Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Arja Mäntylä"'
Autor:
Marja Paloheimo, Arja Mäntylä, Raija Lantto, Sanna Leskinen, Jari Vehmaanperä, Richard Fagerstrom, Pirkko Suominen
Publikováno v:
Leskinen, S, Mäntylä, A, Fagerström, R, Vehmaanperä, J, Lantto, R, Paloheimo, M & Suominen, P 2005, ' Thermostable xylanases, Xyn10A and Xyn11A, from the actinomycete Nonomuraea flexuosa : solation of the genes and characterization of recombinant Xyn11A polypeptides produced in Trichoderma reesei ', Applied Microbiology and Biotechnology, vol. 67, no. 4, pp. 495-505 . https://doi.org/10.1007/s00253-004-1797-x
Two endoxylanases, Nf Xyn11A and Nf Xyn10A, were cloned from a Nonomuraea flexuosa (previously Actinomadura flexuosa) DSM43186 genomic expression library in Escherichia coli. The coding sequences of xyn11A and xyn10A consist of 344 and 492 amino acid
Autor:
Heli Haakana, Vesa Joutsjoki, Jari Vehmaanperä, Arja Miettinen-Oinonen, Arja Mäntylä, Pirkko Suominen
Publikováno v:
Haakana, H, Miettinen-Oinonen, A, Joutsjoki, V, Mäntylä, A, Suominen, P & Vehmaanperä, J 2004, ' Cloning of cellulase genes from Melanocarpus albomyces and their efficient expression in Trichoderma reesei ', Enzyme and Microbial Technology, vol. 34, no. 2, pp. 159-167 . https://doi.org/10.1016/j.enzmictec.2003.10.009
In our previous study, three purified cellulases of Melanocarpus albomyces proved to be effective in biostoning application at neutral pH [Enzyme Microb. Technol., accepted for publication]. We cloned and sequenced three genes of M. albomyces, which
Publikováno v:
Applied and Environmental Microbiology. 69:7073-7082
A bacterial xylanase gene, Nonomuraea flexuosa xyn11A , was expressed in the filamentous fungus Trichoderma reesei from the strong cellobiohydrolase 1 promoter as fusions to a variety of carrier polypeptides. By using single-copy isogenic transforman
Autor:
Arja Lappalainen, Tuula T. Teeri, Pirkko Suominen, Susanna Virtanen, Arja Mäntylä, Anu Koivula
Publikováno v:
Koivula, A, Lappalainen, A, Virtanen, S, Mäntylä, A, Suominen, P & Teeri, T 1996, ' Immunoaffinity chromatographic purification of cellobiohydrolase II mutants from recombinant Trichoderma reesei strains devoid of major endoglucanase genes ', Protein Expression and Purification, vol. 8, no. 4, pp. 391-400 . https://doi.org/10.1006/prep.1996.0116
Efficient purification of Trichoderma reesei cellobiohydrolase II (CBHII) requires the use of affinity chromatography based on a substrate analogue. Due to altered substrate binding, the purification of many active-site mutants of CBHII from the comp
Autor:
Arja Mäntylä, K. Hannele Rossi, K. M. Helena Nevalainen, Sirpa A. Vanhanen, Pirkko Suominen, Merja Penttilä
Publikováno v:
Mäntylä, A L, Rossi, K H, Vanhanen, S A, Penttilä, M E, Suominen, P L & Nevalainen, K M H 1992, ' Electrophoretic karyotyping of wild-type and mutant Trichoderma longibrachiatum (reesei) strains ', Current Genetics, vol. 21, no. 6, pp. 471-477 . https://doi.org/10.1007/BF00351657
An electrophoretic karyotype of Trichoderma longibrachiatum (reesei) was obtained using contourclamped homogeneous electric field (CHEF) gel electrophoresis. Seven chromosomal DNA bands were separated in the wild-type T. longibrachiatum strain QM6a.
Autor:
Arja Mäntylä, Rolf Bühler, Merja Penttilä, Susanna Muttilainen, Jonathan Knowles, Pirkko Suominen, Helena Nevalainen, Anu Marjukka Harkki
Publikováno v:
Harkki, A, Mäntylä, A, Penttilä, M, Muttilainen, S, Bühler, R, Suominen, P, Knowles, J & Nevalainen, H 1991, ' Genetic engineering of Trichoderma to produce strains with novel cellulase profiles ', Enzyme and Microbial Technology, vol. 13, no. 3, pp. 227-233 . https://doi.org/10.1016/0141-0229(91)90133-U
Genetic engineering has been used to modify the proportion of different cellulases produced by a hypercellulolytic Trichoderma reesei mutant strain. A general expression vector, pAMH110, containing the promoter and terminator sequences of the strongl
Publikováno v:
Applied and environmental microbiology. 73(10)
We have previously shown that the Nonomuraea flexuosa Xyn11A polypeptides devoid of the carbohydrate binding module (CBM) have better thermostability than the full-length xylanase and are effective in bleaching of pulp. To produce an enzyme preparati
Autor:
Pirkko Suominen, Sanna Leskinen, Satu Hakola, Jari Vehmaanperä, Marja Paloheimo, Raija Lantto, Emilia Lindberg, Arja Mäntylä, Jarno Kallio
Publikováno v:
Mäntylä, A, Paloheimo, M, Hakola, S, Leskinen, S, Kallio, J, Vehmaanperä, J, Lantto, R, Suominen, P & Lindberg, E 2007, ' Production in Trichoderma reesei of three xylanases from Chaetomium thermophilum : A recombinant thermoxylanase for biobleaching of kraft pulp ', Applied Microbiology and Biotechnology, vol. 76, no. 2, pp. 377-386 . https://doi.org/10.1007/s00253-007-1020-y
Three endoxylanase genes were cloned from the thermophilic fungus Chaetomium thermophilum CBS 730.95. All genes contained the typical consensus sequence of family 11 glycoside hydrolases. Genomic copies of Ct xyn11A, Ct xyn11B, and Ct xyn11C were exp
Publikováno v:
Macquarie University
The gene for barley endopeptidase B (EPB) has been expressed in the filamentous fungus Trichoderma reesei from the cbh1 promoter. The EPB signal sequence allowed secretion of over 90% of the recombinant protein. Yields reached about 500 mg of immunor
Autor:
Ron T. Wester, Helena Nevalainen, Jon B. Cooper, J. E. Pitts, Phil Nugent, Mark D. Crawford, Richard Fagerstrom, Arja Mäntylä
Publikováno v:
Aspartic Proteinases ISBN: 9781461357612
Aspartic proteinases comprise a family of proteolytic enzymes found in a diverse range of species, from vertebrates, to lower eukaryotes and retroviruses. They are active at neutral or low pH. They are all characterised by the presence of two asparti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cddca8f07edc3d9643a93a645b6bfbc4
https://doi.org/10.1007/978-1-4615-1871-6_70
https://doi.org/10.1007/978-1-4615-1871-6_70