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

D. Salvachúa, A. Prieto, Maija Mattinen, Tarja Tamminen, Tiina Liitiä, Martina Lille, S. Willför, A.T. Martinez, M.J. Martinez (Corresponding Author), C.B. Faulds

Research output: Contribution to journalArticleScientificpeer-review

16 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)303-311
Number of pages9
JournalEnzyme and Microbial Technology
Volume52
Issue number6-7
DOIs
Publication statusPublished - 2013
MoE publication typeA1 Journal article-refereed

Fingerprint

Biomolecules
Peptides
Peroxidase
tyrosyl-isoleucyl-glycyl-seryl-arginine
Lignans
Molecular mass
Polymerization
Casein
Condensation reactions
Gelation
Polysaccharides
Macromolecules
Reaction products
Condensation
Pleurotus
Enzymes
Proteins
Caseins
Oxidation-Reduction
Polymers

Keywords

  • ß-casein
  • enzymatic polymerization
  • feruloylated arabinoxylan
  • lignan
  • organic co-solvent
  • peptide

Cite this

Salvachúa, D. ; Prieto, A. ; Mattinen, Maija ; Tamminen, Tarja ; Liitiä, Tiina ; Lille, Martina ; Willför, S. ; Martinez, A.T. ; Martinez, M.J. ; Faulds, C.B. / Versatile peroxidase as a valuable tool for generating new biomolecules by homogeneous and heterogeneous cross-linking. In: Enzyme and Microbial Technology. 2013 ; Vol. 52, No. 6-7. pp. 303-311.
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Versatile peroxidase as a valuable tool for generating new biomolecules by homogeneous and heterogeneous cross-linking. / Salvachúa, D.; Prieto, A.; Mattinen, Maija; Tamminen, Tarja; Liitiä, Tiina; Lille, Martina; Willför, S.; Martinez, A.T.; Martinez, M.J. (Corresponding Author); Faulds, C.B.

In: Enzyme and Microbial Technology, Vol. 52, No. 6-7, 2013, p. 303-311.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Versatile peroxidase as a valuable tool for generating new biomolecules by homogeneous and heterogeneous cross-linking

AU - Salvachúa, D.

AU - Prieto, A.

AU - Mattinen, Maija

AU - Tamminen, Tarja

AU - Liitiä, Tiina

AU - Lille, Martina

AU - Willför, S.

AU - Martinez, A.T.

AU - Martinez, M.J.

AU - Faulds, C.B.

PY - 2013

Y1 - 2013

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 - ß-casein

KW - enzymatic polymerization

KW - feruloylated arabinoxylan

KW - lignan

KW - organic co-solvent

KW - peptide

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DO - 10.1016/j.enzmictec.2013.03.010

M3 - Article

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EP - 311

JO - Enzyme and Microbial Technology

JF - Enzyme and Microbial Technology

SN - 0141-0229

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ER -