References of "Clerisse, Fabienne"
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See detailMethod for the production of recombinant proteins by green microalgae
Versali, Marie-France ULg; Clerisse, Fabienne ULg; Dommes, Jacques ULg et al

Patent (2011)

The present invention relates to a method for the production of recombinant proteins by algal cells, which are fresh water unicellular green microalgae belonging to the order of Sphaeropleales. The ... [more ▼]

The present invention relates to a method for the production of recombinant proteins by algal cells, which are fresh water unicellular green microalgae belonging to the order of Sphaeropleales. The present invention further provides recombinant algal cells, wherein said algal cells are fresh water unicellular green microalgae belonging to the order of Sphaeropleales, and wherein said algal cells are capable of producing a recombinant protein. The invention is also directed to a method for selecting recombinant algal cells. The invention also relates to the use of recombinant algal cells as described herein for producing recombinant proteins. [less ▲]

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See detailCharacterization and Cloning of Chitin Deacetylases from Rhizopus Circinans
Gauthier, Carole ULg; Clerisse, Fabienne ULg; Dommes, Jacques ULg et al

in Protein Expression & Purification (2008), 59

Chitin deacetylase catalyzes hydrolysis of the acetamido groups of N-acetylglucosamine of chitin in fungal cell walls. Here a chitin deacetylase secreted by Rhizopus circinans was purified to homogeneity ... [more ▼]

Chitin deacetylase catalyzes hydrolysis of the acetamido groups of N-acetylglucosamine of chitin in fungal cell walls. Here a chitin deacetylase secreted by Rhizopus circinans was purified to homogeneity and partially characterized. The enzyme exhibits an apparent molecular weight of approximately 75kDa. At 37 degrees C it shows optimal activity at pH 5.5-6. Its pH stability and thermal stability are good. Mn(2+) and Mg(2+) slightly enhance the activity of the enzyme and Cu(2+) strongly inhibits it. An R. circinans cDNA library was constructed and screened with a homologous probe synthesized by RT-PCR or with synthetic primers derived from the N-terminal amino-acid sequence of the native purified chitin deacetylase. Three chitin deacetylase cDNAs (RC, D2, and I3/2) were isolated from the cDNA library and sequenced. These cDNAs exhibit features characteristic of chitin deacetylase sequences: the presence of a polysaccharide deacetylase domain, a metal-binding triad, the conserved catalytic residues, and high homology with various chitin deacetylase genes. The cDNAs were cloned in a Pichia pastoris expression system and produced as polyhistidine-tagged proteins. Only one recombinant enzyme (called RC) was active under the tested conditions. It was purified to homogeneity in a single step and further characterized. The protein showed an apparent molecular mass of approximately 75kDa and, like the native enzyme, showed optimal activity at pH 5.5-6 at 37 degrees C. It was strongly inhibited by Cu(2+). The isolation of several chitin deacetylase cDNAs from the same microorganism is discussed. [less ▲]

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