Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Terhi K. Hakala"'
Autor:
Heli Kangas, Terhi K. Hakala, Tarja Tamminen, Marjo Määttänen, Stella Rovio, Tiina Liitiä, Kristiina Poppius-Levlin
Publikováno v:
BioResources, Vol 10, Iss 2, Pp 2699-2718 (2015)
Birch wood chips were cooked in acetic acid in the presence of phosphinic acid according to the Lignofibre (LGF) organosolv process. The cooking trials were performed according to an experimental design with process time, temperature, and the presenc
Externí odkaz:
https://doaj.org/article/7ba05805dde64d1c9064a09372d64eeb
Publikováno v:
Applied Microbiology and Biotechnology. 77:301-309
The white-rot basidiomycete Physisporinus rivulosus strain T241i is highly selective for degradation of softwood lignin, which makes this fungus suitable for biopulping. In order to promote laccase production, P. rivulosus was cultivated in nutrient-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d690b8813a64c9276e53849ec1138f9
https://doi.org/10.1007/s00253-007-1155-x
https://doi.org/10.1007/s00253-007-1155-x
Publikováno v:
Applied Microbiology and Biotechnology. 73:839-849
Manganese peroxidase (MnP) production in the white-rot basidiomycete Physisporinus rivulosus T241i was studied. Separate MnP isoforms were produced in carbon-limited liquid media supplemented with Mn(2+), veratryl alcohol, or sawdust. The isoforms ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eecc62f75aaa6683a5f6b74d992f1496
https://doi.org/10.1007/s00253-006-0541-0
https://doi.org/10.1007/s00253-006-0541-0
Publikováno v:
Current Genetics. 50:323-333
Laccases are phenol-oxidizing, multicopper enzymes produced by fungi, plants, insects and bacteria. Fungal laccases are involved in ecologically important processes such as decomposition of lignocellulose (wood and plant material). In this work, in o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5aacfa1cdfa3631b420419b46d035179
https://doi.org/10.1007/s00294-006-0090-1
https://doi.org/10.1007/s00294-006-0090-1
Publikováno v:
Enzyme and Microbial Technology. 36:461-468
The white-rot fungus Physisporinus rivulosus T241i produced manganese peroxidase (MnP), laccase, and oxalic acid when it was grown on spruce ( Picea abies ) wood chips. This white-rot basidiomycete degrades lignin selectively and is promising for use
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c0453ac0b600c437c77a72f52c9c6b06
https://doi.org/10.1016/j.enzmictec.2004.10.004
https://doi.org/10.1016/j.enzmictec.2004.10.004
Publikováno v:
Enzyme and Microbial Technology. 34:255-263
Pre-treatment of wood chips with white-rot fungi (i.e. biopulping) has previously been shown to decrease the energy consumption in mechanical pulping. In this study, promising novel fungal isolates were found for biopulping of Norway spruce ( Picea a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9b3e97038fee612eb829c150a33c3012
https://doi.org/10.1016/j.enzmictec.2003.10.014
https://doi.org/10.1016/j.enzmictec.2003.10.014
Publikováno v:
Biotechnology letters. 31(8)
Laccases are phenol-oxidizing, usually four-copper containing metalloenzymes. For industrial and biotechnological purposes, laccases were among the first fungal oxidoreductases providing larger-scale applications such as removal of polyphenols in win
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e6dd93456a4cb2c2ce7629fb6547cd3
https://pubmed.ncbi.nlm.nih.gov/19360388
https://pubmed.ncbi.nlm.nih.gov/19360388
Publikováno v:
Current genetics. 49(2)
Lignin peroxidase (LiP) is the first enzyme connected to oxidative breakdown of the aromatic plant heteropolymer lignin and related xenobiotics. However, this extracellular enzyme has been described in only a few species of wood-decaying basidiomycet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a085149aa6bd8cd17637fc373c331afa
https://pubmed.ncbi.nlm.nih.gov/16333658
https://pubmed.ncbi.nlm.nih.gov/16333658
