Enabling Low Cost Biopharmaceuticals: A Systematic Approach to Delete Proteases from a Well-Known Protein Production Host Trichoderma reesei.

Autor: Christopher P Landowski, Anne Huuskonen, Ramon Wahl, Ann Westerholm-Parvinen, Anne Kanerva, Anna-Liisa Hänninen, Noora Salovuori, Merja Penttilä, Jari Natunen, Christian Ostermeier, Bernhard Helk, Juhani Saarinen, Markku Saloheimo

Publikováno v: PLoS ONE, Vol 10, Iss 8, p e0134723 (2015)

The filamentous fungus Trichoderma reesei has tremendous capability to secrete proteins. Therefore, it would be an excellent host for producing high levels of therapeutic proteins at low cost. Developing a filamentous fungus to produce sensitive ther

Externí odkaz: https://doaj.org/article/ed9e1da5f3cc47a1ad32b7da38c7f35f

Electrophysiological characterization of a diverse group of sugar transporters from Trichoderma reesei

Autor: Sami Havukainen, Jonai Pujol-Giménez, Mari Valkonen, Ann Westerholm-Parvinen, Matthias A. Hediger, Christopher P. Landowski

Publikováno v: Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)

Abstract Trichoderma reesei is an ascomycete fungus known for its capability to secrete high amounts of extracellular cellulose- and hemicellulose-degrading enzymes. These enzymes are utilized in the production of second-generation biofuels and T. re

Externí odkaz: https://doaj.org/article/a3f3643ea6a143de8f982d5be4fdd2fb

Ovalbumin production using Trichoderma reesei culture and low-carbon energy could mitigate the environmental impacts of chicken-egg-derived ovalbumin

Autor: Natasha Järviö, Tuure Parviainen, Netta-Leena Maljanen, Yumi Kobayashi, Lauri Kujanpää, Dilek Ercili-Cura, Christopher P. Landowski, Toni Ryynänen, Emilia Nordlund, Hanna L. Tuomisto

Publikováno v: Järviö, N, Parviainen, T, Maljanen, N L, Kobayashi, Y, Kujanpää, L, Ercili-Cura, D, Landowski, C P, Ryynänen, T, Nordlund, E & Tuomisto, H L 2021, ' Ovalbumin production using Trichoderma reesei culture and low-carbon energy could mitigate the environmental impacts of chicken-egg-derived ovalbumin ', Nature Food, vol. 2, no. 12, pp. 1005-1013 . https://doi.org/10.1038/s43016-021-00418-2

Ovalbumin (OVA) produced using the fungus Trichoderma reesei (Tr-OVA) could become a sustainable replacement for chicken egg white protein powder—a widely used ingredient in the food industry. Although the approach can generate OVA at pilot scale,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d15f1977497feafbb38a65cdbdc2c3e9
http://hdl.handle.net/10138/347276

Single-Molecule Force Spectroscopy Study on Modular Resilin Fusion Protein

Autor: Arja Paananen, Päivi Laaksonen, Christopher P. Landowski, Karin Jacobs, Samuel Grandthyll, Hendrik Hähl, Marja Ilmen, Alessandra Griffo, Frank Müller, Merja Penttilä, Géza R. Szilvay

Publikováno v: Griffo, A, Hähl, H, Grandthyll, S, Müller, F, Paananen, A, Ilmén, M, Szilvay, G, Landowski, C P, Penttilä, M, Jacobs, K & Laaksonen, P 2017, ' Single-Molecule Force Spectroscopy Study on Modular Resilin Fusion Protein ', ACS Omega, vol. 2, no. 10, pp. 6906-6915 . https://doi.org/10.1021/acsomega.7b01133
ACS Omega, Vol 2, Iss 10, Pp 6906-6915 (2017)
ACS Omega

The adhesive and mechanical properties of a modular fusion protein consisting of two different types of binding units linked together via a flexible resilin-like-polypeptide domain are quantified. The adhesive domains have been constructed from funga

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb9b0d5821be3e0bdec871ed3878245e
https://doi.org/10.1021/acsomega.7b01133

Coacervation of resilin fusion proteins containing terminal functionalities

Autor: Wenwen Fang, Pezhman Mohammadi, Miika Soikkeli, Päivi Laaksonen, Ann Westerholm-Parvinen, Marika Vitikainen, Merja Penttilä, Markus Linder, Salla Koskela, Christopher P. Landowski, Nonappa

Publikováno v: Fang, W, Nonappa,, Vitikainen, M, Mohammadi, P, Koskela, S, Soikkeli, M, Westerholm-Parvinen, A, Landowski, C P, Penttilä, M, Linder, M B & Laaksonen, P 2018, ' Coacervation of resilin fusion proteins containing terminal functionalities ', Colloids and Surfaces B: Biointerfaces, vol. 171, pp. 590-596 . https://doi.org/10.1016/j.colsurfb.2018.07.048

Liquid-liquid phase transition known as coacervation of resilin-like-peptide fusion proteins containing different terminal domains were investigated. Two different modular proteins were designed and produced and their behavior were compared to a resi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08ab6e3873d3b5e27a442701faa7b3a8
https://aaltodoc.aalto.fi/handle/123456789/34005