Alleviation of Proteolytic Sensitivity To Enhance Recombinant Lipase Production in Escherichia coli

Two amino acids, Leu149 and Val223, were identified as proteolytically sensitive when Pseudozyma antarctica lipase (PalB) was heterologously expressed in Escherichia coli. The functional expression was enhanced using the double mutant for cultivation. However, the recombinant protein production was...

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Veröffentlicht in:	Applied and Environmental Microbiology 2009-08, Vol.75 (16), p.5424-5427
Hauptverfasser:	Narayanan, Niju, Chou, C. Perry
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Amino acids Bacterial proteins Biological and medical sciences E coli Enzymology and Protein Engineering Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Fundamental and applied biological sciences. Psychology Gene expression Gene Expression Regulation, Bacterial Industrial Microbiology - methods Leucine - genetics Lipase - chemistry Lipase - genetics Lipase - metabolism Microbiology Mutation Peptide Hydrolases - metabolism Protein Disulfide-Isomerases - genetics Protein Disulfide-Isomerases - metabolism Protein Engineering - methods Protein Folding Recombinant Proteins - genetics Recombinant Proteins - metabolism Ustilaginales - enzymology Ustilaginales - genetics Valine - genetics
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Beschreibung
Zusammenfassung:	Two amino acids, Leu149 and Val223, were identified as proteolytically sensitive when Pseudozyma antarctica lipase (PalB) was heterologously expressed in Escherichia coli. The functional expression was enhanced using the double mutant for cultivation. However, the recombinant protein production was still limited by PalB misfolding, which was resolved by DsbA coexpression.
ISSN:	0099-2240 1098-5336 1098-6596
DOI:	10.1128/AEM.00740-09