Selection of a whole-cell biocatalyst for methyl parathion biodegradation.
Whole-cell biocatalyst has the potential to become a cost-effective alternative to conventional enzyme methods for solving ecological and energy issues. However, cytosolic-expressing biocatalyst systems are critically disadvantaged due to the low permeability of the cell membrane. To overcome substrate transport barrier, periplasmic secretion and surface display biocatalysts were developed by expressing signal peptides or anchor proteins in Escherichia coli. In this work, six carriers were compared in regard to whole-cell activity of methyl parathion hydrolase (MPH). Our results indicate that the surface display systems yielded one to three times whole-cell activity than the periplasmic secretion systems. Although periplasmic secretion systems showed generally more stable than surface display systems, surface display appeared more suitable for whole-cell biocatalyst. It should note that the applicability of the DsbA/PhoA/AIDA-I leader to MPH expression is shown here for the first time. In addition, the result provided a useful reference for other whole-cell biocatalyst selection.
Taishan University, Shandong 271021, China.
Jijian
J
Yang
Ruihua
R
Liu
Hong
H
Jiang
Yao
Y
Yang
Chuanling
C
Qiao
D055162:Biocatalysis; D001673:Biodegradation, Environmental; D002462:Cell Membrane / Q000201:enzymology / Q000235:genetics; D052918:Environmental Restoration and Remediation / Q000379:methods*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism; D008743:Methyl Parathion / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics / Q000378:metabolism; D015202:Protein Engineering; D021382:Protein Sorting Signals; D021381:Protein Transport
D029968:Escherichia coli Proteins; D021382:Protein Sorting Signals; D008743:Methyl Parathion; D010744:Phosphoric Monoester Hydrolases