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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Published in:Applied and Environmental Microbiology
Main Authors: Narayanan, Niju, Chou, C. Perry
Format: Text
Language:English
Published: American Society for Microbiology (ASM) 2009
Subjects:
Enzymology and Protein Engineering
Antarc*
Antarctica
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2725454
http://www.ncbi.nlm.nih.gov/pubmed/19542329
https://doi.org/10.1128/AEM.00740-09
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spelling ftpubmed:oai:pubmedcentral.nih.gov:2725454 2023-05-15T13:33:18+02:00 Alleviation of Proteolytic Sensitivity To Enhance Recombinant Lipase Production in Escherichia coli▿ Narayanan, Niju Chou, C. Perry 2009-08 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2725454 http://www.ncbi.nlm.nih.gov/pubmed/19542329 https://doi.org/10.1128/AEM.00740-09 en eng American Society for Microbiology (ASM) http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2725454 http://www.ncbi.nlm.nih.gov/pubmed/19542329 http://dx.doi.org/10.1128/AEM.00740-09 Copyright © 2009, American Society for Microbiology Enzymology and Protein Engineering Text 2009 ftpubmed https://doi.org/10.1128/AEM.00740-09 2013-09-02T15:39:31Z 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. Text Antarc* Antarctica PubMed Central (PMC) Applied and Environmental Microbiology 75 16 5424 5427
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Enzymology and Protein Engineering
spellingShingle Enzymology and Protein Engineering
Narayanan, Niju
Chou, C. Perry
Alleviation of Proteolytic Sensitivity To Enhance Recombinant Lipase Production in Escherichia coli▿
topic_facet Enzymology and Protein Engineering
description 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.
format Text
author Narayanan, Niju
Chou, C. Perry
author_facet Narayanan, Niju
Chou, C. Perry
author_sort Narayanan, Niju
title Alleviation of Proteolytic Sensitivity To Enhance Recombinant Lipase Production in Escherichia coli▿
title_short Alleviation of Proteolytic Sensitivity To Enhance Recombinant Lipase Production in Escherichia coli▿
title_full Alleviation of Proteolytic Sensitivity To Enhance Recombinant Lipase Production in Escherichia coli▿
title_fullStr Alleviation of Proteolytic Sensitivity To Enhance Recombinant Lipase Production in Escherichia coli▿
title_full_unstemmed Alleviation of Proteolytic Sensitivity To Enhance Recombinant Lipase Production in Escherichia coli▿
title_sort alleviation of proteolytic sensitivity to enhance recombinant lipase production in escherichia coli▿
publisher American Society for Microbiology (ASM)
publishDate 2009
url http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2725454
http://www.ncbi.nlm.nih.gov/pubmed/19542329
https://doi.org/10.1128/AEM.00740-09
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2725454
http://www.ncbi.nlm.nih.gov/pubmed/19542329
http://dx.doi.org/10.1128/AEM.00740-09
op_rights Copyright © 2009, American Society for Microbiology
op_doi https://doi.org/10.1128/AEM.00740-09
container_title Applied and Environmental Microbiology
container_volume 75
container_issue 16
container_start_page 5424
op_container_end_page 5427
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