Teaching an old pET new tricks: tuning of inclusion body formation and properties by a mixed feed system in E. coli

Against the outdated belief that inclusion bodies (IBs) in Escherichia coli are only inactive aggregates of misfolded protein, and thus should be avoided during recombinant protein production, numerous biopharmaceutically important proteins are currently produced as IBs. To obtain correctly folded,...

Full description

Saved in:
Bibliographic Details
Published in:Applied Microbiology and Biotechnology 2018, Vol.102 (2), p.667
Main Authors: Wurm, David J, Quehenberger, Julian, Mildner, Julia, Eggenreich, Britta, Slouka, Christoph, Schwaighofer, Andreas, Wieland, Karin
Format: Report
Language:English
Subjects:
Escherichia coli
Physiological aspects
Recombinant proteins
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page
container_issue 2
container_start_page 667
container_title Applied Microbiology and Biotechnology
container_volume 102
creator Wurm, David J
Quehenberger, Julian
Mildner, Julia
Eggenreich, Britta
Slouka, Christoph
Schwaighofer, Andreas
Wieland, Karin
description Against the outdated belief that inclusion bodies (IBs) in Escherichia coli are only inactive aggregates of misfolded protein, and thus should be avoided during recombinant protein production, numerous biopharmaceutically important proteins are currently produced as IBs. To obtain correctly folded, soluble product, IBs have to be processed, namely, harvested, solubilized, and refolded. Several years ago, it was discovered that, depending on cultivation conditions and protein properties, IBs contain partially correctly folded protein structures, which makes IB processing more efficient. Here, we present a method of tailored induction of recombinant protein production in E. coli by a mixed feed system using glucose and lactose and its impact on IB formation. Our method allows tuning of IB amount, IB size, size distribution, and purity, which does not only facilitate IB processing, but is also crucial for potential direct applications of IBs as nanomaterials and biomaterials in regenerative medicine.
doi_str_mv 10.1007/s00253-017-8641-6
format report
fullrecord <record><control><sourceid>gale</sourceid><recordid>TN_cdi_gale_infotracacademiconefile_A521789523</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A521789523</galeid><sourcerecordid>A521789523</sourcerecordid><originalsourceid>FETCH-gale_infotracacademiconefile_A5217895233</originalsourceid><addsrcrecordid>eNqVi11OwzAQhP0AUsvPAXjbCzjYCU5S3hAK4gB5R66zbhcSu_K6gtweV-ICaKQZzYw-IR60qrRS3SMrVZtGKt3Jvn3Ssr0S21KM7Myu34gb5k-ldN237VbwiNYdKRzABojzBKdhhIDfkBO5L36GfA6XN3qg4OYzUwywj9MKPqbF5ku1oWApnjBlQob9ChYW-sEJPBbjlTMuBYehAhdnuhPX3s6M9395K6q3YXx9lwc74wcFH3OyrmjChVwM6KnsL6bWXb8zddP8G_gFNC1XxQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>report</recordtype></control><display><type>report</type><title>Teaching an old pET new tricks: tuning of inclusion body formation and properties by a mixed feed system in E. coli</title><source>ABI/INFORM global</source><source>Springer Nature</source><creator>Wurm, David J ; Quehenberger, Julian ; Mildner, Julia ; Eggenreich, Britta ; Slouka, Christoph ; Schwaighofer, Andreas ; Wieland, Karin</creator><creatorcontrib>Wurm, David J ; Quehenberger, Julian ; Mildner, Julia ; Eggenreich, Britta ; Slouka, Christoph ; Schwaighofer, Andreas ; Wieland, Karin</creatorcontrib><description>Against the outdated belief that inclusion bodies (IBs) in Escherichia coli are only inactive aggregates of misfolded protein, and thus should be avoided during recombinant protein production, numerous biopharmaceutically important proteins are currently produced as IBs. To obtain correctly folded, soluble product, IBs have to be processed, namely, harvested, solubilized, and refolded. Several years ago, it was discovered that, depending on cultivation conditions and protein properties, IBs contain partially correctly folded protein structures, which makes IB processing more efficient. Here, we present a method of tailored induction of recombinant protein production in E. coli by a mixed feed system using glucose and lactose and its impact on IB formation. Our method allows tuning of IB amount, IB size, size distribution, and purity, which does not only facilitate IB processing, but is also crucial for potential direct applications of IBs as nanomaterials and biomaterials in regenerative medicine.</description><identifier>ISSN: 0175-7598</identifier><identifier>DOI: 10.1007/s00253-017-8641-6</identifier><language>eng</language><publisher>Springer</publisher><subject>Escherichia coli ; Physiological aspects ; Recombinant proteins</subject><ispartof>Applied Microbiology and Biotechnology, 2018, Vol.102 (2), p.667</ispartof><rights>COPYRIGHT 2018 Springer</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>776,780,4476,27902</link.rule.ids></links><search><creatorcontrib>Wurm, David J</creatorcontrib><creatorcontrib>Quehenberger, Julian</creatorcontrib><creatorcontrib>Mildner, Julia</creatorcontrib><creatorcontrib>Eggenreich, Britta</creatorcontrib><creatorcontrib>Slouka, Christoph</creatorcontrib><creatorcontrib>Schwaighofer, Andreas</creatorcontrib><creatorcontrib>Wieland, Karin</creatorcontrib><title>Teaching an old pET new tricks: tuning of inclusion body formation and properties by a mixed feed system in E. coli</title><title>Applied Microbiology and Biotechnology</title><description>Against the outdated belief that inclusion bodies (IBs) in Escherichia coli are only inactive aggregates of misfolded protein, and thus should be avoided during recombinant protein production, numerous biopharmaceutically important proteins are currently produced as IBs. To obtain correctly folded, soluble product, IBs have to be processed, namely, harvested, solubilized, and refolded. Several years ago, it was discovered that, depending on cultivation conditions and protein properties, IBs contain partially correctly folded protein structures, which makes IB processing more efficient. Here, we present a method of tailored induction of recombinant protein production in E. coli by a mixed feed system using glucose and lactose and its impact on IB formation. Our method allows tuning of IB amount, IB size, size distribution, and purity, which does not only facilitate IB processing, but is also crucial for potential direct applications of IBs as nanomaterials and biomaterials in regenerative medicine.</description><subject>Escherichia coli</subject><subject>Physiological aspects</subject><subject>Recombinant proteins</subject><issn>0175-7598</issn><fulltext>true</fulltext><rsrctype>report</rsrctype><creationdate>2018</creationdate><recordtype>report</recordtype><sourceid/><recordid>eNqVi11OwzAQhP0AUsvPAXjbCzjYCU5S3hAK4gB5R66zbhcSu_K6gtweV-ICaKQZzYw-IR60qrRS3SMrVZtGKt3Jvn3Ssr0S21KM7Myu34gb5k-ldN237VbwiNYdKRzABojzBKdhhIDfkBO5L36GfA6XN3qg4OYzUwywj9MKPqbF5ku1oWApnjBlQob9ChYW-sEJPBbjlTMuBYehAhdnuhPX3s6M9395K6q3YXx9lwc74wcFH3OyrmjChVwM6KnsL6bWXb8zddP8G_gFNC1XxQ</recordid><startdate>20180101</startdate><enddate>20180101</enddate><creator>Wurm, David J</creator><creator>Quehenberger, Julian</creator><creator>Mildner, Julia</creator><creator>Eggenreich, Britta</creator><creator>Slouka, Christoph</creator><creator>Schwaighofer, Andreas</creator><creator>Wieland, Karin</creator><general>Springer</general><scope/></search><sort><creationdate>20180101</creationdate><title>Teaching an old pET new tricks: tuning of inclusion body formation and properties by a mixed feed system in E. coli</title><author>Wurm, David J ; Quehenberger, Julian ; Mildner, Julia ; Eggenreich, Britta ; Slouka, Christoph ; Schwaighofer, Andreas ; Wieland, Karin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-gale_infotracacademiconefile_A5217895233</frbrgroupid><rsrctype>reports</rsrctype><prefilter>reports</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Escherichia coli</topic><topic>Physiological aspects</topic><topic>Recombinant proteins</topic><toplevel>online_resources</toplevel><creatorcontrib>Wurm, David J</creatorcontrib><creatorcontrib>Quehenberger, Julian</creatorcontrib><creatorcontrib>Mildner, Julia</creatorcontrib><creatorcontrib>Eggenreich, Britta</creatorcontrib><creatorcontrib>Slouka, Christoph</creatorcontrib><creatorcontrib>Schwaighofer, Andreas</creatorcontrib><creatorcontrib>Wieland, Karin</creatorcontrib></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wurm, David J</au><au>Quehenberger, Julian</au><au>Mildner, Julia</au><au>Eggenreich, Britta</au><au>Slouka, Christoph</au><au>Schwaighofer, Andreas</au><au>Wieland, Karin</au><format>book</format><genre>unknown</genre><ristype>RPRT</ristype><atitle>Teaching an old pET new tricks: tuning of inclusion body formation and properties by a mixed feed system in E. coli</atitle><jtitle>Applied Microbiology and Biotechnology</jtitle><date>2018-01-01</date><risdate>2018</risdate><volume>102</volume><issue>2</issue><spage>667</spage><pages>667-</pages><issn>0175-7598</issn><abstract>Against the outdated belief that inclusion bodies (IBs) in Escherichia coli are only inactive aggregates of misfolded protein, and thus should be avoided during recombinant protein production, numerous biopharmaceutically important proteins are currently produced as IBs. To obtain correctly folded, soluble product, IBs have to be processed, namely, harvested, solubilized, and refolded. Several years ago, it was discovered that, depending on cultivation conditions and protein properties, IBs contain partially correctly folded protein structures, which makes IB processing more efficient. Here, we present a method of tailored induction of recombinant protein production in E. coli by a mixed feed system using glucose and lactose and its impact on IB formation. Our method allows tuning of IB amount, IB size, size distribution, and purity, which does not only facilitate IB processing, but is also crucial for potential direct applications of IBs as nanomaterials and biomaterials in regenerative medicine.</abstract><pub>Springer</pub><doi>10.1007/s00253-017-8641-6</doi></addata></record>
fulltext fulltext
identifier ISSN: 0175-7598
ispartof Applied Microbiology and Biotechnology, 2018, Vol.102 (2), p.667
issn 0175-7598
language eng
recordid cdi_gale_infotracacademiconefile_A521789523
source ABI/INFORM global; Springer Nature
subjects Escherichia coli
Physiological aspects
Recombinant proteins
title Teaching an old pET new tricks: tuning of inclusion body formation and properties by a mixed feed system in E. coli
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-23T10%3A56%3A04IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale&rft_val_fmt=info:ofi/fmt:kev:mtx:book&rft.genre=unknown&rft.atitle=Teaching%20an%20old%20pET%20new%20tricks:%20tuning%20of%20inclusion%20body%20formation%20and%20properties%20by%20a%20mixed%20feed%20system%20in%20E.%20coli&rft.jtitle=Applied%20Microbiology%20and%20Biotechnology&rft.au=Wurm,%20David%20J&rft.date=2018-01-01&rft.volume=102&rft.issue=2&rft.spage=667&rft.pages=667-&rft.issn=0175-7598&rft_id=info:doi/10.1007/s00253-017-8641-6&rft_dat=%3Cgale%3EA521789523%3C/gale%3E%3Cgrp_id%3Ecdi_FETCH-gale_infotracacademiconefile_A5217895233%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rft_galeid=A521789523&rfr_iscdi=true