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

AuthorsSalvachúa, Davinia ; Prieto, Alicia ; Mattinen, Maija-Liisa; Tamminen, Tarja; Liitiä, Tiina; Lilleb, Martina; Willför, Stefan; Martínez, Ángel T. ; Martínez, María Jesús ; Faulds, Craig B.
KeywordsEnzymatic polymerization
Organic co-solvent
Feruloylated arabinoxylan
Issue Date10-May-2013
CitationEnzyme and Microbial Technology 52(6–7): 303–311(2013)
AbstractThe 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
Description9 páginas, 8 figuras, 2 tablas -- PAGS nros. 303-311
Publisher version (URL)http://dx.doi.org/10.1016/j.enzmictec.2013.03.010
Appears in Collections:(CIB) Artículos
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