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Public Library of Science, PLoS ONE, 4(9), p. e95128, 2014

DOI: 10.1371/journal.pone.0095128

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Construction of a Highly Active Xylanase Displaying Oleaginous Yeast: Comparison of Anchoring Systems

Journal article published in 2014 by Sophie Duquesne, Sophie Bozonnet, Florence Bordes, Claire Dumon, Jean-Marc Nicaud ORCID, Alain Marty
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.