Versatile peroxidase as a valuable tool for generating new biomolecules by homogeneous and heterogeneous cross-linking |
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Authors: | Davinia Salvachúa Alicia Prieto Maija-Liisa Mattinen Tarja Tamminen Tiina Liitiä Martina Lille Stefan Willför Angel T. Martínez María Jesús Martínez Craig B. Faulds |
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Affiliation: | 1. Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu 9, E-28040 Madrid, Spain;2. VTT Technical Research Centre of Finland, P.O. Box 1000, FI-02044 VTT, Finland;3. Process Chemistry Centre, Åbo Akademi University, Porthansgatan 3, FI-20500 Turku, Finland |
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Abstract: | 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. |
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Keywords: | Enzymatic polymerization Organic co-solvent Lignan Peptide β-Casein Feruloylated arabinoxylan |
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