Construction of a highly active xylanase displaying oleaginous yeast: Comparison of anchoring systems

25Citations
Citations of this article
45Readers
Mendeley users who have this article in their library.

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.©2014 Duquesne et al.

Cite

CITATION STYLE

APA

Duquesne, S., Bozonnet, S., Bordes, F., Dumon, C., Nicaud, J. M., & Marty, A. (2014). Construction of a highly active xylanase displaying oleaginous yeast: Comparison of anchoring systems. PLoS ONE, 9(4). https://doi.org/10.1371/journal.pone.0095128

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free