Dynamic rheological properties of native and cross-linked gliadin proteins

A comparison of cross-linked and native gliadin suspensions, with respect to the state of protein globular structure was carried out using small-angle X-ray scattering (SAXS), dynamic light scattering (DLS) and rheological analysis. Gliadin suspensions were also analyzed in the presence and absence...

Full description

Saved in:
Bibliographic Details
Published inInternational journal of biological macromolecules Vol. 51; no. 4; pp. 640 - 646
Main Authors Soares, Rosane M.D., Lionzo, Maria I., Da Silveira, Nadya P., Rayas-Duarte, Patricia, Soldi, Valdir
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.11.2012
Subjects
Online AccessGet full text

Cover

Loading…
Abstract A comparison of cross-linked and native gliadin suspensions, with respect to the state of protein globular structure was carried out using small-angle X-ray scattering (SAXS), dynamic light scattering (DLS) and rheological analysis. Gliadin suspensions were also analyzed in the presence and absence of glycerol. DLS analysis showed that Rh increased only with gliadin/EDC/NHS suspensions. However, Kratky plots revealed that gliadin and gliadin/l-cysteine maintained their globular shape even in absence or presence of glycerol. Rheological experiments revealed that gliadin and gliadin/l-cysteine suspension exhibited a similar profile with three main domains, and a sol–gel transition. Gliadin/EDC/NHS did not present any sol–gel transition, and this fact corroborates with DLS results and the hypothesis of lower protein–protein interaction, which are in agreement with G″>G′.
AbstractList A comparison of cross-linked and native gliadin suspensions, with respect to the state of protein globular structure was carried out using small-angle X-ray scattering (SAXS), dynamic light scattering (DLS) and rheological analysis. Gliadin suspensions were also analyzed in the presence and absence of glycerol. DLS analysis showed that R(h) increased only with gliadin/EDC/NHS suspensions. However, Kratky plots revealed that gliadin and gliadin/L-cysteine maintained their globular shape even in absence or presence of glycerol. Rheological experiments revealed that gliadin and gliadin/L-cysteine suspension exhibited a similar profile with three main domains, and a sol-gel transition. Gliadin/EDC/NHS did not present any sol-gel transition, and this fact corroborates with DLS results and the hypothesis of lower protein-protein interaction, which are in agreement with G″ > G'.
A comparison of cross-linked and native gliadin suspensions, with respect to the state of protein globular structure was carried out using small-angle X-ray scattering (SAXS), dynamic light scattering (DLS) and rheological analysis. Gliadin suspensions were also analyzed in the presence and absence of glycerol. DLS analysis showed that Rₕ increased only with gliadin/EDC/NHS suspensions. However, Kratky plots revealed that gliadin and gliadin/l-cysteine maintained their globular shape even in absence or presence of glycerol. Rheological experiments revealed that gliadin and gliadin/l-cysteine suspension exhibited a similar profile with three main domains, and a sol–gel transition. Gliadin/EDC/NHS did not present any sol–gel transition, and this fact corroborates with DLS results and the hypothesis of lower protein–protein interaction, which are in agreement with G″>G′.
A comparison of cross-linked and native gliadin suspensions, with respect to the state of protein globular structure was carried out using small-angle X-ray scattering (SAXS), dynamic light scattering (DLS) and rheological analysis. Gliadin suspensions were also analyzed in the presence and absence of glycerol. DLS analysis showed that Rh increased only with gliadin/EDC/NHS suspensions. However, Kratky plots revealed that gliadin and gliadin/l-cysteine maintained their globular shape even in absence or presence of glycerol. Rheological experiments revealed that gliadin and gliadin/l-cysteine suspension exhibited a similar profile with three main domains, and a sol–gel transition. Gliadin/EDC/NHS did not present any sol–gel transition, and this fact corroborates with DLS results and the hypothesis of lower protein–protein interaction, which are in agreement with G″>G′.
A comparison of cross-linked and native gliadin suspensions, with respect to the state of protein globular structure was carried out using small-angle X-ray scattering (SAXS), dynamic light scattering (DLS) and rheological analysis. Gliadin suspensions were also analyzed in the presence and absence of glycerol. DLS analysis showed that R(h) increased only with gliadin/EDC/NHS suspensions. However, Kratky plots revealed that gliadin and gliadin/L-cysteine maintained their globular shape even in absence or presence of glycerol. Rheological experiments revealed that gliadin and gliadin/L-cysteine suspension exhibited a similar profile with three main domains, and a sol-gel transition. Gliadin/EDC/NHS did not present any sol-gel transition, and this fact corroborates with DLS results and the hypothesis of lower protein-protein interaction, which are in agreement with G″ > G'.
Author Soldi, Valdir
Soares, Rosane M.D.
Rayas-Duarte, Patricia
Lionzo, Maria I.
Da Silveira, Nadya P.
Author_xml – sequence: 1
  givenname: Rosane M.D.
  surname: Soares
  fullname: Soares, Rosane M.D.
  email: soaresr@iq.ufrgs.br
  organization: Institute of Chemistry, Universidade Federal do Rio Grande do Sul, 91501-970, Porto Alegre, Brazil
– sequence: 2
  givenname: Maria I.
  surname: Lionzo
  fullname: Lionzo, Maria I.
  organization: Institute of Chemistry, Universidade Federal do Rio Grande do Sul, 91501-970, Porto Alegre, Brazil
– sequence: 3
  givenname: Nadya P.
  surname: Da Silveira
  fullname: Da Silveira, Nadya P.
  organization: Institute of Chemistry, Universidade Federal do Rio Grande do Sul, 91501-970, Porto Alegre, Brazil
– sequence: 4
  givenname: Patricia
  surname: Rayas-Duarte
  fullname: Rayas-Duarte, Patricia
  organization: Food and Agricultural Products Research Center, Oklahoma State University (OSU), Stillwater, OK 74078-3035, United States
– sequence: 5
  givenname: Valdir
  surname: Soldi
  fullname: Soldi, Valdir
  organization: Department of Chemistry, Universidade Federal de Santa Catarina, 88040-900, Florianópolis, Brazil
BackLink https://www.ncbi.nlm.nih.gov/pubmed/22771580$$D View this record in MEDLINE/PubMed
BookMark eNqFkE1v1DAQhi1URLeFv1By5JLgcRJ_3EAtn6rEAXq2HGeyzJLYi52t1H-Pl225chpp9Lwzr54LdhZiQMaugDfAQb7dNbQbKC7ON4KDaLhseAfP2Aa0MjXnvD1jGw4d1Bpafs4uct6VrexBv2DnQigFveYb9vXmIbiFfJV-Ypzjlrybq32Ke0wrYa7iVAW30j1WLoyVTzHneqbwC8dqO5MbKRzpFSnkl-z55OaMrx7nJbv7-OHH9ef69tunL9fvb2vfGrHWg--E8p6jnjoJUqpe4QBGiFJu8rrrBSinlRoMNx57YwYDWoDrOEzgcGgv2ZvT3fL49wHzahfKHufZBYyHbIG3Suu-WCqoPKF_iyec7D7R4tJDgezRo93ZJ4_26NFyaYvHErx6_HEYFhz_xZ7EFeD1CZhctG6bKNu77-WCLJJ7bboj8e5EYHFxT5hs9oTB40gJ_WrHSP9r8QdVWpGr
CitedBy_id crossref_primary_10_1016_j_ijbiomac_2013_02_001
Cites_doi 10.1016/j.jsb.2009.08.009
10.1021/bi8000616
10.1021/bc00031a015
10.1006/jmbi.1997.1456
10.1016/j.foodhyd.2007.06.006
10.1007/s00249-003-0354-3
10.1006/jmbi.1995.0418
10.1016/j.ijbiomac.2011.05.025
10.1016/S0021-9258(19)74308-7
10.1088/0034-4885/66/10/R05
10.1016/0144-8617(94)00107-5
10.1021/jf049061x
10.1007/s00122-001-0552-2
10.1016/j.foodhyd.2003.11.002
10.1021/ma7023792
10.1016/j.msec.2010.02.026
10.1016/S0167-4838(99)00019-9
10.1002/bip.21188
10.1021/bi800900d
10.1016/S0167-4838(96)00212-9
10.1021/jf0491613
10.1016/j.jfoodeng.2008.06.024
10.1006/jcrs.2001.0430
10.1046/j.1365-2621.2002.00623.x
10.1016/j.foodhyd.2006.03.006
10.1016/j.foodhyd.2007.12.009
10.1016/j.foodchem.2006.02.057
10.1021/bm7011136
10.1016/S0032-3861(00)00168-3
10.1002/bip.21352
10.1016/j.foodhyd.2009.08.010
10.1002/bip.21109
ContentType Journal Article
Copyright 2012 Elsevier B.V.
Copyright © 2012 Elsevier B.V. All rights reserved.
Copyright_xml – notice: 2012 Elsevier B.V.
– notice: Copyright © 2012 Elsevier B.V. All rights reserved.
DBID FBQ
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7X8
DOI 10.1016/j.ijbiomac.2012.06.041
DatabaseName AGRIS
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
MEDLINE - Academic
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
MEDLINE - Academic
DatabaseTitleList MEDLINE - Academic


MEDLINE
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
– sequence: 3
  dbid: FBQ
  name: AGRIS
  url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN
  sourceTypes: Publisher
DeliveryMethod fulltext_linktorsrc
Discipline Chemistry
EISSN 1879-0003
EndPage 646
ExternalDocumentID 10_1016_j_ijbiomac_2012_06_041
22771580
US201600058940
S0141813012002735
Genre Research Support, Non-U.S. Gov't
Journal Article
GroupedDBID ---
--K
--M
.~1
0R~
1B1
1RT
1~.
1~5
29J
4.4
457
4G.
53G
5GY
5VS
7-5
71M
8P~
9JM
AACTN
AAEDT
AAEDW
AAIAV
AAIKJ
AAKOC
AALRI
AAOAW
AAQFI
AAQXK
AAXUO
ABFNM
ABFRF
ABGSF
ABJNI
ABMAC
ABUDA
ABXDB
ABYKQ
ACDAQ
ACGFO
ACGFS
ACIUM
ACRLP
ADBBV
ADEZE
ADMUD
ADUVX
AEBSH
AEFWE
AEHWI
AEKER
AENEX
AFKWA
AFTJW
AFXIZ
AGHFR
AGRDE
AGUBO
AGYEJ
AHHHB
AIEXJ
AIKHN
AITUG
AJBFU
AJOXV
ALMA_UNASSIGNED_HOLDINGS
AMFUW
AMRAJ
ASPBG
AVWKF
AXJTR
AZFZN
BKOJK
BLXMC
CS3
DOVZS
DU5
EBS
EFJIC
EFLBG
EJD
EO8
EO9
EP2
EP3
F5P
FDB
FEDTE
FGOYB
FIRID
FNPLU
FYGXN
G-2
G-Q
GBLVA
HLW
HVGLF
HZ~
IHE
J1W
KOM
LX3
M41
MO0
N9A
O-L
O9-
OAUVE
OZT
P-8
P-9
P2P
PC.
Q38
R2-
RIG
ROL
RPZ
SBG
SCC
SDF
SDG
SDP
SES
SEW
SPCBC
SSU
SSZ
T5K
UHS
UNMZH
WUQ
~02
~G-
ABPIF
ABPTK
FBQ
AAHBH
AAXKI
AFJKZ
AKRWK
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7X8
ID FETCH-LOGICAL-c392t-bc427cc0e8f46166757eb1922065fc845217a877b909ce599b91821a401f1aeb3
IEDL.DBID .~1
ISSN 0141-8130
IngestDate Fri Oct 25 09:30:12 EDT 2024
Thu Sep 26 16:23:55 EDT 2024
Sat Sep 28 07:54:49 EDT 2024
Wed Dec 27 19:16:22 EST 2023
Fri Feb 23 02:33:37 EST 2024
IsPeerReviewed true
IsScholarly true
Issue 4
Keywords Oscillatory rheology
Gliadin
Globular protein
Language English
License Copyright © 2012 Elsevier B.V. All rights reserved.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c392t-bc427cc0e8f46166757eb1922065fc845217a877b909ce599b91821a401f1aeb3
Notes http://dx.doi.org/10.1016/j.ijbiomac.2012.06.041
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
PMID 22771580
PQID 1037885016
PQPubID 23479
PageCount 7
ParticipantIDs proquest_miscellaneous_1037885016
crossref_primary_10_1016_j_ijbiomac_2012_06_041
pubmed_primary_22771580
fao_agris_US201600058940
elsevier_sciencedirect_doi_10_1016_j_ijbiomac_2012_06_041
PublicationCentury 2000
PublicationDate 2012-11-01
PublicationDateYYYYMMDD 2012-11-01
PublicationDate_xml – month: 11
  year: 2012
  text: 2012-11-01
  day: 01
PublicationDecade 2010
PublicationPlace Netherlands
PublicationPlace_xml – name: Netherlands
PublicationTitle International journal of biological macromolecules
PublicationTitleAlternate Int J Biol Macromol
PublicationYear 2012
Publisher Elsevier B.V
Publisher_xml – name: Elsevier B.V
References Hernandez-Muñoz, Villalobos (bib0020) 2004; 18
Wang, Zhao, Yang, Jiang (bib0175) 2007; 21
Giacomelli, Riegel, Petzhold, Silveira (bib0150) 2008; 41
Song, Zheng (bib0010) 2008; 22
Forato, Doriguetto, Fischer, Mascarenhas, Craievich, Colnago (bib0105) 2004; 54
Sun, Song, Zheng (bib0025) 2009; 90
Dong, Dicharry, Waxman, Parnas, Asendei (bib0070) 2008; 9
Tatham, Field, Morris, K.J.I’Anson, Cardle, Dufton, Shewry (bib0095) 1993; 268
Thomson, Miles, Popineau, Harries, Shewry, Tatham (bib0125) 1999; 1430
Durand, Corinne, Cannella, Pérez, Pebay-Peyroula, Vachette, Fieschi (bib0135) 2010; 169
Secundo, Guerrieri (bib0085) 2005; 53
Sarkar (bib0165) 1995; 26
Liang, Pinier, Leroux, Subirade (bib0045) 2009; 91
Song, Gao, Li, Zheng (bib0030) 2010; 24
Soares, Maia, Rayas-Duarte, Soldi (bib0075) 2009; 23
Arai, Ikura, Semisotnov, Kihara, Ameiya, Kuwajima (bib0080) 1998; 275
Khatkar, Fido, Tatham, Schofield (bib0065) 2002; 35
Hernandez-Muñoz, Kanavouras, Villalobos, Chiralt (bib0015) 2004; 52
Bugs, Forato, Bortoleto-Bugs, Fischer, Mascarenhas, Ward, Colnago (bib0110) 2004; 33
Nakajima, Ikada (bib0120) 1995; 6
Wolff, Czapla, Heyer, Radosta, Mischnick, Springer (bib0130) 2000; 41
Totosaus, Montejano, Salazar, Guerreiro (bib0170) 2002; 37
Soares, Patzer, Dersch, Wendorff, da Silveira, Pranke (bib0035) 2011; 49
Banc, Desbat, Renard, Popineau (bib0050) 2009; 91
Mylonas, Hascher, Bernad, Blackledge, Mandelkow, Svergun (bib0140) 2008; 47
Soares, Soldi (bib0040) 2010; 30
Liang, Pinier, Leroux, Subirade (bib0055) 2009; 93
Konno, Kataoka, Kamatari, Kanaori, Nosaka, Akasaka (bib0115) 1995; 251
Hsia, Anderson (bib0160) 2001; 103
Krysmann, Castelletto, Kelarakis, Hamley, Hule, Pochan (bib0145) 2008; 47
Shewry, D’Ovidio, Lafiandra, Jensins, Mills Enc, Békés (bib0155) 2008
Svergun, Koch (bib0090) 2003; 66
Sing, Khatkar (bib0005) 2005; 42
Xu, Bietz, Carrieri (bib0060) 2007; 101
Matsushima, Danno, Takezawa, Izumi (bib0100) 1997; 1339
Forato (10.1016/j.ijbiomac.2012.06.041_bib0105) 2004; 54
Thomson (10.1016/j.ijbiomac.2012.06.041_bib0125) 1999; 1430
Sun (10.1016/j.ijbiomac.2012.06.041_bib0025) 2009; 90
Dong (10.1016/j.ijbiomac.2012.06.041_bib0070) 2008; 9
Liang (10.1016/j.ijbiomac.2012.06.041_bib0045) 2009; 91
Khatkar (10.1016/j.ijbiomac.2012.06.041_bib0065) 2002; 35
Wang (10.1016/j.ijbiomac.2012.06.041_bib0175) 2007; 21
Secundo (10.1016/j.ijbiomac.2012.06.041_bib0085) 2005; 53
Matsushima (10.1016/j.ijbiomac.2012.06.041_bib0100) 1997; 1339
Giacomelli (10.1016/j.ijbiomac.2012.06.041_bib0150) 2008; 41
Hsia (10.1016/j.ijbiomac.2012.06.041_bib0160) 2001; 103
Hernandez-Muñoz (10.1016/j.ijbiomac.2012.06.041_bib0015) 2004; 52
Song (10.1016/j.ijbiomac.2012.06.041_bib0030) 2010; 24
Soares (10.1016/j.ijbiomac.2012.06.041_bib0035) 2011; 49
Konno (10.1016/j.ijbiomac.2012.06.041_bib0115) 1995; 251
Bugs (10.1016/j.ijbiomac.2012.06.041_bib0110) 2004; 33
Shewry (10.1016/j.ijbiomac.2012.06.041_bib0155) 2008
Xu (10.1016/j.ijbiomac.2012.06.041_bib0060) 2007; 101
Tatham (10.1016/j.ijbiomac.2012.06.041_bib0095) 1993; 268
Svergun (10.1016/j.ijbiomac.2012.06.041_bib0090) 2003; 66
Arai (10.1016/j.ijbiomac.2012.06.041_bib0080) 1998; 275
Krysmann (10.1016/j.ijbiomac.2012.06.041_bib0145) 2008; 47
Song (10.1016/j.ijbiomac.2012.06.041_bib0010) 2008; 22
Liang (10.1016/j.ijbiomac.2012.06.041_bib0055) 2009; 93
Durand (10.1016/j.ijbiomac.2012.06.041_bib0135) 2010; 169
Soares (10.1016/j.ijbiomac.2012.06.041_bib0075) 2009; 23
Mylonas (10.1016/j.ijbiomac.2012.06.041_bib0140) 2008; 47
Nakajima (10.1016/j.ijbiomac.2012.06.041_bib0120) 1995; 6
Sing (10.1016/j.ijbiomac.2012.06.041_bib0005) 2005; 42
Soares (10.1016/j.ijbiomac.2012.06.041_bib0040) 2010; 30
Hernandez-Muñoz (10.1016/j.ijbiomac.2012.06.041_bib0020) 2004; 18
Sarkar (10.1016/j.ijbiomac.2012.06.041_bib0165) 1995; 26
Banc (10.1016/j.ijbiomac.2012.06.041_bib0050) 2009; 91
Wolff (10.1016/j.ijbiomac.2012.06.041_bib0130) 2000; 41
Totosaus (10.1016/j.ijbiomac.2012.06.041_bib0170) 2002; 37
References_xml – volume: 35
  start-page: 307
  year: 2002
  end-page: 313
  ident: bib0065
  publication-title: Journal of Cereal Science
  contributor:
    fullname: Schofield
– volume: 268
  start-page: 26253
  year: 1993
  end-page: 26289
  ident: bib0095
  publication-title: Journal of Biological Chemistry
  contributor:
    fullname: Shewry
– volume: 1430
  start-page: 359
  year: 1999
  end-page: 366
  ident: bib0125
  publication-title: Biochimica et Biophysica Acta
  contributor:
    fullname: Tatham
– volume: 42
  start-page: 455
  year: 2005
  end-page: 471
  ident: bib0005
  publication-title: Journal of Food Science and Technology
  contributor:
    fullname: Khatkar
– volume: 91
  start-page: 169
  year: 2009
  end-page: 178
  ident: bib0045
  publication-title: Biopolymers
  contributor:
    fullname: Subirade
– volume: 23
  start-page: 181
  year: 2009
  end-page: 187
  ident: bib0075
  publication-title: Food Hydrocolloids
  contributor:
    fullname: Soldi
– volume: 26
  start-page: 195
  year: 1995
  end-page: 203
  ident: bib0165
  publication-title: Carbohydrate Polymers
  contributor:
    fullname: Sarkar
– volume: 251
  start-page: 95
  year: 1995
  end-page: 103
  ident: bib0115
  publication-title: Journal of Molecular Biology
  contributor:
    fullname: Akasaka
– volume: 47
  start-page: 10345
  year: 2008
  end-page: 10353
  ident: bib0140
  publication-title: Biochemistry
  contributor:
    fullname: Svergun
– volume: 1339
  start-page: 14
  year: 1997
  end-page: 22
  ident: bib0100
  publication-title: Biochimica et Biophysica Acta
  contributor:
    fullname: Izumi
– volume: 21
  start-page: 174
  year: 2007
  end-page: 179
  ident: bib0175
  publication-title: Food Hydrocolloids
  contributor:
    fullname: Jiang
– volume: 49
  start-page: 480
  year: 2011
  end-page: 486
  ident: bib0035
  publication-title: International Journal of Biological Macromolecules
  contributor:
    fullname: Pranke
– volume: 24
  start-page: 98
  year: 2010
  end-page: 104
  ident: bib0030
  publication-title: Food Hydrocolloids
  contributor:
    fullname: Zheng
– volume: 41
  start-page: 8009
  year: 2000
  end-page: 8016
  ident: bib0130
  publication-title: Polymer
  contributor:
    fullname: Springer
– volume: 37
  start-page: 589
  year: 2002
  end-page: 601
  ident: bib0170
  publication-title: International Journal of Food Science and Technology
  contributor:
    fullname: Guerreiro
– volume: 9
  start-page: 568
  year: 2008
  end-page: 573
  ident: bib0070
  publication-title: Biomacromolecules
  contributor:
    fullname: Asendei
– volume: 53
  start-page: 1757
  year: 2005
  end-page: 1764
  ident: bib0085
  publication-title: Journal of Agricultural and Food Chemistry
  contributor:
    fullname: Guerrieri
– volume: 22
  start-page: 1090
  year: 2008
  end-page: 1096
  ident: bib0010
  publication-title: Food Hydrocolloids
  contributor:
    fullname: Zheng
– volume: 30
  start-page: 691
  year: 2010
  end-page: 698
  ident: bib0040
  publication-title: Materials Science & Engineering C
  contributor:
    fullname: Soldi
– year: 2008
  ident: bib0155
  publication-title: Wheat Chemistry and Technology
  contributor:
    fullname: Békés
– volume: 66
  start-page: 1735
  year: 2003
  end-page: 1782
  ident: bib0090
  publication-title: Reports on Progress in Physics
  contributor:
    fullname: Koch
– volume: 18
  start-page: 647
  year: 2004
  end-page: 654
  ident: bib0020
  publication-title: Food Hydrocolloids
  contributor:
    fullname: Villalobos
– volume: 47
  start-page: 4597
  year: 2008
  end-page: 4605
  ident: bib0145
  publication-title: Biochemistry
  contributor:
    fullname: Pochan
– volume: 54
  start-page: 543
  year: 2004
  end-page: 547
  ident: bib0105
  publication-title: Journal of Agricultural and Food Chemistry
  contributor:
    fullname: Colnago
– volume: 169
  start-page: 45
  year: 2010
  end-page: 53
  ident: bib0135
  publication-title: Journal of Structural Biology
  contributor:
    fullname: Fieschi
– volume: 91
  start-page: 610
  year: 2009
  end-page: 622
  ident: bib0050
  publication-title: Biopolymers
  contributor:
    fullname: Popineau
– volume: 6
  start-page: 126
  year: 1995
  end-page: 130
  ident: bib0120
  publication-title: Bioconjugate Chemistry
  contributor:
    fullname: Ikada
– volume: 275
  start-page: 149
  year: 1998
  end-page: 162
  ident: bib0080
  publication-title: Journal of Molecular Biology
  contributor:
    fullname: Kuwajima
– volume: 103
  start-page: 37
  year: 2001
  end-page: 44
  ident: bib0160
  publication-title: Theoretical Applied Genetics
  contributor:
    fullname: Anderson
– volume: 93
  start-page: 418
  year: 2009
  end-page: 428
  ident: bib0055
  publication-title: Biopolymers
  contributor:
    fullname: Subirade
– volume: 33
  start-page: 335
  year: 2004
  end-page: 343
  ident: bib0110
  publication-title: European Biophysics Journal
  contributor:
    fullname: Colnago
– volume: 52
  start-page: 7897
  year: 2004
  end-page: 7904
  ident: bib0015
  publication-title: Journal of Agricultural and Food Chemistry
  contributor:
    fullname: Chiralt
– volume: 41
  start-page: 2677
  year: 2008
  end-page: 2682
  ident: bib0150
  publication-title: Macromolecules
  contributor:
    fullname: Silveira
– volume: 101
  start-page: 1025
  year: 2007
  end-page: 1030
  ident: bib0060
  publication-title: Food Chemistry
  contributor:
    fullname: Carrieri
– volume: 90
  start-page: 207
  year: 2009
  end-page: 211
  ident: bib0025
  publication-title: Journal of Food Engineering
  contributor:
    fullname: Zheng
– volume: 169
  start-page: 45
  year: 2010
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0135
  publication-title: Journal of Structural Biology
  doi: 10.1016/j.jsb.2009.08.009
  contributor:
    fullname: Durand
– volume: 54
  start-page: 543
  year: 2004
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0105
  publication-title: Journal of Agricultural and Food Chemistry
  contributor:
    fullname: Forato
– volume: 47
  start-page: 4597
  year: 2008
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0145
  publication-title: Biochemistry
  doi: 10.1021/bi8000616
  contributor:
    fullname: Krysmann
– volume: 6
  start-page: 126
  year: 1995
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0120
  publication-title: Bioconjugate Chemistry
  doi: 10.1021/bc00031a015
  contributor:
    fullname: Nakajima
– volume: 275
  start-page: 149
  year: 1998
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0080
  publication-title: Journal of Molecular Biology
  doi: 10.1006/jmbi.1997.1456
  contributor:
    fullname: Arai
– volume: 22
  start-page: 1090
  year: 2008
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0010
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2007.06.006
  contributor:
    fullname: Song
– volume: 33
  start-page: 335
  year: 2004
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0110
  publication-title: European Biophysics Journal
  doi: 10.1007/s00249-003-0354-3
  contributor:
    fullname: Bugs
– volume: 251
  start-page: 95
  year: 1995
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0115
  publication-title: Journal of Molecular Biology
  doi: 10.1006/jmbi.1995.0418
  contributor:
    fullname: Konno
– volume: 49
  start-page: 480
  year: 2011
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0035
  publication-title: International Journal of Biological Macromolecules
  doi: 10.1016/j.ijbiomac.2011.05.025
  contributor:
    fullname: Soares
– volume: 268
  start-page: 26253
  year: 1993
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0095
  publication-title: Journal of Biological Chemistry
  doi: 10.1016/S0021-9258(19)74308-7
  contributor:
    fullname: Tatham
– volume: 66
  start-page: 1735
  year: 2003
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0090
  publication-title: Reports on Progress in Physics
  doi: 10.1088/0034-4885/66/10/R05
  contributor:
    fullname: Svergun
– volume: 42
  start-page: 455
  year: 2005
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0005
  publication-title: Journal of Food Science and Technology
  contributor:
    fullname: Sing
– volume: 26
  start-page: 195
  year: 1995
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0165
  publication-title: Carbohydrate Polymers
  doi: 10.1016/0144-8617(94)00107-5
  contributor:
    fullname: Sarkar
– volume: 53
  start-page: 1757
  year: 2005
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0085
  publication-title: Journal of Agricultural and Food Chemistry
  doi: 10.1021/jf049061x
  contributor:
    fullname: Secundo
– volume: 103
  start-page: 37
  year: 2001
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0160
  publication-title: Theoretical Applied Genetics
  doi: 10.1007/s00122-001-0552-2
  contributor:
    fullname: Hsia
– volume: 18
  start-page: 647
  year: 2004
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0020
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2003.11.002
  contributor:
    fullname: Hernandez-Muñoz
– volume: 41
  start-page: 2677
  year: 2008
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0150
  publication-title: Macromolecules
  doi: 10.1021/ma7023792
  contributor:
    fullname: Giacomelli
– volume: 30
  start-page: 691
  year: 2010
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0040
  publication-title: Materials Science & Engineering C
  doi: 10.1016/j.msec.2010.02.026
  contributor:
    fullname: Soares
– volume: 1430
  start-page: 359
  year: 1999
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0125
  publication-title: Biochimica et Biophysica Acta
  doi: 10.1016/S0167-4838(99)00019-9
  contributor:
    fullname: Thomson
– volume: 91
  start-page: 610
  year: 2009
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0050
  publication-title: Biopolymers
  doi: 10.1002/bip.21188
  contributor:
    fullname: Banc
– volume: 47
  start-page: 10345
  year: 2008
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0140
  publication-title: Biochemistry
  doi: 10.1021/bi800900d
  contributor:
    fullname: Mylonas
– volume: 1339
  start-page: 14
  year: 1997
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0100
  publication-title: Biochimica et Biophysica Acta
  doi: 10.1016/S0167-4838(96)00212-9
  contributor:
    fullname: Matsushima
– volume: 52
  start-page: 7897
  year: 2004
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0015
  publication-title: Journal of Agricultural and Food Chemistry
  doi: 10.1021/jf0491613
  contributor:
    fullname: Hernandez-Muñoz
– volume: 90
  start-page: 207
  year: 2009
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0025
  publication-title: Journal of Food Engineering
  doi: 10.1016/j.jfoodeng.2008.06.024
  contributor:
    fullname: Sun
– year: 2008
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0155
  contributor:
    fullname: Shewry
– volume: 35
  start-page: 307
  year: 2002
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0065
  publication-title: Journal of Cereal Science
  doi: 10.1006/jcrs.2001.0430
  contributor:
    fullname: Khatkar
– volume: 37
  start-page: 589
  year: 2002
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0170
  publication-title: International Journal of Food Science and Technology
  doi: 10.1046/j.1365-2621.2002.00623.x
  contributor:
    fullname: Totosaus
– volume: 21
  start-page: 174
  year: 2007
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0175
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2006.03.006
  contributor:
    fullname: Wang
– volume: 23
  start-page: 181
  year: 2009
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0075
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2007.12.009
  contributor:
    fullname: Soares
– volume: 101
  start-page: 1025
  year: 2007
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0060
  publication-title: Food Chemistry
  doi: 10.1016/j.foodchem.2006.02.057
  contributor:
    fullname: Xu
– volume: 9
  start-page: 568
  year: 2008
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0070
  publication-title: Biomacromolecules
  doi: 10.1021/bm7011136
  contributor:
    fullname: Dong
– volume: 41
  start-page: 8009
  year: 2000
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0130
  publication-title: Polymer
  doi: 10.1016/S0032-3861(00)00168-3
  contributor:
    fullname: Wolff
– volume: 93
  start-page: 418
  year: 2009
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0055
  publication-title: Biopolymers
  doi: 10.1002/bip.21352
  contributor:
    fullname: Liang
– volume: 24
  start-page: 98
  year: 2010
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0030
  publication-title: Food Hydrocolloids
  doi: 10.1016/j.foodhyd.2009.08.010
  contributor:
    fullname: Song
– volume: 91
  start-page: 169
  year: 2009
  ident: 10.1016/j.ijbiomac.2012.06.041_bib0045
  publication-title: Biopolymers
  doi: 10.1002/bip.21109
  contributor:
    fullname: Liang
SSID ssj0006518
Score 2.0525508
Snippet A comparison of cross-linked and native gliadin suspensions, with respect to the state of protein globular structure was carried out using small-angle X-ray...
SourceID proquest
crossref
pubmed
fao
elsevier
SourceType Aggregation Database
Index Database
Publisher
StartPage 640
SubjectTerms Cross-Linking Reagents - pharmacology
crosslinking
Cysteine - pharmacology
Disulfides - chemistry
Gliadin
Gliadin - chemistry
Globular protein
glycerol
Glycerol - pharmacology
light scattering
Models, Molecular
Oscillatory rheology
Protein Unfolding
protein-protein interactions
Reducing Agents - pharmacology
rheological properties
Rheology
X-radiation
Title Dynamic rheological properties of native and cross-linked gliadin proteins
URI https://dx.doi.org/10.1016/j.ijbiomac.2012.06.041
https://www.ncbi.nlm.nih.gov/pubmed/22771580
https://search.proquest.com/docview/1037885016
Volume 51
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV07T8MwED4VGGBBvCkvGYk1beK6tjOiAipFsEAlNsvOA1KhtCpl5bdz5yQ8BsTAmMiJTnfWPez7vgM4S3sYNBTXgU0FFihEgumkVYGSTubC2Sj3B263d3I4FqPH_mMLBg0Whtoqa99f-XTvres33Vqb3VlRdKktCcNTj9CfRMpCQHOB4Q_3dOf9q81D9v0ZHy0OaPU3lPCkU0wI5G6JypDOBGUnFNFvAWopt9Pf01Afjq42YL3OI9l5JeomtLJyC1YHzfi2bRhdVLPm2fw5axwcm9HR-5w4VNk0Z6Un_Wa2TJmXJaDb3CxlTy8FddYzz-FQlK87ML66fBgMg3pwQpBgurMIXCK4SpIw07mQkcSaQKFLjjlHbeSJFhiyldVKuTiMCYYVuxjLjMhirZVHFsvrXVgup2W2DwzTqzTOMK1zLhecx1YqLFp6OsF_60Smbeg22jKzih_DNI1jE9Po15B-DXXQiagNcaNU88PSBp34n9_uoxWMfUIHaMb3nOjx_GBEEbbhtDGNQU3TtYcts-nbqyEkpNZ9XNuGvcpmn6JyrlTU1-HBP4Q6hDV6qgCKR7C8mL9lx5ipLNyJ34onsHJ-fTO8-wDJNuRQ
link.rule.ids 315,783,787,4509,24128,27936,27937,45597,45691
linkProvider Elsevier
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1LT-MwEB5BObAXxGuX8vRKXNMmrmM7R1RA5XmBStwsOw821SqtSnvltzPjJCwc0B64JpNoNGPNyzPfAJxmA3QaiuvAZgITFALBdNKqQEknC-FsVPiC2929HI3F9VP8tALDdhaG2iob21_bdG-tmyf9Rpr9WVn2qS0J3dOApj8JlCVehTVB8TEe6t7rvz4PGfsiH1EHRP5hTHjSKyc05W4Jy5CKgrIXiugrD7Va2OnXcaj3R5ebsNEEkuys5nULVvJqG9aH7f62Hbg-r5fNs_mfvLVwbEa19zmBqLJpwSqP-s1slTHPS0DXuXnGnv-W1FrPPIhDWb3swvjy4nE4CprNCUGK8c4icKngKk3DXBdCRhKTAoU2OeEcpVGkWqDPVlYr5ZIwoTmsxCWYZ0QWk60isphf_4RONa3yPWAYX2VJjnGdc4XgPLFSYdYy0Cn-W6cy60K_lZaZ1QAZpu0cm5hWvobka6iFTkRdSFqhmk-qNmjF__vtHmrB2Ge0gGb8wAkfz29GFGEXfreqMShpuvewVT5dvhgahdQ6Rtou_Kp19s4q50pFsQ73v8HUCayPHu9uze3V_c0B_KA39bTiIXQW82V-hGHLwh37Y_kGM7bl6Q
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Dynamic+rheological+properties+of+native+and+cross-linked+gliadin+proteins&rft.jtitle=International+journal+of+biological+macromolecules&rft.au=Soares%2C+Rosane+M.D.&rft.au=Lionzo%2C+Maria+I.&rft.au=Da+Silveira%2C+Nadya+P.&rft.au=Rayas-Duarte%2C+Patricia&rft.date=2012-11-01&rft.issn=0141-8130&rft.volume=51&rft.issue=4&rft.spage=640&rft.epage=646&rft_id=info:doi/10.1016%2Fj.ijbiomac.2012.06.041&rft.externalDBID=n%2Fa&rft.externalDocID=10_1016_j_ijbiomac_2012_06_041
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0141-8130&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0141-8130&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0141-8130&client=summon