TY - JOUR
T1 - Versatile peroxidase as a valuable tool for generating new biomolecules by homogeneous and heterogeneous cross-linking
AU - Salvachúa, Davinia
AU - Prieto, Alicia
AU - Mattinen, Maija Liisa
AU - Tamminen, Tarja
AU - Liitiä, Tiina
AU - Lille, Martina
AU - Willför, Stefan
AU - Martínez, Angel T.
AU - Martínez, María Jesús
AU - Faulds, Craig B.
N1 - Funding Information:
D. Salvachúa thanks the Spanish Ministry of Economy and Competitiveness for a FPU fellowship, P. Matikainen and B. Hillebrandt for technical assistance and Dr. K. Viljanen for the phenolic acids analysis (VTT, Espoo, Finland). We also thank Fernando Escolar for its help in TEM and J. Gil (CIB, Madrid, Spain). This work has been carried out with funding from the EU FP7 project “Peroxicats” (KBBE-2010-4-265397), the Spanish Ministry of Science and Innovation (BIO2009-08446, PRI-PIBAR-2011-1402), and the project “Lignin Fibre” financed by the Academy of Finland (Grant number 133091).
Copyright:
Copyright 2013 Elsevier B.V., All rights reserved.
PY - 2013/5/10
Y1 - 2013/5/10
N2 - 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.
AB - 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.
KW - β-Casein
KW - Enzymatic polymerization
KW - Feruloylated arabinoxylan
KW - Lignan
KW - Organic co-solvent
KW - Peptide
UR - http://www.scopus.com/inward/record.url?scp=84876709843&partnerID=8YFLogxK
U2 - 10.1016/j.enzmictec.2013.03.010
DO - 10.1016/j.enzmictec.2013.03.010
M3 - Article
C2 - 23608497
AN - SCOPUS:84876709843
SN - 0141-0229
VL - 52
SP - 303
EP - 311
JO - Enzyme and Microbial Technology
JF - Enzyme and Microbial Technology
IS - 6-7
ER -