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Massachusetts Institute of Technology

Global transcriptional analysis of an Escherichia coli recombinant protein process during hypoxia and hyperoxia

Abstract

dc:description.abstract

(cont.) The effects of recombinant protein production were observed through expression analysis of induced, uninduced, and Empty-Vector cultures. As expected, recombinant α₁AT production led to increased expression of heat-shock genes, including proteases and chaperones that are known to be involved in α₁AT degradation. Based on expression analysis data, production of recombinant α₁AT also resulted in catabolite repression and decreased amino acid biosynthesis. This work demonstrates the utility of DNA microarrays in analyzing and improving microbial fermentations. Global expression studies have suggested several strategies for increasing the resistance of bioprocesses to the damaging effects of oxygen and recombinant protein production.

Degree

thesis:*
Department dc:contributor.department
Massachusetts Institute of Technology. Dept. of Chemical Engineering.
Grantor dc:publisher
Massachusetts Institute of Technology
Year dc:date.issued
2004

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Perry, William B
Advisor dc:contributor.advisor
  • Charles L. Cooney.

Subjects

dc:subject × 1

Rights

dc:rights
Statement dc:rights
  • M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission.
Language dc:language.iso
en_US

Identifiers

dc:identifier.*
Handle dc:identifier.uri
http://hdl.handle.net/1721.1/28666
OAI identifier oai:identifier
oai:dspace.mit.edu:1721.1/28666

Chain of custody

source
Harvested from
MIT
Base URL
dspace.mit.edu/oai/request
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
citation

Perry, William B. Global transcriptional analysis of an Escherichia coli recombinant protein process during hypoxia and hyperoxia. Massachusetts Institute of Technology, 2004. http://hdl.handle.net/1721.1/28666