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Antimicrobial action of the pepsin hydrolysate of lactoferrin (LfH) on Escherichia coli O157:H7

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TypeOfResource
Text
TitleInfo (ID = T-1)
Title
Antimicrobial action of the pepsin hydrolysate of lactoferrin (LfH) on Escherichia coli O157:H7
Identifier
ETD_1558
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.000051382
Language
LanguageTerm (authority = ISO639-2); (type = code)
eng
Genre (authority = marcgt)
theses
Subject (ID = SBJ-1); (authority = RUETD)
Topic
Food Science
Subject (ID = SBJ-1); (authority = ETD-LCSH)
Topic
Lactoferrin--Physiological effect
Subject (ID = SBJ-1); (authority = ETD-LCSH)
Topic
Anti-infective agents
Abstract
Foodborne illnesses are a significant problem and a major public health concern in the United States and throughout the world. The control of microbial pathogens in foods is a significant concern and numerous methods have been employed to control or prevent the growth of pathogenic microorganisms in food, including the use of synthetic and natural antimicrobial agents. There exist a plethora of literature on "natural" antimicrobial compounds (e.g. nisin, lactoferrin) and their possible use in food systems to eliminate or control the growth of pathogenic microorganisms. The actual antimicrobial mechanism of action for some antimicrobials has been extensively studied and well documented but for other potential natural biopreservatives, such as lactoferrin, the actual mechanism of action is not well defined. Lactoferrin is a 78 kilo Dalton cationic iron-binding antimicrobial glycoprotein produced in many mammalian secretions, including milk, tears, saliva, and serum. Previous research has focused on iron starvation and cell membrane damage. However, treatment with pepsin yields a peptide fragment, termed lactoferricin that lacks the iron binding sites and is still antimicrobial. It has also been hypothesized that the peptide, due to its small size, in comparison to the whole molecule, might be able to penetrate the outer membrane or that the smaller size of lactoferricin may facilitate its access to microbial cell surface components. The peptide and pepsin hydrolysate have been shown to depolarize the outer membrane of E. coli, however, this is likely not the mechanism of action. The data presented in this study demonstrate that the pepsin hydrolysate of lactoferrin (LfH) exerts its antimicrobial action on the inner membrane of E. coli O157:H7 by forming pores in the membrane. This membrane damage results in a loss of energy and ion balance (potassium ion (K+) efflux and decreases in intracellular ATP concentrations coupled with increases in extracellular ATP concentrations) leading to a collapse of membrane potential and a loss of cell viability.
PhysicalDescription
Form (authority = gmd)
electronic resource
Extent
xvi, 144 p. : ill.
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application/pdf
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text/xml
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Christopher A. Murdock
Name (ID = NAME-1); (type = personal)
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Murdock
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Christopher A.
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author
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Christopher A. Murdock
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NamePart (type = family)
Matthews
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Karl
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chair
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Advisory Committee
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Karl R Matthews
Name (ID = NAME-3); (type = personal)
NamePart (type = family)
Montville
NamePart (type = given)
Thomas
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internal member
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Advisory Committee
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Thomas J Montville
Name (ID = NAME-4); (type = personal)
NamePart (type = family)
Chikindas
NamePart (type = given)
Michael
Role
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internal member
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Advisory Committee
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Michael L Chikindas
Name (ID = NAME-5); (type = personal)
NamePart (type = family)
Katz
NamePart (type = given)
Stanley
Role
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outside member
Affiliation
Advisory Committee
DisplayForm
Stanley E Katz
Name (ID = NAME-1); (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB); (type = )
degree grantor
Name (ID = NAME-2); (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB); (type = )
school
OriginInfo
DateCreated (point = ); (qualifier = exact)
2009
DateOther (qualifier = exact); (type = degree)
2009-05
Place
PlaceTerm (type = code)
xx
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Location
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NjNbRU
Identifier (type = doi)
doi:10.7282/T3JM29TH
Genre (authority = ExL-Esploro)
ETD doctoral
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The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
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Type
Permission or license
Detail
Non-exclusive ETD license
AssociatedObject (AUTHORITY = rulib); (ID = 1)
Type
License
Name
Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
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ETD
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application/pdf
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application/x-tar
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2232320
Checksum (METHOD = SHA1)
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