Journal
ENZYME AND MICROBIAL TECHNOLOGY
Volume 52, Issue 6-7, Pages 303-311Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.enzmictec.2013.03.010
Keywords
Enzymatic polymerization; Organic co-solvent; Lignan; Peptide; beta-Casein; Feruloylated arabinoxylan
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Funding
- EU [KBBE-2010-4-265397]
- Spanish Ministry of Science and Innovation [BIO2009-08446, PRI-PIBAR-2011-1402]
- project Lignin Fibre
- Academy of Finland [133091]
- Academy of Finland (AKA) [133091, 133091] Funding Source: Academy of Finland (AKA)
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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 beta-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. (C) 2013 Elsevier Inc. All rights reserved.
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