| Literature DB >> 31486973 |
Lu Bian1, Zhen Zhang1, Rong-Xing Tang1, Wei Shen1, Li-Xin Ma2.
Abstract
Methyl parathion hydrolase (MPH) plays an important role in degrading a range of organophosphorus compounds. In order to display MPH on the cell surface of Escherichia coli strain RosettaBlue™, the Flavin-based fluorescent protein EcFbFP was severed as an auto-anchoring matrix. With net negative charges of EcFbFP supplying the driving forces, fusion protein MPH-EcFbFP through a two-step auto-surface display process was finally verified by (a) inner membrane translocation and (b) anchoring at outer membrane. Cells with surface-displayed MPH obtained activity of 0.12 U/OD600 against substrate methyl parathion. MPH when fused with engineered EcFbFP containing 20 net negative charges exhibited fivefold higher anchoring efficiency and tenfold higher enzymatic catalytic activity of 1.10 U/OD600. The above result showed that MPH was successfully displayed on cell surface and can be used for biodegradation of methyl parathion.Entities:
Keywords: Cell-surface display; EcFbFP; Flavin-based fluorescent protein; Methyl parathion hydrolase; Net negative charge
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Year: 2019 PMID: 31486973 DOI: 10.1007/s12033-019-00204-3
Source DB: PubMed Journal: Mol Biotechnol ISSN: 1073-6085 Impact factor: 2.695