylan and the polymerization of β-casein. These results demonstrate the efficacy of VP to catalyze homo- and hetero-condensation reactions, and reveal its potential exploitation for polymerizing different types of compounds.

Original languageEnglish
Pages (from-to)303-311
Number of pages9
JournalEnzyme and Microbial Technology
Issue number6-7
Publication statusPublished - 10 May 2013
MoE publication typeA1 Journal article-refereed


  • β-Casein
  • Enzymatic polymerization
  • Feruloylated arabinoxylan
  • Lignan
  • Organic co-solvent
  • Peptide


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