Construction of a novel cell-surface display system for heterologous gene expression in Escherichia coli by using an outer membrane protein of Zymomonas mobilis as anchor motif.
A novel bacterial cell-surface display system was developed in Escherichia coli using omp1, a hypothetical outer membrane protein of Zymomonas mobilis. By using this system, we successfully expressed beta-amylase gene of sweet potato in E. coli. The display of enzyme on the membrane surface was also confirmed. The recombinant beta-amylase showed to significantly increase hydrolytic activity toward soluble starch. Our results provide a basis for constructing an engineered Z. mobilis strain directly fermenting raw starch to produce ethanol.
He
Ming-Xiong
MX
Sichuan Key Laboratory of Molecular Biology & Biotechnology, Key Laboratory of Resource Biology & Eco-environment of Ministry of Education, College of Life Science, Sichuan University, Chengdu 610064, China.
Feng
Hong
H
Zhang
Yi-Zheng
YZ
D020816:Amino Acid Motifs; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D000431:Ethanol; D015870:Gene Expression; D027723:Ipomoea batatas / Q000201:enzymology / Q000235:genetics; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D013347:Subcellular Fractions; D017355:Zymomonas / Q000235:genetics*; D001614:beta-Amylase / Q000235:genetics* / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; D008565:Membrane Proteins; D011994:Recombinant Proteins; D000431:Ethanol; D001614:beta-Amylase