Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Hanna Kontkanen"'
Autor:
Kristiina Kruus, Susanna Rokka, Raija Lantto, Eila Järvenpää, Antti Nyyssölä, Hanna Kontkanen, Riitta Partanen, Martina Lille, Hanna Miettinen
Publikováno v:
Nyyssölä, A, Miettinen, H, Kontkanen, H, Lille, M, Partanen, R, Rokka, S, Järvenpää, E, Lantto, R & Kruus, K 2015, ' Treatment of milk fat with sn-2 specific Pseudozyma antarctica lipase A for targeted hydrolysis of saturated medium and long-chain fatty acids ', International Dairy Journal, vol. 41, pp. 16-22 . https://doi.org/10.1016/j.idairyj.2014.09.003
Milk fat was treated with the sn- 2 specific PAN-2 lipase from Pseudozyma antarctica with the aim of achieving selective removal of saturated fatty acids with chain lengths between C12 and C16, which are abundant at the sn- 2 position. Hydrolysis was
Publikováno v:
Miettinen, H, Nyyssölä, A, Rokka, S, Kontkanen, H & Kruus, K 2013, ' Screening of microbes for lipases specific for saturated medium and long-chain fatty acids of milk fat ', International Dairy Journal, vol. 32, no. 2, pp. 61-67 . https://doi.org/10.1016/j.idairyj.2013.05.007
Over 250 microbial strains were screened for lipase activity specific towards saturated medium and long-chain fatty acids. Strains showing trimyristin (C14:0) hydrolysis on agar medium were further streaked on tricaprylin (C8:0) and on olive oil (mos
Autor:
Johanna Buchert, Marjaana Rättö, Ann Westerholm-Parvinen, Ismo Mattila, Tiina Nakari-Setälä, Marzia Mohsina, Michael Bailey, Markku Saloheimo, Hanna Kontkanen, Nisse Kalkkinen
Publikováno v:
Kontkanen, H, Westerholm-Parvinen, A, Saloheimo, M, Bailey, M, Rättö, M, Mattila, I, Mohsina, M, Kalkkinen, N, Nakari-Setälä, T & Buchert, J 2009, ' Novel Coprinopsis cinerea Polyesterase that hydrolyzes cutin and Suberin ', Applied and Environmental Microbiology, vol. 75, no. 7, pp. 2148-2157 . https://doi.org/10.1128/AEM.02103-08
Three cutinase gene-like genes from the basidiomycete Coprinopsis cinerea ( Coprinus cinereus ) found with a similarity search were cloned and expressed in Trichoderma reesei under the control of an inducible cbh1 promoter. The selected transformants
Publikováno v:
Kontkanen, H, Reinikainen, T & Saloheimo, M 2006, ' Cloning and expression of a Melanocarpus albomyces steryl esterase gene in Pichia pastoris and Trichoderma reesei ', Biotechnology and Bioengineering, vol. 94, no. 3, pp. 407-415 . https://doi.org/10.1002/bit.20686
The ste1 gene encoding a steryl esterase was isolated from the thermophilic fungus Melanocarpus albomyces. The gene has one intron, and it encodes a protein consisting of 576 amino acids. The deduced amino acid sequence of the steryl esterase was sho
Publikováno v:
Kontkanen, H, Tenkanen, M, Fagerström, R & Reinikainen, T 2004, ' Characterisation of steryl esterase activities in commercial lipase preparations ', Journal of Biotechnology, vol. 108, no. 1, pp. 51-59 . https://doi.org/10.1016/j.jbiotec.2003.11.003
Triglycerides, steryl esters, resin acids, free fatty acids and sterols are lipophilic extractives of wood (commonly referred to as pitch or wood resin) and have a negative impact on paper machine runnability and quality of paper. Thus, enzymes capab
Publikováno v:
Tenkanen, M, Kontkanen, H, Isoniemi, R, Spetz, P & Holmbom, B 2002, ' Hydrolysis of steryl esters by a lipase (Lip 3) from Candida rugosa ', Applied Microbiology and Biotechnology, vol. 60, no. 1-2, pp. 120-127 . https://doi.org/10.1007/s00253-002-1063-z
A well-known lipase, Lip 3 of Candida rugosa, was purified to homogeneity from a commercial lipase preparation, using hydrophobic interaction and anion exchange chromatography. Lip 3, which has been reported to act on cholesteryl esters, was also fou
Autor:
Antti Nyyssölä, Alain Roussel, Ann Westerholm-Parvinen, Stéphanie Blangy, Frédéric Carrière, Sawsan Amara, Eduardo Mateos-Diaz, Hanna Kontkanen, Christian Cambillau
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2014, 426 (22), pp.3757-3772. ⟨10.1016/j.jmb.2014.09.003⟩
Journal of Molecular Biology, 2014, 426 (22), pp.3757-3772. ⟨10.1016/j.jmb.2014.09.003⟩
Roussel, A, Amara, S, Nyyssölä, A, Mateos-Diaz, E, Blangy, S, Kontkanen, H, Westerholm-Parvinen, A, Carriere, F & Cambillau, C 2014, ' A Cutinase from Trichoderma reesei with a lid-covered active site and kinetic properties of true lipases ', Journal of Molecular Biology, vol. 426, no. 22, pp. 3757-3772 . https://doi.org/10.1016/j.jmb.2014.09.003
Journal of Molecular Biology, Elsevier, 2014, 426 (22), pp.3757-3772. ⟨10.1016/j.jmb.2014.09.003⟩
Journal of Molecular Biology, 2014, 426 (22), pp.3757-3772. ⟨10.1016/j.jmb.2014.09.003⟩
Roussel, A, Amara, S, Nyyssölä, A, Mateos-Diaz, E, Blangy, S, Kontkanen, H, Westerholm-Parvinen, A, Carriere, F & Cambillau, C 2014, ' A Cutinase from Trichoderma reesei with a lid-covered active site and kinetic properties of true lipases ', Journal of Molecular Biology, vol. 426, no. 22, pp. 3757-3772 . https://doi.org/10.1016/j.jmb.2014.09.003
Cutinases belong to the α/β-hydrolase fold family of enzymes and degrade cutin and various esters, including triglycerides, phospholipids and galactolipids. Cutinases are able to degrade aggregated and soluble substrates because, in contrast with t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a46415fa2a5a6fe0393abf8913c73350
https://hal.archives-ouvertes.fr/hal-02066305
https://hal.archives-ouvertes.fr/hal-02066305
Autor:
Tiina Nakari-Setälä, Hanna Kontkanen, Ville Pihlajaniemi, Mari Häkkinen, Markku Saloheimo, Antti Nyyssölä
Publikováno v:
Nyyssölä, A, Pihlajaniemi, V, Häkkinen, M, Kontkanen, H, Saloheimo, M & Nakari-Setälä, T 2014, ' Cloning and characterization of a novel acidic cutinase from Sirococcus conigenus ', Applied Microbiology and Biotechnology, vol. 98, no. 8, pp. 3639-3650 . https://doi.org/10.1007/s00253-013-5293-z
A cutinase gene (ScCut1) was amplified by PCR from the genomic DNA of the ascomycetous plant pathogen Sirococcous conigenus VTT D-04989 using degenerate primers designed on the basis of conserved segments of known cutinases and cutinase-like enzymes.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0eaa435daa2f2bc9b36fa1d387ef148b
https://cris.vtt.fi/en/publications/2500de60-783f-413c-a1c8-c832daa94f59
https://cris.vtt.fi/en/publications/2500de60-783f-413c-a1c8-c832daa94f59
Autor:
Hanna Kontkanen, Saara Mikander, Heikki Kallio, Johanna Buchert, Ville Pihlajaniemi, Antti Nyyssölä, Kristiina Kruus, Riikka Järvinen
Publikováno v:
Nyyssölä, A, Pihlajaniemi, V, Järvinen, R, Mikander, S, Kontkanen, H, Kruus, K, Kallio, H & Buchert, J 2013, ' Screening of microbes for novel acidic cutinases and cloning and expression of an acidic cutinase from Aspergillus niger CBS 513.88 ', Enzyme and Microbial Technology, vol. 52, no. 4-5, pp. 272-278 . https://doi.org/10.1016/j.enzmictec.2013.01.005
Isolates from gardening waste compost and 38 culture collection microbes were grown on agar plates at pH 4.0 with the cutinase model substrate polycaprolactone as a carbon source. The strains showing polycaprolactone hydrolysis were cultivated in liq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b2999b609eebe34ae71fe4a08263f41
https://cris.vtt.fi/en/publications/a31890f3-a827-46d2-a481-9dfa23b84d85
https://cris.vtt.fi/en/publications/a31890f3-a827-46d2-a481-9dfa23b84d85
Autor:
Hanna Kontkanen, Hannu Korhonen, Kristiina Kruus, Pertti Marnila, Jarkko Hellström, Hanna Miettinen, Susanna Rokka, Tapani Alatossava, Asmo Kemppinen
Publikováno v:
Kontkanen, H, Rokka, S, Kemppinen, A, Miettinen, H, Hellström, J, Kruus, K, Marnila, P, Alatossava, T & Korhonen, H 2011, ' Enzymatic and physical modification of milk fat : A review ', International Dairy Journal, vol. 21, no. 1, pp. 3-13 . https://doi.org/10.1016/j.idairyj.2010.05.003
Bovine milk fat has one of the most complex compositions of all natural fats. It is composed of more than 400 different fatty acids, present primarily as triacylglycerols, which gives milk fat highly diverse functional and nutritional properties. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d3c6c1ddb3ce04fdeb9b14f7e24d0ce
https://cris.vtt.fi/en/publications/d342538f-b7c5-4e87-a3b3-fed5e5237014
https://cris.vtt.fi/en/publications/d342538f-b7c5-4e87-a3b3-fed5e5237014