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Characterization and application of carrot antifreeze protein in keeping bacterial cell viability under low temperature

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TitleInfo
Title
Characterization and application of carrot antifreeze protein in keeping bacterial cell viability under low temperature
Name (type = personal)
NamePart (type = family)
Wang
NamePart (type = given)
Ying
NamePart (type = date)
1980-
DisplayForm
Ying Wang
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
HUANG
NamePart (type = given)
QINGRONG
DisplayForm
QINGRONG HUANG
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Di
NamePart (type = given)
Rong
DisplayForm
Rong Di
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
co-chair
Name (type = personal)
NamePart (type = family)
HO
NamePart (type = given)
CHI-TANG
DisplayForm
CHI-TANG HO
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2015
DateOther (qualifier = exact); (type = degree)
2015-05
CopyrightDate (encoding = w3cdtf); (qualifier = exact)
2015
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract (type = abstract)
The ice-structuring protein (ISP) or antifreeze protein (AFP) has great potential applications in frozen food preservation. This study aims at developing a fast and economical method to prepare carrot (Daucus carota) AFP (DcAFP) and apply it in the preservation of bacterial cell. The carrot AFP (DcAFP) was cloned and transformed into the recombinant bacteria. The recombinant protein was purified and refolded, and its second structure, as determined by circular-dichroism (CD), was found to contain approximately 60% beta sheet structure, suggesting the potential binding plane for ice and liquid water. The inhibition of ice crystal formation by DcAFP was further demonstrated by the following three experiments: first, the recrystallization of ice crystals with the DcAFP solution was monitored by using video microscopy. By quantifying the crystal number and their average diameter, the ability of DcAFP to inhibit the recrystallization has been demonstrated. Second, bacterial cell viability under 0ºC was detected. With the addition of DcAFP, cell survival rate was 50% higher than that of the control sample. Finally, the addition of DcAFP in the lactobacillus without any other protective agent significantly increased cell viability under 0ºC. These results suggested the potential applications of DcAFP in the preservation of probiotic foods.
Subject (authority = RUETD)
Topic
Food Science
Subject (authority = ETD-LCSH)
Topic
Antifreeze proteins
Subject (authority = ETD-LCSH)
Topic
Plants--Effect of cold on
Subject (authority = ETD-LCSH)
Topic
Carrots
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
Identifier
ETD_6444
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
1 online resource (ix, 51 p. : ill.)
Note (type = degree)
M.S.
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Ying Wang
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier (type = doi)
doi:10.7282/T3ZW1NRV
Genre (authority = ExL-Esploro)
ETD graduate
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Rights

RightsDeclaration (ID = rulibRdec0006)
The author owns the copyright to this work.
RightsHolder (type = personal)
Name
FamilyName
Wang
GivenName
Ying
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2015-04-20 22:36:33
AssociatedEntity
Name
ying wang
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - New Brunswick
AssociatedObject
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.
RightsEvent
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2015-05-31
DateTime (encoding = w3cdtf); (qualifier = exact); (point = end)
2015-11-30
Type
Embargo
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after November 30th, 2015.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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Technical

RULTechMD (ID = TECHNICAL1)
ContentModel
ETD
OperatingSystem (VERSION = 5.1)
windows xp
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