Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Martina, Andberg"'
Publikováno v:
Fungal Biology and Biotechnology, Vol 6, Iss 1, Pp 1-13 (2019)
Abstract Background Crude glycerol coming from biodiesel production is an attractive carbon source for biological production of chemicals. The major impurity in preparations of crude glycerol is methanol, which is toxic for most microbes. Development
Externí odkaz:
https://doaj.org/article/c2712428d331409fb45f2ddad0458557
Autor:
Senthil K. Thangaraj, Sanni Voutilainen, Martina Andberg, Anu Koivula, Janne Jänis, Juha Rouvinen
Publikováno v:
ACS Omega, Vol 4, Iss 8, Pp 13447-13453 (2019)
Externí odkaz:
https://doaj.org/article/0ba09fb1917c4ef2aa001d0c3586c3fe
Publikováno v:
AMB Express, Vol 9, Iss 1, Pp 1-13 (2019)
Abstract The oxidative d-xylose pathway, i.e. Dahms pathway, can be utilised to produce from cheap biomass raw material useful chemical intermediates. In vitro metabolic pathways offer a fast way to study the rate-limiting steps and find the most sui
Externí odkaz:
https://doaj.org/article/84061153233442359e6f38f12ba46191
Publikováno v:
Applied Microbiology and Biotechnology
Rouvinen, J, Andberg, M, Pääkkönen, J, Hakulinen, N & Koivula, A 2021, ' Current state of and need for enzyme engineering of 2-deoxy-D-ribose 5-phosphate aldolases and its impact ', Applied Microbiology and Biotechnology, vol. 105, no. 16-17, pp. 6215-6228 . https://doi.org/10.1007/s00253-021-11462-0
Rouvinen, J, Andberg, M, Pääkkönen, J, Hakulinen, N & Koivula, A 2021, ' Current state of and need for enzyme engineering of 2-deoxy-D-ribose 5-phosphate aldolases and its impact ', Applied Microbiology and Biotechnology, vol. 105, no. 16-17, pp. 6215-6228 . https://doi.org/10.1007/s00253-021-11462-0
Abstract Deoxyribose-5-phosphate aldolases (DERAs, EC 4.1.2.4) are acetaldehyde-dependent, Class I aldolases catalyzing in nature a reversible aldol reaction between an acetaldehyde donor (C2 compound) and glyceraldehyde-3-phosphate acceptor (C3 comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::730d74615e737cef128b57b9fe233419
http://europepmc.org/articles/PMC8403123
http://europepmc.org/articles/PMC8403123
Autor:
Emmi Jokinen, Sanni Voutilainen, Markus Heinonen, Hannu Maaheimo, Anu Koivula, Martina Andberg, Juho Rousu, Juha Rouvinen, Merja Penttilä, Harri Lähdesmäki, Samuel Kaski, Johan Pääkkönen, Nina Hakulinen
Publikováno v:
Applied Microbiology and Biotechnology
Voutilainen, S, Heinonen, M, Andberg, M, Jokinen, E, Maaheimo, H, Pääkkönen, J, Hakulinen, N, Rouvinen, J, Lähdesmäki, H, Kaski, S, Rousu, J, Penttilä, M & Koivula, A 2020, ' Substrate specificity of 2-deoxy-D-ribose 5-phosphate aldolase (DERA) assessed by different protein engineering and machine learning methods ', Applied Microbiology and Biotechnology, vol. 104, no. 24, pp. 10515-10529 . https://doi.org/10.1007/s00253-020-10960-x
'Applied Microbiology and Biotechnology ', vol: 104, pages: 10515-10529 (2020)
Voutilainen, S, Heinonen, M, Andberg, M, Jokinen, E, Maaheimo, H, Pääkkönen, J, Hakulinen, N, Rouvinen, J, Lähdesmäki, H, Kaski, S, Rousu, J, Penttilä, M & Koivula, A 2020, ' Substrate specificity of 2-deoxy-D-ribose 5-phosphate aldolase (DERA) assessed by different protein engineering and machine learning methods ', Applied Microbiology and Biotechnology, vol. 104, no. 24, pp. 10515-10529 . https://doi.org/10.1007/s00253-020-10960-x
'Applied Microbiology and Biotechnology ', vol: 104, pages: 10515-10529 (2020)
Abstract In this work, deoxyribose-5-phosphate aldolase (Ec DERA, EC 4.1.2.4) from Escherichia coli was chosen as the protein engineering target for improving the substrate preference towards smaller, non-phosphorylated aldehyde donor substrates, in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1df04bea6ee5917b68fa5f071bc2b647
https://doi.org/10.1007/s00253-020-10960-x
https://doi.org/10.1007/s00253-020-10960-x
Autor:
Terhi Saarinen, Hannes Orelma, Stina Grönqvist, Martina Andberg, Susanna Holappa, Janne Laine
Publikováno v:
BioResources, Vol 4, Iss 1, Pp 94-110 (2009)
The adsorption of Trametes hirsuta and Melanocarpus albomyces laccases on cellulose and lignin model substrates was studied by quartz crystal microbalance with dissipation, QCM-D. The laccase-treated surfaces were also analyzed by atomic force micros
Externí odkaz:
https://doaj.org/article/f92b509b0032415d9bd7aeae404a6c56
Publikováno v:
Protein science : a publication of the Protein Society. 31(2)
Xylonolactonase Cc XylC from Caulobacter crescentus catalyzes the hydrolysis of the intramolecular ester bond of d-xylonolactone. We have determined crystal structures of Cc XylC in complex with d-xylonolactone isomer analogues d-xylopyranose and (r)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5e21408663ab4f2cfac5df7b039cf093
https://pubmed.ncbi.nlm.nih.gov/34761460
https://pubmed.ncbi.nlm.nih.gov/34761460
Autor:
Nina, Aro, Dilek, Ercili-cura, Martina, Andberg, Pia, Silventoinen, Martina, Lille, Waltteri, Hosia, Emilia, Nordlund, Landowski christopher, P.
Publikováno v:
Nina, A, Dilek, E, Martina, A, Pia, S, Martina, L, Waltteri, H, Emilia, N & Landowski christopher, P 2023, ' Production of bovine beta-lactoglobulin and hen egg ovalbumin by Trichoderma reesei using precision fermentation technology and testing of their techno-functional properties ', Food Research International, vol. 163, 112131, pp. 112131 . https://doi.org/10.1016/j.foodres.2022.112131
The food protein ingredient market is dominated by dairy and egg proteins. Both milk whey and egg proteins are challenging proteins to replace, e.g. with plant proteins, due to the unique structural features of the animal proteins that render them hi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::430d1da54082251aed7940fa5e0978dd
https://doi.org/10.1016/j.foodres.2022.112131
https://doi.org/10.1016/j.foodres.2022.112131
Autor:
Janne Jänis, Mohammad Mubinur Rahman, Merja Penttilä, Martina Andberg, Senthil K. Thangaraj, Nina Hakulinen, Tarja Parkkinen, Juha Rouvinen, Anu Koivula
Publikováno v:
Rahman, M, Andberg, M, Thangaraj, S, Parkkinen, T, Penttilä, M, Jänis, J, Koivula, A, Rouvinen, J & Hakulinen, N 2017, ' The Crystal Structure of a Bacterial l-Arabinonate Dehydratase Contains a [2Fe-2S] Cluster ', ACS Chemical Biology, vol. 12, no. 7, pp. 1919-1927 . https://doi.org/10.1021/acschembio.7b00304
We present a novel crystal structure of the IlvD/EDD family enzyme, l-arabinonate dehydratase from Rhizobium leguminosarum bv. trifolii (RlArDHT, EC 4.2.1.25), which catalyzes the conversion of l-arabinonate to 2-dehydro-3-deoxy-L-arabinonate. The en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33b227c96364985554dff6ebd8f76f39
http://juuli.fi/Record/0284346517
http://juuli.fi/Record/0284346517
Autor:
Paul Carlson, Martina Andberg, Merja Oja, Anu Koivula, Merja Penttilä, Sophie Bozonnet, Niina Hakulinen, Niina Aro-Kärkkäinen, Mervi Toivari, Michael J. O’Donohue
Publikováno v:
Applied Microbiology and Biotechnology
Applied Microbiology and Biotechnology, 2016, 100 (17), pp.7549-7563. ⟨10.1007/s00253-016-7530-8⟩
Applied Microbiology and Biotechnology, Springer Verlag, 2016, 100 (17), pp.7549-7563. ⟨10.1007/s00253-016-7530-8⟩
Andberg, M, Aro-Kärkkäinen, N, Carlson, P, Oja, M, Bozonnet, S, Toivari, M, Hakulinen, N, O'Donohue, M, Penttilä, M & Koivula, A 2016, ' Characterization and mutagenesis of two novel iron-sulphur cluster pentonate dehydratases ', Applied Microbiology and Biotechnology, vol. 100, no. 17, pp. 7549-7563 . https://doi.org/10.1007/s00253-016-7530-8
Applied Microbiology and Biotechnology, 2016, 100 (17), pp.7549-7563. ⟨10.1007/s00253-016-7530-8⟩
Applied Microbiology and Biotechnology, Springer Verlag, 2016, 100 (17), pp.7549-7563. ⟨10.1007/s00253-016-7530-8⟩
Andberg, M, Aro-Kärkkäinen, N, Carlson, P, Oja, M, Bozonnet, S, Toivari, M, Hakulinen, N, O'Donohue, M, Penttilä, M & Koivula, A 2016, ' Characterization and mutagenesis of two novel iron-sulphur cluster pentonate dehydratases ', Applied Microbiology and Biotechnology, vol. 100, no. 17, pp. 7549-7563 . https://doi.org/10.1007/s00253-016-7530-8
We describe here the identification and characterization of two novel enzymes belonging to the IlvD/EDD protein family, the D-xylonate dehydratase from Caulobacter crescentus, Cc XyDHT, (EC 4.2.1.82), and the L-arabonate dehydratase from Rhizobium le
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce6f9bb3a1d54cb5f1d8cb65e681e742
https://doi.org/10.1007/s00253-016-7530-8
https://doi.org/10.1007/s00253-016-7530-8