Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Alizée Vergès"'
Autor:
David Daudé, Alizée Vergès, Magali Remaud-Simeon, Stéphane Emond, Isabelle André, Emmanuelle Cambon, Samuel Tranier
Publikováno v:
'ACS Catalysis ', vol: 9, pages: 1241-1252 (2019)
ACS Catalysis
ACS Catalysis, American Chemical Society, 2019, 9 (2), pp.1241-1252. ⟨10.1021/acscatal.8b03609⟩
ACS Catalysis, 2019, 9 (2), pp.1241-1252. ⟨10.1021/acscatal.8b03609⟩
ACS Catalysis
ACS Catalysis, American Chemical Society, 2019, 9 (2), pp.1241-1252. ⟨10.1021/acscatal.8b03609⟩
ACS Catalysis, 2019, 9 (2), pp.1241-1252. ⟨10.1021/acscatal.8b03609⟩
Neutral drift (also called purifying selection) is an attractive approach to generate polymorphic variant libraries for enzyme engineering. Here, we have applied this strategy to modify the substrate specificity of a transglucosylase. Our model enzym
Autor:
Magali Remaud-Simeon, Sophie Barbe, Isabelle André, Emmanuelle Cambon, Claire Moulis, Alizée Vergès
Publikováno v:
Protein Science. 26:566-577
A computer-aided engineering approach recently enabled to deeply reshape the active site of N. polysaccharea amylosucrase for recognition of non-natural acceptor substrates. Libraries of variants were constructed and screened on sucrose allowing the
Autor:
Sophie Barbe, Alizée Vergès, Emmanuelle Cambon, Isabelle André, Magali Remaud-Simeon, Samuel Tranier, Claire Moulis
Publikováno v:
Carbohydrate Polymers
Carbohydrate Polymers, Elsevier, 2017, 173, pp.403-411. ⟨10.1016/j.carbpol.2017.06.011⟩
Carbohydrate Polymers, 2017, 173, pp.403-411. ⟨10.1016/j.carbpol.2017.06.011⟩
Carbohydrate Polymers, Elsevier, 2017, 173, pp.403-411. ⟨10.1016/j.carbpol.2017.06.011⟩
Carbohydrate Polymers, 2017, 173, pp.403-411. ⟨10.1016/j.carbpol.2017.06.011⟩
Amylosucrase from Neisseria polysaccharea naturally catalyzes the synthesis of α-1,4 glucans from sucrose. The product profile is quite polydisperse, ranging from soluble chains called maltooligosaccharides to high-molecular weight insoluble amylose
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07ad3fd3b75c845a5ce6069e40746db3
https://hal.archives-ouvertes.fr/hal-01602744
https://hal.archives-ouvertes.fr/hal-01602744
Autor:
Yann Le Guen, Isabelle André, Emmanuelle Cambon, Sophie Barbe, Magali Remaud-Simeon, Laurence A. Mulard, Stéphane Salamone, Claire Moulis, Alizée Vergès
Publikováno v:
ACS Catalysis
ACS Catalysis, 2015, 5 (2), pp.1186-1198. ⟨10.1021/cs501288r⟩
ACS Catalysis, American Chemical Society, 2015, 5 (2), pp.1186-1198. ⟨10.1021/cs501288r⟩
ACS Catalysis, 2015, 5 (2), pp.1186-1198. ⟨10.1021/cs501288r⟩
ACS Catalysis, American Chemical Society, 2015, 5 (2), pp.1186-1198. ⟨10.1021/cs501288r⟩
International audience; The exploration of chemo-enzymatic routes to complex carbohydrates has been hampered by the lack of appropriate enzymatic tools having the substrate specificity for new reactions. Here, we used a computer-aided design framewor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aeffb479c26cb836b193805bb80eaad5
https://hal-pasteur.archives-ouvertes.fr/pasteur-02043360
https://hal-pasteur.archives-ouvertes.fr/pasteur-02043360