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Título

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

AutorSalvachúa, Davinia; Prieto Orzanco, Alicia CSIC ORCID ; Mattinen, Maija-Liisa; Tamminen, Tarja; Liitiä, Tiina; Lilleb, Martina; Willför, Stefan; Martínez, Ángel T. CSIC ORCID ; Martínez, María Jesús CSIC ORCID ; Faulds, Craig B. CSIC
Palabras claveEnzymatic polymerization
Organic co-solvent
Lignan
Peptide
β-Casein
Feruloylated arabinoxylan
Fecha de publicación10-may-2013
EditorElsevier
CitaciónEnzyme and Microbial Technology 52(6–7): 303–311(2013)
ResumenThe 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
Descripción9 páginas, 8 figuras, 2 tablas -- PAGS nros. 303-311
Versión del editorhttp://dx.doi.org/10.1016/j.enzmictec.2013.03.010
URIhttp://hdl.handle.net/10261/89413
DOI10.1016/j.enzmictec.2013.03.010
ISSN0141-0229
E-ISSN1879-0909
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