Characterisation of steryl esterase activities in commercial lipase preparations

Autor: Maija Tenkanen, Tapani Reinikainen, Richard Fagerström, Hanna Kontkanen

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c97c650bcad61ca1e2787b478d4d27d
https://doi.org/10.1016/j.jbiotec.2003.11.003

Thermostable laccases produced by a white-rot fungus from Peniophora species

Autor: Marja-Leena Niku-Paavola, Kristiina Kruus, Richard Fagerström, Liisa Viikari

Publikováno v: Niku-Paavola, M-L, Fagerström, R, Kruus, K & Viikari, L 2004, ' Thermostable laccases produbed by a white-rot fungus from Peniophora species ', Enzyme and Microbial Technology, vol. 35, no. 1, pp. 100-102 . https://doi.org/10.1016/j.enzmictec.2004.03.008

A strain of Peniophora species was shown to produce laccase, which is a new feature for this species. Peniophora secreted several laccase isoforms with pI-values 3.7–4.2 when grown on glucose and soya meal medium. The Peniophora laccases were typic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0367003b388f70d92935a48b8b86b09
https://doi.org/10.1016/j.enzmictec.2004.03.008

Evidence for a polysaccharide-binding domain in Hormoconis resinae glucoamylase P: effects of its proteolytic removal on substrate specificity and inhibition by -cyclodextrin

Autor: Richard Fagerström

Publikováno v: Microbiology. 140:2399-2407

The hydrolysis of soluble starch, raw starch and pullulan with recombinant glucoamylase P from Hormoconis resinae was competitively inhibited by beta-cyclodextrin with apparent Ki values of 190 microM, 13 microM and 1.4 microM, respectively. Inhibiti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e53e5ca6d57d4ba80081acf2eee48a3e
https://doi.org/10.1099/13500872-140-9-2399

Comparison of two glucoamylases from Hormoconis resinae

Autor: Tiina Pakula, Kari Suoranta, Nisse Kalkkinen, Helena Torkkeli, Arja Vainio, Richard Fagerström

Publikováno v: Journal of General Microbiology. 136:913-920

SUMMARY: Two extracellular glucoamylases (EC 3.2.1.3), glucoamylase P and glucoamylase S, were purified to homogeneity from the culture medium of Hormoconis resinae (ATCC 20495; formerly Cladosporium resinae) by a new method. Their apparent molecular

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29d425375e4f783b2c923e96bd58751e
https://doi.org/10.1099/00221287-136-5-913

Large-scale separation and production of engineered proteins, designed for facilitated recovery in detergent-based aqueous two-phase extraction systems

Autor: Anna Collén, Merja Penttilä, Tiina Nakari-Setälä, Richard Fagerström, Joop van der Laan, M.-R. Kula, Folke Tjerneld, Michael Bailey, John Kan, Klaus Selber, Teppo Hyytiä

Publikováno v: Selber, K, Tjerneld, F, Collén, A, Hyytiä, T, Nakari-Setälä, T, Bailey, M, Fagerström, R, Kan, J, Van Der Laan, J, Penttilä, M & Kula, M R 2004, ' Large-scale separation and production of engineered proteins, designed for facilitated recovery in detergent-based aqueous two-phase extraction systems ', Process Biochemistry, vol. 39, no. 7, pp. 889-896 . https://doi.org/10.1016/S0032-9592(03)00198-5

The feasibility and scalability of extraction in detergent-based aqueous two-phase systems for the separation of proteins from culture broth is demonstrated. At the same time the large-scale production of a fusion protein and the influence of cultiva

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd2c4d741bb39609bb8247ea5150bbc1
https://cris.vtt.fi/en/publications/1b950585-61f9-44cd-9b5d-c7847ea65783