Protein discovery and engineering

Better proteins with unique properties

​We develop proteins for various applications and carry out research and development on many aspects of protein chemistry: new and better enzymes, robust nanomaterials with unique properties.

Feel free to contact us if you wish to improve the performance and cost efficiency of your proteins or to develop new ones. 

We have conducted several development projects for our clients. As an example, we have engineered a yeast strain capable of consolidated bioprocessing for Mascoma Corp. 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 their reaction mechanisms as well as the improvement of enzyme properties through modern protein engineering techniques.

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

Our current activities are focused on engineering enzymes in metabolic pathways and functionalization of materials with proteins. 

Solid expertise in modern facilities

In addition to decades of experience we have an excellent infrastructure for protein development. Classic screening methods are utilized, as well as modern techniques based on genomes and metagenomics. High-throughput screening methods can be used by our robotic system. In order to characterize and study the properties of proteins we have a wide spectrum of spectroscopic and imaging instruments.

Most of our projects have been 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) 

 

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. http://www.ncbi.nlm.nih.gov/pubmed/25643956

 

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. http://www.ncbi.nlm.nih.gov/pubmed/25686794

 

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. http://www.ncbi.nlm.nih.gov/pubmed/25260922

 

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, www.mdpi.com/journal/microorganisms.

 

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. http://www.ncbi.nlm.nih.gov/pubmed/24419616

 

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. http://www.ncbi.nlm.nih.gov/pubmed/24692563

 

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. http://www.ncbi.nlm.nih.gov/pubmed/25236800

 

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. http://www.ncbi.nlm.nih.gov/pubmed/25454257

 

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. http://www.ncbi.nlm.nih.gov/pubmed/25187379

 

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. http://www.ncbi.nlm.nih.gov/pubmed/25079355

 

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. http://www.ncbi.nlm.nih.gov/pubmed/23949662

 

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. http://www.ncbi.nlm.nih.gov/pubmed/23920120

 

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. http://www.ncbi.nlm.nih.gov/pubmed/23608505

 

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. http://www.ncbi.nlm.nih.gov/pubmed/23759433

 

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. http://www.ncbi.nlm.nih.gov/pubmed/24034430

 

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. http://www.ncbi.nlm.nih.gov/pubmed/23484974

 

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. http://www.ncbi.nlm.nih.gov/pubmed/23428824

 

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. http://www.ncbi.nlm.nih.gov/pubmed/23560597

 

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. http://www.ncbi.nlm.nih.gov/pubmed/22608726

 

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. http://www.ncbi.nlm.nih.gov/pubmed/22493433

 

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. http://www.ncbi.nlm.nih.gov/pubmed/22655797

 

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. http://www.ncbi.nlm.nih.gov/pubmed/22315927

 

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. http://www.ncbi.nlm.nih.gov/pubmed/21676870

 

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. http://www.ncbi.nlm.nih.gov/pubmed/21535408

 

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. http://www.ncbi.nlm.nih.gov/pubmed/21885779

 

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. http://www.ncbi.nlm.nih.gov/pubmed/21702025

 

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. http://www.ncbi.nlm.nih.gov/pubmed/20736135

 

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. http://www.ncbi.nlm.nih.gov/pubmed/21488910

 

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. http://www.ncbi.nlm.nih.gov/pubmed/19921179

 

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. http://www.ncbi.nlm.nih.gov/pubmed/20377680

 

Protein engineering

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. http://www.ncbi.nlm.nih.gov/pubmed/25724119

 

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. http://www.ncbi.nlm.nih.gov/pubmed/25725398

 

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. http://www.ncbi.nlm.nih.gov/pubmed/25522202

 

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. http://www.ncbi.nlm.nih.gov/pubmed/23974371

 

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. http://www.ncbi.nlm.nih.gov/pubmed/24871427

 

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. http://www.ncbi.nlm.nih.gov/pubmed/23532843

 

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. http://www.ncbi.nlm.nih.gov/pubmed/23757174

 

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. http://www.ncbi.nlm.nih.gov/pubmed/23612175

 

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. http://www.ncbi.nlm.nih.gov/pubmed/22709678

 

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. http://www.ncbi.nlm.nih.gov/pubmed/22310297

 

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. http://www.ncbi.nlm.nih.gov/pubmed/21910902

 

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.  http://www.ncbi.nlm.nih.gov/pubmed/21541425

 

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. http://www.ncbi.nlm.nih.gov/pubmed/16219510

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. https://fi.linkedin.com/in/timopulli


Merja ItävaaraDr. Merja Itävaara, Principal Scientist, Principal Investigator


I have long experience and expertise in molecular microbial ecology, metagenomics and metatranscriptomics. Several solutions for industrial problems caused by microorganisms can be investigated and solutions found by applying methods based on ‘metaomics’. Geobiological processes in sulphide formation in deep earth crustal ecosystems and in deep groundwaters  have been the most recent topics of my research. Earlier I also worked on biodegradability and compostability of biodegradable plastics, organic pollutants, the quality criteria for compost growth media. I made my Ph.D thesis in cultivation of edible fungi. I have led several research teams on different topics, acted as scientist, senior scientist, group manager and now as principal scientist and principal investigator. I am also Adjunct Professor in Environmental Technology at University of Helsinki since 2003.
https://fi.linkedin.com/in/merja-itävaara-23b6b17

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: https://www.researchgate.net/profile/Anu_Koivula

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.
https://www.linkedin.com/in/martina-andberg-ba69103, https://www.researchgate.net/profile/Martina_Andberg, http://scholar.google.se/citations?user=d2AIFOkAAAAJ&hl=fi

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.
https://www.linkedin.com/in/harry-boer-79055234

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.
https://www.researchgate.net/profile/Kaisa_Marjamaa
https://www.linkedin.com/in/kaisa-marjamaa-7638b47a

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.

Arja PaananenDr. Arja Paananen, Senior Scientist


I have worked for VTT since 1997. My current research activities focus on hydrophobins in materials applications, and biophysical characterization of 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 received my MSc degree in Physical Chemistry at the University of Helsinki in 1996. In 2007 I finalised my PhD at the Åbo Akademi University, also in the field of Physical Chemistry. The PhD thesis focussed on the interactions and interfacial behaviour of biopolymers.

Marika EkroosMarika Ekroos, Research Scientist


I studied Bichemistry at Åbo Akademi University from where I have my M.Sc. degree. Before joining VTT in 2007 I worked at both international research institutes and at the pharmaceutical industry. At the European Molecular Biology Laboratory (EMBL) in Heidelberg, Germany my work focused on molecular biology and protein chemistry. I worked at the structural department focusing on protein characterization and solving protein structures with X-ray crystallography. At the Max-Planck institute for Molecular Cell Biology and Genetics I concentrated on understanding protein-lipid interactions. Then I moved to AstraZeneca (Mölndal, Sweden) where I did protein expression, purification, characterization and crystallization. At VTT I have been involved in various projects spanning from electrochemical microbiology to antibody-based sensor development.

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.
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