Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Isabelle Housen"'
Publikováno v:
Vandamme, A-M, Michaux, C, Mayard, A & Housen, I 2013, ' Asparagine 42 of the conserved endo-inulinase INU2 motif WMNDPN from Aspergillus ficuum plays a role in activity specificity ', FEBS open bio, vol. 3, pp. 467-72 . https://doi.org/10.1016/j.fob.2013.10.009
FEBS Open Bio
FEBS Open Bio
Endo-inulinase INU2 from Aspergillus ficuum belongs to glycosidase hydrolase family 32 (GH32) that degrades inulin into fructo oligosaccharides consisting mainly of inulotriose and inulotetraose. The 3D structure of INU2 was recently obtained (Pouyez
Autor:
Guillaume Roussel, Anne-Michèle Vandamme, Aurélie Mayard, Johan Wouters, Eric A. Perpète, Jenny Pouyez, Isabelle Housen, Catherine Michaux
Publikováno v:
Biochimie. 94:2423-2430
Endo-inulinase is a member of glycosidase hydrolase family 32 (GH32) degrading fructans of the inulin type with an endo-cleavage mode and is an important class of industrial enzyme. In the present study, we report the first crystal structure of an en
Autor:
Catherine Michaux, Jenny Pouyez, Isabelle Housen, Johan Wouters, Pierre Vandurm, Aurélie Mayard
Publikováno v:
Biochimie. 92:1407-1415
In this study, the crystal structure of a novel endo-1,4-β-xylanase from Scytalidium acidophilum, XYL1, was solved at 1.9. Å resolution. This is one of the few solved crystal structures of acidophilic proteins. The enzyme has the overall fold typic
Autor:
Kurt Gebruers, Jean Vandenhaute, Isabelle Housen, Kristof Brijs, Bassam Al Balaa, Johan Wouters
Publikováno v:
Bioresource Technology. 100:6465-6471
The role of residues Asp60, Tyr35 and Glu141 in the pH-dependent activity of xylanase XYL1p from Scytalidium acidophilum was investigated by site-directed mutagenesis. These amino acids are highly conserved among the acidophilic family 11 xylanases a
Autor:
Sophie Dogné, Eric Depiereux, Jean Michel Schaus, Bassam Al Balaa, Jean Vandenhaute, Johan Wouters, Isabelle Housen, Carlos Rossini
Publikováno v:
Bioscience, biotechnology and biochemistry. 70(1):269-272
We cloned XYL1, a Scytalidium acidophilum gene encoding for an acidophilic family 11 xylanase. The XYL1p protein was expressed in Pichia pastoris using the pPICZalphaA expression plasmid. The secreted protein was purified by TAXI affinity column chro
Publikováno v:
Yeast. 13:777-781
The KlDIM1 gene encoding the m2(6)A rRNA dimethylase was cloned from a Kluyveromyces lactis genomic library using a PCR amplicon from the Saccharomyces cerevisiae ScDIM1 gene as probe. The KlDIM1 gene encodes a 320-amino acid protein which shows 81%
Publikováno v:
Biochimie. 102
A new multicopper oxidase gene AaMco1 was identified in Acidomyces acidophilus, a pigmented extremophile ascomycete originally isolated from acidic water. Sequence analysis revealed that it encodes a 682 amino acid protein with an apparent molecular
Autor:
Mi Sun Chung, Tai-Boong Uhm, Jean Vandenhaute, Bernard Haye, Sun Hee Lee, Jong Hwa Kim, Josef van Beeumen, Françoise Gourronc, Isabelle Housen
Publikováno v:
Bioscience, biotechnology, and biochemistry. 63(1)
Endoinulinase from Aspergillus ficuum, which catalyzes the hydrolysis of inulin via an endo-cleavage mode, was purified by chromatography from Novozym 230 as a starting commercial enzyme mixture on CM-Sephadex and DEAE-Sepharose, and by preparative e