Maija-Liisa Mattinen
VTT Technical Research Centre of Finland
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Featured researches published by Maija-Liisa Mattinen.
Journal of Agricultural and Food Chemistry | 2008
Emilia Selinheimo; Piritta Lampila; Maija-Liisa Mattinen; Johanna Buchert
Proteins and certain carbohydrates contain phenolic moieties, which are potential sites for modification of the function of the biopolymers. In this study, the capability of two different fungal oxidative enzymes, laccase from Trametes hirsuta (ThL) and tyrosinase from Trichoderma reesei (TrT), to catalyze formation of hetero-cross-linking between tyrosine side chains of alpha-casein and phenolic acids of hydrolyzed oat spelt xylan (hOSX) was studied. Formation of reaction products was followed by size exclusion chromatography (SEC), fluorescence spectroscopy, and SDS-PAGE, using specific staining methods for proteins and protein-carbohydrate conjugates. ThL and TrT were observed to differ significantly in their ability to catalyze the formation of protein-carbohydrate conjugates or the linking of the small molecular weight phenolic compounds to alpha-casein. The efficiency of these enzymes to directly cross-link protein also differed notably. TrT was able to cross-link alpha-casein more efficiently than ThL. ThL-catalyzed casein cross-linking was significantly enhanced by ferulic acid, p-coumaric acid, and also hOSX. The main reaction products by ThL appeared to be phenolic acid-bridged alpha-caseins. Indications of hetero-cross-link formation between alpha-casein and hOSX by both oxidative enzymes could be visualized by glycoprotein-specific staining in the SDS-PAGE analysis, although ThL was observed to be more effective in the heteroconjugate formation than TrT.
FEBS Journal | 2005
Maija-Liisa Mattinen; Kristiina Kruus; Johanna Buchert; Jacob Holm Nielsen; Henrik J. Andersen; Charlotte Steffensen
Laccase‐catalyzed polymerization of tyrosine and tyrosine‐containing peptides was studied in the presence and absence of ferulic acid (FA). Advanced spectroscopic methods such as MALDI‐TOF MS, EPR, FTIR microscopy and HPLC‐fluorescence, as well as more conventional analytical tools: oxygen consumption measurements and SDS/PAGE were used in the reaction mechanism studies. Laccase was found to oxidize tyrosine and tyrosine‐containing peptides, with consequent polymerization of the compounds. The covalent linkage connecting the compounds was found to be an ether bond. Only small amounts of dityrosine bonds were detected in the polymers. When FA was added to the reaction mixtures, it was found to be incorporated into the polymer structure. Thus, in addition to homopolymers, different heteropolymers containing two or four FA residues were formed in the reactions.
Holzforschung | 2006
Stina Grönqvist; Kari Rantanen; Raimo Alén; Maija-Liisa Mattinen; Johanna Buchert; Liisa Viikari
Abstract Modified wood fibres open new perspectives to create value-added products based on renewable raw materials. An interesting option is the targeted modification of fibre surfaces by oxidative enzymes. This two-stage functionalisation method consists of enzymatic activation of fibre surfaces followed by addition of radicalised compounds reacting preferentially by radical coupling. In this work, the activation of bleached and unbleached softwood TMPs with laccase isolated from Trametes hirsuta was studied. The formation and stability of the radicals were studied by EPR spectroscopy. The reaction of the radicals with 3-hydroxytyramine hydrochloride and the type of chemical linkages were investigated. EPR, ESCA and FTIR spectroscopy were used for analysis. Bleached TMP was radicalised more efficiently than unbleached TMP. The radicals were unstable, as 90% of them were quenched within a few hours. Their lifetime was, however, found to be adequately long for performing coupling reactions. Bonding of new compounds to pulps via radical reactions thus seems to be possible.
Journal of Agricultural and Food Chemistry | 2009
Maija-Liisa Mattinen; Ilari Filpponen; Riikka Järvinen; Bin Li; Heikki Kallio; Pekka Lehtinen; Dimitris S. Argyropoulos
Suberin is present in the underground parts of vegetables and in the bark of trees. Characterization of suberin and the structure of its polyphenolic component have been hampered by insolubility of the polymers. Thus, enzymatically isolated and extractive free suberin enriched fraction from potato, Solanum tuberosum var. Nikola, and the chemically further fractionated phenolics were characterized in solid state by FTIR, DSC, and elemental analysis to identify the groups and to verify success of isolation. For MW and quantitative determination of the groups, polymers were solubilized in ionic liquid derivatized and analyzed by GPC and (31)P NMR. Suberin enriched fraction, MW = ca. 44 x 10(3) g/mol, is a mixture of carbohydrates and polyesters of aliphatic long chain hydroxy fatty acids and diacids linked via ester bonds to the phenolics, MW = ca. 27 x 10(3) g/mol, formed by guaiacyl- and p-hydroxyphenyl structures. Phenolics in peels may be important sources of antioxidants for various applications.
Bioresource Technology | 2011
Raquel Moya; Päivi Saastamoinen; Manuel Hernández; Anna Suurnäkki; Enriqueta Arias; Maija-Liisa Mattinen
The ability of Streptomyces ipomoea laccase to polymerize secoisolariciresinol lignan and technical lignins was assessed. The reactivity of S. ipomoea laccase was also compared to that of low redox fungal laccase from Melanocarpus albomyces using low molecular mass p-coumaric, ferulic and sinapic acid as well as natural (acetosyringone) and synthetic 2,2,6,6-tetramethylpiperidine 1-oxyl (TEMPO) mediators as substrates. Oxygen consumption measurement, MALDI-TOF MS and SEC were used to follow the enzymatic reactions at pH 7, 8, 9 and 10 at 30°C and 50°C. Polymerization of lignins and lignan by S. ipomoea laccase under alkaline reaction conditions was observed, and was enhanced in the presence of acetosyringone almost to the level obtained with M. albomyces laccase without mediator. Reactivities of the enzymes towards acetosyringone and TEMPO were similar, suggesting exploitation of the compounds and low redox laccase in lignin valorization under alkaline conditions. The results have scientific impact on basic research of laccases.
Novel Enzyme Technology for Food Applications | 2007
Johanna Buchert; Emilia Selinheimo; Kristiina Kruus; Maija-Liisa Mattinen; Raija Lantto; Karin Autio
Publisher Summary This chapter explains that food texture plays a major role in food product quality. The rheological properties of a food are determined by the number of weak and strong physical interactions and the permanent covalent bonds, crosslinks, present in the food matrix. Covalent crosslinks make the major contribution to the firmness of food matrices. Crosslinks can be introduced to a food matrix by chemical, enzymatic, and physical means as reviewed by Munindar P. Singh (1991) and Scott N. Gerrard (2002) . Enzymatic crosslinking of food biopolymers is an attractive option owing to the specificity of enzymes and mild reaction conditions. Both food proteins and carbohydrates can be crosslinked by enzymes. Sensory perception of texture plays an important role in different types of foods. The significance of food texture has further been increased with the trend toward low fat products and “natural” additive-free products. Enzymes provide specific and natural means for tailoring food structure. By the use of enzymes, it will be possible to transform inherently available food components into functional ingredients during food processing and manufacturing. Enzymatic crosslinking in the food matrix can occur via proteins or certain carbohydrates. The type of enzyme used affects the chemistry of the crosslink formed and subsequently the structure of the biopolymer network of the food product.
Enzyme and Microbial Technology | 2013
Davinia Salvachúa; Alicia Prieto; Maija-Liisa Mattinen; Tarja Tamminen; Tiina Liitiä; Martina Lille; Stefan Willför; Ángel T. Martínez; María Jesús Martínez; Craig B. Faulds
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 Mn(2+). 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.
Enzyme and Microbial Technology | 2011
Riitta Partanen; Mika Torkkeli; Maarit Hellman; Perttu Permi; Ritva Serimaa; Johanna Buchert; Maija-Liisa Mattinen
Globular proteins such as β-lactoglobulin (BLG) are poorly accessible to enzymes. We have studied susceptibility of BLG to oxidation by Trichoderma reesei (TrTyr) and Agaricus bisporus (AbTyr) tyrosinases and subsequent intermolecular cross-linking with respect to pH-induced structural changes. We evaluated pH-induced structural changes in BLG using circular dichroism, tryptophan fluorescence and small angle X-ray scattering (SAXS) measurements, where after these results were correlated with the analysis of cross-linking by sodium dodecyl sulphate polyacrylamide gel electrophoresis. Oxygen consumption measurement and changes in radii of gyration determined by SAXS during the enzyme-induced oxidation at the respective reaction conditions were also followed. Intermolecular cross-linking of BLG by TrTyr was found at pH 9 but not at pH 7.5. AbTyr was unable to catalyze cross-linking at pH 7.5 or pH 9. Increased accessibility and cross-linking by TrTyr was addressed to loosening of the three dimensional structure of the protein, increased flexibility of the backbone as well as partial hydrolysis. In addition to basic research of the effect of protein folding on enzymatic cross-linking the research results have significance on the exploitation of TrTyr at alkaline conditions.
Journal of Biotechnology | 2011
Maarit Hellman; Maija-Liisa Mattinen; Biao Fu; Johanna Buchert; Perttu Permi
Enzymatic cross-linking of proteins can be catalyzed either by transferase-type enzymes, e.g., transglutaminases, or by oxidoreductases, e.g., tyrosinases or laccases. Three-dimensional structure of protein substrate plays a key role in these reactions, that is, the reactivity and end product are strongly modulated by the accessibility of target amino acid residues to the cross-linking enzyme. Typically structural integrity of protein can be distorted by heat, pH, or mechanical action, as well as by varying ionic concentration of the solution. In this study we used partially unfolded protein (wild-type DrkN SH3) and its structurally stabilized mutant (T22G) to investigate the impact of folded/unfolded conformations on cross-linking by Trichoderma reesei tyrosinase. Our results clearly showed formation of intermolecular cross-links solely between unfolded conformations, making them superior substrates to folded proteins when using tyrosinase as a cross-linking enzyme. Multidimensional heteronuclear magnetic resonance experiments in solution state were employed to investigate cross-linked end-products. The results presented in this study form basis for application development in food, medical, cosmetic, textile, packing and other sectors. In addition, the outcome of this study has a high value for the basic understanding of reaction mechanism of tyrosinases on proteins.
Journal of Agricultural and Food Chemistry | 2011
Evanthia Monogioudi; Perttu Permi; Ilari Filpponen; Michael Lienemann; Bin Li; Dimitris S. Argyropoulos; Johanna Buchert; Maija-Liisa Mattinen
Cross-linking of β-casein by Trichoderma reesei tyrosinase (TrTyr) and Streptoverticillium mobaraense transglutaminase (Tgase) was analyzed by (31)P nuclear magnetic resonance (NMR) spectroscopy in ionic liquid (IL). According to (31)P NMR, 91% of the tyrosine side chains were cross-linked by TrTyr at high dosages. When Tgase was used, no changes were observed because a different cross-linking mechanism was operational. However, this verified the success of the phosphitylation of phenolics within the protein matrix in the IL. Atomic force microscopy (AFM) in solid state showed that disk-shaped nanoparticles were formed in the reactions with average diameters of 80 and 20 nm for TrTyr and Tgase, respectively. These data further advance the current understanding of the action of tyrosinases on proteins on molecular and chemical bond levels. Quantitative (31)P NMR in IL was shown to be a simple and efficient method for the study of protein modification.