Cell-surface display technology and metabolic engineering of Saccharomyces cerevisiae for enhancing xylitol production from woody biomass

2019 ◽  
Vol 21 (7) ◽  
pp. 1795-1808 ◽  
Author(s):  
Gregory Guirimand ◽  
Kentaro Inokuma ◽  
Takahiro Bamba ◽  
Mami Matsuda ◽  
Kenta Morita ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Metabolic Engineering ◽  
Cell Surface ◽  
Surface Display ◽  
Woody Biomass ◽  
Cell Surface Display ◽  
Xylitol Production ◽  
Display Technology ◽  
Pharmaceutical Industries

Xylitol is a major commodity chemical widely used in both the food and pharmaceutical industries.

scholarly journals Cell Surface Expression of Bacterial Esterase A by Saccharomyces cerevisiae and Its Enhancement by Constitutive Activation of the Cellular Unfolded Protein Response

2006 ◽  
Vol 72 (11) ◽  
pp. 7140-7147 ◽  
Author(s):  
Frank Breinig ◽  
Björn Diehl ◽  
Sabrina Rau ◽  
Christian Zimmer ◽  
Helmut Schwab ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Cell Surface ◽  
Surface Display ◽  
Cell Surface Display ◽  
Constitutive Activation ◽  
Unfolded Protein ◽  
Yeast Cell Surface ◽  
Protein Response

ABSTRACT Yeast cell surface display is a powerful tool for expression and immobilization of biocatalytically active proteins on a unicellular eukaryote. Here bacterial carboxylesterase EstA from Burkholderia gladioli was covalently anchored into the cell wall of Saccharomyces cerevisiae by in-frame fusion to the endogenous yeast proteins Kre1p, Cwp2p, and Flo1p. When p-nitrophenyl acetate was used as a substrate, the esterase specific activities of yeast expressing the protein fusions were 103 mU mg−1 protein for Kre1/EstA/Cwp2p and 72 mU mg−1 protein for Kre1/EstA/Flo1p. In vivo cell wall targeting was confirmed by esterase solubilization after laminarinase treatment and immunofluorescence microscopy. EstA expression resulted in cell wall-associated esterase activities of 2.72 U mg−1 protein for Kre1/EstA/Cwp2p and 1.27 U mg−1 protein for Kre1/EstA/Flo1p. Furthermore, esterase display on the yeast cell surface enabled the cells to effectively grow on the esterase-dependent carbon source glycerol triacetate (Triacetin). In the case of Kre1/EstA/Flo1p, in vivo maturation within the yeast secretory pathway and final incorporation into the wall were further enhanced when there was constitutive activation of the unfolded protein response pathway. Our results demonstrate that esterase cell surface display in yeast, which, as shown here, is remarkably more effective than EstA surface display in Escherichia coli, can be further optimized by activating the protein folding machinery in the eukaryotic secretion pathway.

Cell Surface Display of MerR on Saccharomyces cerevisiae for Biosorption of Mercury

2017 ◽  
Vol 60 (1) ◽  
pp. 12-20 ◽  
Author(s):  
Qinguo Wei ◽  
Jiakuo Yan ◽  
Yao Chen ◽  
Lei Zhang ◽  
Xiaoyang Wu ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Surface ◽  
Surface Display ◽  
Cell Surface Display

scholarly journals Combined cell-surface display- and secretion-based strategies for production of cellulosic ethanol with Saccharomyces cerevisiae

2015 ◽  
Vol 8 (1) ◽  
Author(s):  
Zhuo Liu ◽  
Kentaro Inokuma ◽  
Shih-Hsin Ho ◽  
Riaan den Haan ◽  
Tomohisa Hasunuma ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Surface ◽  
Cellulosic Ethanol ◽  
Surface Display ◽  
Cell Surface Display

Cell Surface Display of Cellulase Activity–Free Xylanase Enzyme on Saccharomyces Cerevisiae EBY100

2010 ◽  
Vol 164 (3) ◽  
pp. 294-304 ◽  
Author(s):  
Shabina Yeasmin ◽  
Chul Hawn Kim ◽  
Hyeon Jin Park ◽  
Mominul Islam Sheikh ◽  
Ji Yong Lee ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Surface ◽  
Surface Display ◽  
Cellulase Activity ◽  
Cell Surface Display ◽  
Xylanase Enzyme
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