title: Construction of a highly active xylanase displaying oleaginous yeast: comparison of anchoring systems.
abstract: Three Yarrowia lipolytica cell wall proteins (YlPir, YlCWP1 and YlCBM) were evaluated for their ability to display the xylanase TxXYN from Thermobacillus xylanilyticus on the cell surface of Y. lipolytica. The fusion proteins were produced in Y. lipolytica JMY1212, a strain engineered for mono-copy chromosomal insertion, and enabling accurate comparison of anchoring systems. The construction using YlPir enabled cell bound xylanase activity to be maximised (71.6 U/g). Although 48% of the activity was released in the supernatant, probably due to proteolysis at the fusion zone, this system is three times more efficient for the anchoring of TxXYN than the YlCWP1 system formerly developed for Y. lipolytica. As far as we know it represents the best displayed xylanase activity ever published. It could be an attractive alternative anchoring system to display enzymes in Y. lipolytica.
authors.affiliation: Université de Toulouse; INSA, UPS, INP; LISBP, Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, Toulouse, France; CNRS, UMR5504, Toulouse, France.
authors.forename: Sophie
authors.initials: S
authors.lastname: Duquesne
authors.affiliation: Université de Toulouse; INSA, UPS, INP; LISBP, Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, Toulouse, France; CNRS, UMR5504, Toulouse, France.
authors.forename: Sophie
authors.initials: S
authors.lastname: Bozonnet
authors.affiliation: Université de Toulouse; INSA, UPS, INP; LISBP, Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, Toulouse, France; CNRS, UMR5504, Toulouse, France.
authors.forename: Florence
authors.initials: F
authors.lastname: Bordes
authors.affiliation: Université de Toulouse; INSA, UPS, INP; LISBP, Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, Toulouse, France; CNRS, UMR5504, Toulouse, France.
authors.forename: Claire
authors.initials: C
authors.lastname: Dumon
authors.affiliation: INRA, UMR1319 Micalis, Domaine de Vilvert, Jouy-en-Josas, France; AgroParisTech, UMR Micalis, Jouy-en-Josas, France.
authors.forename: Jean-Marc
authors.initials: JM
authors.lastname: Nicaud
authors.affiliation: Université de Toulouse; INSA, UPS, INP; LISBP, Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, Toulouse, France; CNRS, UMR5504, Toulouse, France.
authors.forename: Alain
authors.initials: A
authors.lastname: Marty
mesh_terms: D056449:Bacillales / Q000201:enzymology / Q000235:genetics; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000235:genetics; D002473:Cell Wall / Q000235:genetics / Q000378:metabolism; D043364:Endo-1,4-beta Xylanases / Q000096:biosynthesis / Q000235:genetics; D005656:Fungal Proteins / Q000096:biosynthesis; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics; D025062:Yarrowia / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D005656:Fungal Proteins; D011993:Recombinant Fusion Proteins; D043364:Endo-1,4-beta Xylanases
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