Modulation of the gelation efficiency of fibrillar and spherical aggregates by means of thiolation

Claire D. Munialo, Harmen H.J. De Jongh, Kerensa Broersen, Erik Van Der Linden, Anneke H. Martin

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Fibrillar and spherical aggregates were prepared from whey protein isolate (WPI). These aggregates were thiolated to a substantial degree to observe any impact on functionality. Sulfur-containing groups were introduced on these aggregates which could be converted to thiol groups by deblocking. Changes on a molecular and microstructural level were studied using tryptophan fluorescence, transmission electron microscopy, and particle size analysis. The average size (nm) of spherical aggregates increased from 38 to 68 nm (blocked variant) and 106 nm (deblocked variant) after thiolation, whereas the structure of fibrillar aggregates was not affected. Subsequently, gels containing these different aggregates were prepared. Rheological measurements showed that thiolation decreased the gelation concentration and increased gel strength for both WPI fibrillar and spherical aggregates. This effect was more pronounced upon thiolation of preformed fibrillar aggregates. The findings suggest that thiolation at a protein aggregate level is a promising strategy to increase gelation efficiency.
Original languageEnglish
Pages (from-to)11628-11635
Number of pages8
JournalJournal of Agricultural and Food Chemistry
Volume61
Issue number47
DOIs
Publication statusPublished - 27 Nov 2013

Fingerprint

protein aggregates
Gelation
gelation
Gels
Modulation
Transmission Electron Microscopy
Particle Size
Sulfur
Sulfhydryl Compounds
Tryptophan
Fluorescence
whey protein isolate
Whey Proteins
gel strength
Particle size analysis
thiols
tryptophan
Proteins
transmission electron microscopy
particle size

Keywords

  • aggregates
  • chemical cross-linking
  • fibrillar
  • gelation efficiency
  • spherical
  • thiolation
  • whey protein isolate

Cite this

Modulation of the gelation efficiency of fibrillar and spherical aggregates by means of thiolation. / Munialo, Claire D.; De Jongh, Harmen H.J.; Broersen, Kerensa; Van Der Linden, Erik; Martin, Anneke H.

In: Journal of Agricultural and Food Chemistry, Vol. 61, No. 47, 27.11.2013, p. 11628-11635.

Research output: Contribution to journalArticle

Munialo, Claire D. ; De Jongh, Harmen H.J. ; Broersen, Kerensa ; Van Der Linden, Erik ; Martin, Anneke H. / Modulation of the gelation efficiency of fibrillar and spherical aggregates by means of thiolation. In: Journal of Agricultural and Food Chemistry. 2013 ; Vol. 61, No. 47. pp. 11628-11635.
@article{2937724cb7384f819e6d112d3fe7a85e,
title = "Modulation of the gelation efficiency of fibrillar and spherical aggregates by means of thiolation",
abstract = "Fibrillar and spherical aggregates were prepared from whey protein isolate (WPI). These aggregates were thiolated to a substantial degree to observe any impact on functionality. Sulfur-containing groups were introduced on these aggregates which could be converted to thiol groups by deblocking. Changes on a molecular and microstructural level were studied using tryptophan fluorescence, transmission electron microscopy, and particle size analysis. The average size (nm) of spherical aggregates increased from 38 to 68 nm (blocked variant) and 106 nm (deblocked variant) after thiolation, whereas the structure of fibrillar aggregates was not affected. Subsequently, gels containing these different aggregates were prepared. Rheological measurements showed that thiolation decreased the gelation concentration and increased gel strength for both WPI fibrillar and spherical aggregates. This effect was more pronounced upon thiolation of preformed fibrillar aggregates. The findings suggest that thiolation at a protein aggregate level is a promising strategy to increase gelation efficiency.",
keywords = "aggregates, chemical cross-linking, fibrillar, gelation efficiency, spherical, thiolation, whey protein isolate",
author = "Munialo, {Claire D.} and {De Jongh}, {Harmen H.J.} and Kerensa Broersen and {Van Der Linden}, Erik and Martin, {Anneke H.}",
year = "2013",
month = "11",
day = "27",
doi = "10.1021/jf403723m",
language = "English",
volume = "61",
pages = "11628--11635",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "47",

}

TY - JOUR

T1 - Modulation of the gelation efficiency of fibrillar and spherical aggregates by means of thiolation

AU - Munialo, Claire D.

AU - De Jongh, Harmen H.J.

AU - Broersen, Kerensa

AU - Van Der Linden, Erik

AU - Martin, Anneke H.

PY - 2013/11/27

Y1 - 2013/11/27

N2 - Fibrillar and spherical aggregates were prepared from whey protein isolate (WPI). These aggregates were thiolated to a substantial degree to observe any impact on functionality. Sulfur-containing groups were introduced on these aggregates which could be converted to thiol groups by deblocking. Changes on a molecular and microstructural level were studied using tryptophan fluorescence, transmission electron microscopy, and particle size analysis. The average size (nm) of spherical aggregates increased from 38 to 68 nm (blocked variant) and 106 nm (deblocked variant) after thiolation, whereas the structure of fibrillar aggregates was not affected. Subsequently, gels containing these different aggregates were prepared. Rheological measurements showed that thiolation decreased the gelation concentration and increased gel strength for both WPI fibrillar and spherical aggregates. This effect was more pronounced upon thiolation of preformed fibrillar aggregates. The findings suggest that thiolation at a protein aggregate level is a promising strategy to increase gelation efficiency.

AB - Fibrillar and spherical aggregates were prepared from whey protein isolate (WPI). These aggregates were thiolated to a substantial degree to observe any impact on functionality. Sulfur-containing groups were introduced on these aggregates which could be converted to thiol groups by deblocking. Changes on a molecular and microstructural level were studied using tryptophan fluorescence, transmission electron microscopy, and particle size analysis. The average size (nm) of spherical aggregates increased from 38 to 68 nm (blocked variant) and 106 nm (deblocked variant) after thiolation, whereas the structure of fibrillar aggregates was not affected. Subsequently, gels containing these different aggregates were prepared. Rheological measurements showed that thiolation decreased the gelation concentration and increased gel strength for both WPI fibrillar and spherical aggregates. This effect was more pronounced upon thiolation of preformed fibrillar aggregates. The findings suggest that thiolation at a protein aggregate level is a promising strategy to increase gelation efficiency.

KW - aggregates

KW - chemical cross-linking

KW - fibrillar

KW - gelation efficiency

KW - spherical

KW - thiolation

KW - whey protein isolate

U2 - 10.1021/jf403723m

DO - 10.1021/jf403723m

M3 - Article

VL - 61

SP - 11628

EP - 11635

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 47

ER -