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Protein discovery and engineering

Better proteins with unique properties

​We develop and engineer enzymes and other proteins for various applications and carry out research and development on many aspects of protein chemistry.

In contract research projects for our customers, we develop new enzymes or other proteins for different applications, and improve their properties and performance according to customer´s needs. 

As an example, we have engineered a yeast strain capable of consolidated bioprocessing for Mascoma Corporation. It reduced the need for external enzymes about 50%, improving significantly the economics of bioethanol production.

Development of enzymes and other proteins for various applications

We discover novel enzymes and engineer them for diverse applications depending on the client’s needs. This includes discovery of novel activities, characterization of reaction mechanisms as well as improvement of enzyme properties through modern protein engineering techniques.

In addition, we explore and develop novel biomolecules for nanomaterial applications. Interactions between proteins and nanomaterials are used to build functional devices and materials by self-assembly. A special focus is on protein engineering, surface techniques, characterization of interactions, self-assembly, and microscopy.

Especially, we have expertise in engineering enzymes for biomass hydrolysis and modification, and functionalization of materials with proteins. 

Solid expertise in modern facilities

In addition to strong scientific track record and expertise, we have an excellent infrastructure for protein development. We can utilize modern as well as classical screening methods, and use robotics in high-throughput screening. In order to characterize and study the properties of proteins we have a wide spectrum of devices for analytics and imaging.

Most of our projects are related to biochemical, biofuel, nanomaterial and food industries. However, our expertise is applicable wherever protein engineering is needed.


​Scientific publications


Protein discovery

(Please scroll to Protein engineering below) 


Enzymatically and chemically oxidized lignin nanoparticles for biomaterial applications.

Mattinen M-L, Valle-Delgado JJ, Leskinen T, Anttila T, Riviere G, Sipponen M, Paananen A, Lintinen K, Kostiainen M and Österberg M.

Enzyme Microb. Technol. 2018, 111, 48–56. DOI: 10.1016/j.enzmictec.2018.01.005


Simple process for lignin nanoparticle preparation.

Lievonen M, Valle-Delgado JJ, Mattinen M-L, Hult E-L, Lintinen K, Kostiainen MA, Paananen A, Szilvay GR, Setälä H and Österberg M.

Green Chem., 2016, 18, 1416–1422.


Keratin-reinforced cellulose filaments from ionic liquid solutions.

Kammiovirta K, Jääskeläinen A-S, Kuutti L, Holopainen-Mantila U, Paananen A, Suurnäkki A and Orelma H.

RSC Adv., 2016, 6, 88797-88806.


Swollenin from Trichoderma reesei exhibits hydrolytic activity against cellulosic substrates with features of both endoglucanases and cellobiohydrolases.

Andberg M, Penttilä M, Saloheimo M.

Bioresour Technol. 2015 Apr;181:105-13.


Interaction of transglutaminase with adsorbed and spread films of β-casein and к-casein.

Ridout MJ, Paananen A, Mamode A, Linder MB, Wilde PJ.

Colloids Surf B Biointerfaces. 2015 Apr 1;128:254-60.


Adsorption of oat proteins to air-water interface in relation to their colloidal state.

Ercili-Cura D, Miyamoto A, Paananen A, Yoshii H, Poutanen K and Partanen R.

Food Hydrocolloids (2015) 44, 183–190.


Heterotrophic communities supplied by ancient organic carbon predominate in deep fennoscandian bedrock fluids.

Purkamo L, Bomberg M, Nyyssönen M, Kukkonen I, Ahonen L, Itävaara M.

Microb Ecol. 2015 Feb;69(2):319-32.


Rapid reactivation of deep subsurface microbes in the presence of C-1 compounds.

Rajala P, Bomberg M, Kietäväinen R, Kukkonen I, Ahonen L, Nyyssönen M, Itävaara M.

Microorganisms (2015) 3, 17-33, doi:10.3390/microorganisms3010017, Open access, Microorganisms. ISSN 2076-2607,


Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase from Agrobacterium tumefaciens.

Taberman H, Andberg M, Parkkinen T, Richard P, Hakulinen N, Koivula A, Rouvinen J.

Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):49-52.


Single-molecule imaging analysis of elementary reaction steps of Trichoderma reesei cellobiohydrolase I (Cel7A) hydrolyzing crystalline cellulose Iα and IIII.

Shibafuji Y, Nakamura A, Uchihashi T, Sugimoto N, Fukuda S, Watanabe H, Samejima M, Ando T, Noji H, Koivula A, Igarashi K, Iino R.

J Biol Chem. 2014 May 16;289(20):14056-65.


L-arabinose/D-galactose 1-dehydrogenase of Rhizobium leguminosarum bv. trifolii characterised and applied for bioconversion of L-arabinose to L-arabonate with Saccharomyces cerevisiae.

Aro-Kärkkäinen N, Toivari M, Maaheimo H, Ylilauri M, Pentikäinen OT, Andberg M, Oja M, Penttilä M, Wiebe MG, Ruohonen L, Koivula A.

Appl Microbiol Biotechnol. 2014 Dec;98(23):9653-65.


Structure and function of a decarboxylating Agrobacterium tumefaciens keto-deoxy-d-galactarate dehydratase.

Taberman H, Andberg M, Parkkinen T, Jänis J, Penttilä M, Hakulinen N, Koivula A, Rouvinen J.

Biochemistry. 2014 Dec 30;53(51):8052-60.


Micelle formation of coenzyme Q10 with dipotassium glycyrrhizate using inclusion complex of coenzyme Q10 with γ-cyclodextrin.

Uekaji Y, Onishi M, Nakata D, Terao K, Paananen A, Partanen R, Yoshii H.

J Phys Chem B. 2014 Oct 2;118(39):11480-6.


Hydrophobin film structure for HFBI and HFBII and mechanism for accelerated film formation.

Magarkar A, Mele N, Abdel-Rahman N, Butcher S, Torkkeli M, Serimaa R, Paananen A, Linder M, Bunker A.

PLoS Comput Biol. 2014 Jul 31;10(7):e1003745.


Taxonomically and functionally diverse microbial communities in deep crystalline rocks of the Fennoscandian shield.

Nyyssönen M, Hultman J, Ahonen L, Kukkonen I, Paulin L, Laine P, Itävaara M, Auvinen P.

ISME J. 2014 Jan;8(1):126-38.


A spectroscopic characterization of a phenolic natural mediator in the laccase biocatalytic reaction.

Martorana A, Sorace L, Boer H, Vazquez-Duhalt R, Basosi R.

Journal of Molecular Catalysis B: Enzymatic (2013)  97: 203–208


Effect of temperature on lignin-derived inhibition studied with three structurally different cellobiohydrolases.

Rahikainen JL, Moilanen U, Nurmi-Rantala S, Lappas A, Koivula A, Viikari L, Kruus K.

Bioresour Technol. 2013 Oct;146:118-25.


Novel Penicillium cellulases for total hydrolysis of lignocellulosics.

Marjamaa K, Toth K, Bromann PA, Szakacs G, Kruus K.

Enzyme Microb Technol. 2013 May 10;52(6-7):358-69.


Swollenin aids in the amorphogenesis step during the enzymatic hydrolysis of pretreated biomass.

Gourlay K, Hu J, Arantes V, Andberg M, Saloheimo M, Penttilä M, Saddler J.

Bioresour Technol. 2013 Aug;142:498-503.


Cellulase-lignin interactions-the role of carbohydrate-binding module and pH in non-productive binding.

Rahikainen JL, Evans JD, Mikander S, Kalliola A, Puranen T, Tamminen T, Marjamaa K, Kruus K.

Enzyme Microb Technol. 2013 Oct 10;53(5):315-21.


Preferential adsorption and activity of monocomponent cellulases on lignocellulose thin films with varying lignin content.

Martín-Sampedro R, Rahikainen JL, Johansson LS, Marjamaa K, Laine J, Kruus K, Rojas OJ.

Biomacromolecules. 2013 Apr 8;14(4):1231-9.


Inhibitory effect of lignin during cellulose bioconversion: the effect of lignin chemistry on non-productive enzyme adsorption.

Rahikainen JL, Martin-Sampedro R, Heikkinen H, Rovio S, Marjamaa K, Tamminen T, Rojas OJ, Kruus K.

Bioresour Technol. 2013 Apr;133:270-8.


Dissecting the deep biosphere: retrieving authentic microbial communities from packer-isolated deep crystalline bedrock fracture zones.

Purkamo L, Bomberg M, Nyyssönen M, Kukkonen I, Ahonen L, Kietäväinen R, Itävaara M.

FEMS Microbiol Ecol. 2013 Aug;85(2):324-37.


Visualization of cellobiohydrolase I from Trichoderma reesei moving on crystalline cellulose using high-speed atomic force microscopy.

Igarashi K, Uchihashi T, Koivula A, Wada M, Kimura S, Penttilä M, Ando T, Samejima M.

Methods Enzymol. 2012;510:169-82.


Characterization of a novel Agrobacterium tumefaciens galactarolactone cycloisomerase enzyme for direct conversion of D-galactarolactone to 3-deoxy-2-keto-L-threo-hexarate.

Andberg M, Maaheimo H, Boer H, Penttilä M, Koivula A, Richard P.

J Biol Chem. 2012 May 18;287(21):17662-71.


Transglutaminase catalyzed cross-linking of sodium caseinate improves oxidative stability of flaxseed oil emulsion.

Ma H, Forssell P, Kylli P, Lampi AM, Buchert J, Boer H, Partanen R.

J Agric Food Chem. 2012 Jun 20;60(24):6223-9.


Methanogenic and sulphate-reducing microbial communities in deep groundwater of crystalline rock fractures in Olkiluoto, Finland.

Nyyssönen M, Bomberg M, Kapanen A, Nousiainen A, Pitkänen P, Itävaara M.

Geomicrobiology Journal (2012) 29, 863–878, 2012, doi-link: 10.1080/01490451.2011.635759


Microbes in bentonite.

Rättö M and Itävaara M.

VTT Technology: (2012) 20, 30 pages, ISBN 978-951-38-7833-7


Self-assembly of class II hydrophobins on polar surfaces.

Grunér MS, Szilvay GR, Berglin M, Lienemann M, Laaksonen P, Linder MB.

Langmuir. 2012 Mar 6;28(9):4293-300.


Direct Electron Transfer of Trametes Hirsuta Laccase in a Dual-Layer-Architecture of Poly(3,4-Ethylenedioxythiophene) Films.

Wang X, Latonen R-M, Sjöberg-Eerola P, Eriksson J-E, Bobacka J, Boer H, Bergelin M.

J. Phys. Chem. (2011) 115, 5919–5929


Crystal structure of uronate dehydrogenase from Agrobacterium tumefaciens.

Parkkinen T, Boer H, Jänis J, Andberg M, Penttilä M, Koivula A, Rouvinen J.

J Biol Chem. 2011 Aug 5;286(31):27294-300.


Crystal structure of an ascomycete fungal laccase from Thielavia arenaria--common structural features of asco-laccases.

Kallio JP, Gasparetti C, Andberg M, Boer H, Koivula A, Kruus K, Rouvinen J, Hakulinen N.

FEBS J. 2011 Jul;278(13):2283-95.


Traffic jams reduce hydrolytic efficiency of cellulase on cellulose surface.

Igarashi K, Uchihashi T, Koivula A, Wada M, Kimura S, Okamoto T, Penttilä M, Ando T, Samejima M.

Science. 2011 Sep 2;333(6047):1279-82.


Inhibition of enzymatic hydrolysis by residual lignins from softwood--study of enzyme binding and inactivation on lignin-rich surface.

Rahikainen J, Mikander S, Marjamaa K, Tamminen T, Lappas A, Viikari L, Kruus K.

Biotechnol Bioeng. 2011 Dec;108(12):2823-34.


Adsorption of monocomponent enzymes in enzyme mixture analyzed quantitatively during hydrolysis of lignocellulose substrates.

Várnai A, Viikari L, Marjamaa K, Siika-aho M.

Bioresour Technol. 2011 Jan;102(2):1220-7.


Characterization of bacterial diversity to a depth of 1500 m in the Outokumpu deep borehole, Fennoscandian Shield.

Itävaara M, Nyyssönen M, Kapanen A, Nousiainen A, Ahonen L, Kukkonen I.

FEMS Microbiol Ecol. 2011 Aug;77(2):295-309.


Identification in Agrobacterium tumefaciens of the D-galacturonic acid dehydrogenase gene.

Boer H, Maaheimo H, Koivula A, Penttilä M, Richard P.

Appl Microbiol Biotechnol. 2010 Apr;86(3):901-9.


Bio-electrochemical characterisation of high and low redox potential laccases from fungal and bacterial origin.

Frasconi M, Favero G, Boer H, Koivula A and Mazzei F.

BBA (2010) 1804,  899–908.


Cell wall lignin is polymerised by class III secretable plant peroxidases in Norway spruce.

Fagerstedt KV, Kukkola EM, Koistinen VV, Takahashi J, Marjamaa K.

J Integr Plant Biol. 2010 Feb;52(2):186-94.


Protein engineering

Single-Molecule Force Spectroscopy Reveals Self-Assembly Enhanced Surface Binding of Hydrophobins.

Li B, Wang X, Li Y, Paananen A, Szilvay GR, Qin M, Wang W and Cao Y.

Accepted to Chem. Eur. J. 2018, 10.1002/chem.201801730

Single-molecule force spectroscopy study on modular resilin fusion protein.

Griffo A, Hähl H, Grandthyll S, Muller F, Paananen A, Ilmén M, Szilvay GR, Landowski CP, Penttilä M, Jacobs K, and Laaksonen P.

ACS Omega, 2017, 2 (10), 6906-6915. DOI: 10.1021/acsomega.7b01133

Pure protein bilayers and vesicles from native fungal hydrophobins

Hähl, H., Vargas, J. N., Griffo, A., Laaksonen, P., Szilvay, G., Lienemann, M., Jacobs, K., Seemann, R., Fleury, J.-B.,

Advanced Materials, 2017, 29, 1602888,

Elastic and pH responsive hybrid interfaces created with engineered resilin and nanocellulose.

Fang W, Paananen A, Vitikainen M, Koskela S, Westerholm-Parvinen A, Joensuu J, Landowski C, Penttilä M, Linder MB and Laaksonen P.

Biomacromolecules, 2017, 18(6), 1866-1873.


The Dynamics of Multimer Formation of the Amphiphilic Hydrophobin Protein HFBII.

Grunér MS, Paananen A, Szilvay GR and Linder MB.

Colloids Surf. B., 2017, 155, 111–117.


Molecular Structure of Hydrophobins Studied with Site-Directed Mutagenesis and Vibrational Sum-Frequency Generation Spectroscopy.

Meister K, Paananen A, Speet B, Lienemann M and Bakker HJ.

J. Phys. Chem., 2017, 121(40), 9398-9402. DOI: 10.1021/acs.jpcb.7b08865


Observation of PH-Induced Protein Reorientation at the Water Surface.

Meister K, Roeters S, Paananen A, Woutersen S, Versluis J, Szilvay GR and Bakker H.

J. Phys. Chem. Lett., 2017, 8, 1772−1776.


Identification of the response of protein N–H vibrations in vibrational sum-frequency generation spectroscopy of aqueous protein films.

Meister K, Paananen A and Bakker HJ.

Phys. Chem. Chem. Phys., 2017, 19(17), 10804-10807. DOI: 10.1039/c6cp08325k


Graphene Biosensor Programming with Genetically Engineered Fusion Protein Monolayers.

Soikkeli M, Kurppa K, Kainlauri M, Arpiainen S, Paananen A, Gunnarsson D, Joensuu JJ, Laaksonen P, Prunnila M, Linder M. and Ahopelto J.

ACS Appl. Mater. Interfaces, 2016, 8, 8257–8264.


Self-Assembly of Hydrophobin Classes at the Air-Water Interface.

Meister K, Bäumer A, Szilvay GR, Paananen A and Bakker HJ.

J. Phys. Chem. Lett., 2016, 7, 4067–4071.


Modular architecture of protein binding units for designing properties of cellulose nanomaterials

Malho, J-M., Arola, S., Laaksonen, P., Szilvay, G. R., Ikkala, O., Linder, M. B.,  

Angewandte Chemie International Edition, 2015, 54, 12025 – 12028


Hydrophobin as a nanolayer primer that enables the fluorinated coating of poorly reactive polymer surfaces.

Gazzera L, Corti C, Pirrie L, Paananen A, Monfredini A, Cavallo G, Bettini S, Giancane G, Valli L, Linder MB, Resnati G, Milani R and Metrangolo P.

Adv. Mater. Interfaces 2015, 2, article number 1500170.


Charge-Based Engineering of Hydrophobin HFBI: Effect on Interfacial Assembly and Interactions.

Lienemann M, Grunér MS, Paananen A, Siika-Aho M, Linder MB.

Biomacromolecules. 2015 Apr 13;16(4):1283-92.


A synthetically modified hydrophobin showing enhanced fluorous affinity.

Milani R, Pirrie L, Gazzera L, Paananen A, Baldrighi M, Monogioudi E, Cavallo G, Linder M, Resnati G, Metrangolo P.

J Colloid Interface Sci. 2015 Jun 15;448:140-7.


The effect of hydrophobin protein on conductive properties of carbon nanotube field-effect transistors: first study on sensing mechanism

Yotprayoonsak, P., Szilvay, G.R., Laaksonen, P., Linder, M.B., Ahlskog, M.,

Journal of Nanoscience and Nanotechnology, 2015, 15, 2079 – 2087.


Engineering of the function of diamond-like carbon binding peptides through structural design.

Gabryelczyk B, Szilvay GR, Singh VK, Mikkilä J, Kostiainen MA, Koskinen J, Linder MB.

Biomacromolecules. 2015 Feb 9;16(2):476-82.


Engineering chimeric thermostable GH7 cellobiohydrolases in Saccharomyces cerevisiae.

Voutilainen SP, Nurmi-Rantala S, Penttilä M, Koivula A.

Appl Microbiol Biotechnol. 2014 Apr;98(7):2991-3001.


Formation of ceramophilic chitin and biohybrid materials enabled by a genetically engineered bifunctional protein.

Malho JM, Heinonen H, Kontro I, Mushi NE, Serimaa R, Hentze HP, Linder MB, Szilvay GR.

Chem Commun (Camb). 2014 Jul 14;50(55):7348-51.


The tryptophan residue at the active site tunnel entrance of Trichoderma reesei cellobiohydrolase Cel7A is important for initiation of degradation of crystalline cellulose.

Nakamura A, Tsukada T, Auer S, Furuta T, Wada M, Koivula A, Igarashi K, Samejima M.

J Biol Chem. 2013 May 10;288(19):13503-10.


A His-tagged Melanocarpus albomyces laccase and its electrochemistry upon immobilisation on NTA-modified electrodes and in conducting polymer films.

Sosna M, Boer H, Bartlett PN.

Chemphyschem. 2013 Jul 22;14(10):2225-31.


Impact of hydrothermal pre-treatment to chemical composition, enzymatic digestibility and spatial distribution of cell wall polymers.

Holopainen-Mantila U, Marjamaa K, Merali Z, Käsper A, de Bot P, Jääskeläinen AS, Waldron K, Kruus K, Tamminen T.

Bioresour Technol. 2013 Jun;138:156-62.


Directing enzymatic cross-linking activity to the air-water interface by a fusion protein approach.

Paananen A, Ercili-Cura D, Saloheimo M, Lantto R & Linder M.

Soft Matter (2013) 9, 1612 – 1619.


Engineering chitinases for the synthesis of chitin oligosaccharides: catalytic aminoacid mutations convert the GH-18 family glycoside hydrolases into transglycosylases.

Andres E, Boer H, Koivula A, Samain E, Driguez H, Armand S, and Cottaz S.

Journal of Molecular Catalysis B: Enzymatic (2012),  74: 89-96


Metabolic engineering of Saccharomyces cerevisiae for bioconversion of D-xylose to D-xylonate.

Toivari M, Nygård Y, Kumpula EP, Vehkomäki ML, Benčina M, Valkonen M, Maaheimo H, Andberg M, Koivula A, Ruohonen L, Penttilä M, Wiebe MG.

Metab Eng. 2012 Jul;14(4):427-36.


Lignocellulosic ethanol: from science to industry.

Viikari L, Vehmaanperä J and Koivula A.

Biomass and Bioenergy (2012)  46, 13-24.


Genetic engineering in biomimetic composites.

Laaksonen P, Szilvay GR, Linder MB.

Trends Biotechnol. 2012 Apr;30(4):191-7.


High level secretion of cellobiohydrolases by Saccharomyces cerevisiae.

Ilmén M, den Haan R, Brevnova E, McBride J, Wiswall E, Froehlich A, Koivula A, Voutilainen SP, Siika-Aho M, la Grange DC, Thorngren N, Ahlgren S, Mellon M, Deleault K, Rajgarhia V, van Zyl WH, Penttilä M.

Biotechnol Biofuels. 2011 Sep 12;4:30.


Self-assembly of cellulose nanofibrils by genetically engineered fusion proteins.

Varjonen S, Laaksonen P, Paananen A, Valo H, Hähl H, Laaksonen T & Linder M.

Soft Matter (2011) 7, 2402 – 2411.


Engineering of a redox protein for DNA-directed assembly.

Szilvay GR, Brocato S, Ivnitski D, Li C, De La Iglesia P, Lau C, Chi E, Werner-Washburne M, Banta S, Atanassov P.

Chem Commun (Camb). 2011 Jul 14;47(26):7464-6.


Expression of Talaromyces emersonii cellobiohydrolase Cel7A in Saccharomyces cerevisiae and rational mutagenesis to improve its thermostability and activity.

Voutilainen S, Murray P, Tuohy M and Koivula A.

PEDS (2010), 23, 69–79.


Electrochemical evaluation of electron transfer kinetics of high and low redox potential laccases on gold electrode.

Frasconi M, Boer H, Koivula A and Mazzei F.

Electrochimica Acta (2010) 56,  817–82


Performance of a printable enzymatic fuel cell - study on mediated ThL laccase cathode.

Tuurala S, Smolander M, Uotila J, Kaukoniemi O-V, Boer H, Valkiainen M, Vaari A, Koivula A and Jenkins P.

ECS Transactions (2010)  25, 1-10.


Hydrophobins: the protein-amphiphiles of filamentous fungi.

Linder MB, Szilvay GR, Nakari-Setälä T, Penttilä ME.

FEMS Microbiol Rev. 2005 Nov;29(5):877-96.

Timo PulliDr. Timo Pulli, Research Team Leader

I have MSc degree in biotechnology with minor studies in biochemistry and chemistry (University of Turku, 1996). I received my PhD from University of Helsinki, Faculty of Medicine, in 1998. Since then I have worked at VTT in different roles in R&D and business development. I have also worked in German Cancer Research Centre (DKFZ, Heidelberg) as a Marie Curie Research Fellow in 2003-2004. I have wide know-how and experience in R&D, project management, business development and commercialization of life science related technologies.

Anu KoivulaDr. Anu Koivula, Principal Scientist, Principal Investigator

I received my Ph.D. in 1996 at the Department of Biochemistry, University of Helsinki. My main activities relate to enzymology, protein engineering and applications of industrially relevant enzymes. I have been working at VTT particularly with different polysaccharide degrading enzymes (such as amylases, cellulases and chitinases) as well as oxidative enzymes (such as laccases). In addition, I have been involved in projects for metabolic engineering of microbes for chemical production and dealing with various types enzymes, e.g. dehydrogenases, lactonases, dehydratases and aldolases. I have acted at VTT in different positions as a Researcher and as a Team Leader.  My current position is Principal Scientist at the Protein Discovery and Engineering Team. I have been working as a Project manager at VTT since 1999 in various projects funded by the Academy of Finland, Finnish Funding Agency for Innovation (Tekes), and EU ( under FP6, FP7, H2020) as well as in contract research projects funded by industry. I have supervised Master’s and PhD Thesis, given lectures at Finnish universities, acted as an opponent for PhD Thesis, and participated in organising international conferences. For publications, see:

Martina AndbergDr. Martina Andberg, Senior Scientist

My research focus is on enzymology and enzyme discovery and engineering, i.e. the characterization of structure, function and mechanism of enzymes with important biotechnological roles. I received my MSc degree from Department of Biochemistry and Pharmacy, Åbo Akademi and doctoral degree (Med Dr) from Department of Medical Chemistry at Karolinska Institutet. During my 15 years at VTT I have been working with many industrial enzymes as well as enzymes in various metabolic pathways, e.g hydrolases, oxidoreductases (laccases, tyrosinases, haloperoxidases, sugar oxidases), sugar dehydrogenases, dehydratases, and aldolases. Currently the main focus is on aldolase reactions for synthetic pathways in the “Living factories: Synthetic Biology for a Sustainable Bioeconomy” project of the Finnish Funding Agency for Innovation, TEKES.,,

Harry BoerDr. Harry Boer, Senior Scientist

I am originally from The Netherlands where I received my doctoral degree from the Department of Chemistry of the University of Groningen. My expertise includes enzymology, protein chemistry, protein engineering, and high throughput screening. More specific my research activities have focused on membrane transporters, glycosyl hydrolases and various oxidative enzymes. I have participated in EU consortium projects in the different framework programmes.

Kaisa MarjamaaDr. Kaisa Marjamaa, Senior Scientist

My work is focused on development of enzymatic methods for industrial utilization of plant biomass components e.g. conversion into fuels and chemicals or fibre products. I have background in plant physiology, where I received my PhD from University of Helsinki in 2007. I’ve been working at VTT since 2008. I’ve expertise in enzyme discovery utilizing classical activity based and bioinformatics assisted methods and enzymology and applications of plant biomass degrading microbial enzymes.

Antti NyyssöläDr. Antti Nyyssölä, Senior Scientist

I have a M. Sc. (Chem. Eng.) degree in Applied Biochemistry (1995) and a D.Sc. (Tech.) degree in Bioprocessing  (2002) from the Helsinki University of Technology. After working in the biotechnological industry (Cultor Ltd.) and in academia I joined VTT in 2008. As a Research Fellow I have also been responsible for the duties of the Professor of Biochemistry in Aalto University for a year in 2015. My research has been related to various aspects of enzymology, bioprocessing and metabolic engineering. Recently, my main research focus has been on lipid modifying enzymes such as lipases, lipoxygenases and cutinases.

   Dr. Arja Paananen, Senior Scientist

My current research activities focus on hydrophobins and other proteins in materials applications, for example as protein-nanocellulose assemblies. I have expertise in interfacial engineering, surface and colloid chemistry, protein chemistry, nanobiomaterials, and related biophysical characterization techniques (for example AFM, rheology, QCM-D, DLS, tensiometer, contact angle, Langmuir trough).  I have experience in project management and have been involved in several interdisciplinary projects. In 2007 I finalised my PhD at the Åbo Akademi University in the field of Physical Chemistry. The PhD thesis focussed on the interactions and interfacial behaviour of biopolymers.

Sanni VoutilainenDr. Sanni Voutilainen, Research Scientist

I have expertise in protein engineering using both rational (site-directed mutagenesis) and directed evolution methods including high-throughput screening of the variants with robotic work station. I have gained experience in cellulase research in several research projects at VTT. The cellulase work has included heterologous expression and biochemical characterization cellulases, as well as protein engineering. I received my PhD in 2011 and in my doctoral thesis study the aim was to utilize different protein engineering methods for improving the hydrolysis of crystalline cellulose by fungal cellulase enzymes.  During 2013-2014 I visited Aalto University and studied the effect of different proteins in nanocellulose based materials. In addition to cellulases, the current research focus is on carbon-carbon bond forming enzymes for the production of valuable chemicals from simple carbon compounds.

 Dr. Géza Szilvay, Senior Scientist

My current research concentrates on utilizing the exceptional functions of biological proteins in the development of new sustainable materials and products. More specifically, we use bioengineering methods to produce proteins that control material interactions and interfaces. I have over 17 years of experience working on fungal hydrophobin proteins, biointerface interactions, and bioengineering. My relevant expertise are fungal biotechnology, biomimetic materials, colloidal and surface chemistry, protein chemistry and protein engineering, as well as hydrophobin protein production and molecular understanding. Before my current position at VTT I worked as a post-doc at Columbia University, NYC, USA, department of Chemical Engineering.