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

*Tämän työn vastaava kirjoittaja

Tutkimustuotos: LehtiartikkeliArtikkeliTieteellinenvertaisarvioitu

24 Sitaatiot (Scopus)

Abstrakti

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.

AlkuperäiskieliEnglanti
Sivut303-311
Sivumäärä9
JulkaisuEnzyme and Microbial Technology
Vuosikerta52
Numero6-7
DOI - pysyväislinkit
TilaJulkaistu - 10 toukokuuta 2013
OKM-julkaisutyyppiA1 Julkaistu artikkeli, soviteltu

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