Effect of transglutaminase on structure and syneresis of neutral and acidic sodium caseinate gels

Riitta Partanen, Karin Autio, Päivi Myllärinen, Martina Lille, Johanna Buchert, Pirkko Forssell

Research output: Contribution to journalArticleScientificpeer-review

26 Citations (Scopus)

Abstract

The effect of transglutaminase on nuclear magnetic resonance (NMR) relaxation behaviour, porosity, firmness and syneresis of neutral and acidic sodium caseinate gels was studied. A drastic increase in porosity was observed to increase the amount of separating water up to 15% of gel weight, but structural homogeneity at the level of confocal laser scanning microscope (CLSM) resolution did not inhibit water separation in other acidic gels. Spin–spin relaxation time was reduced from 0.32 s (peak value) of the neutral transglutaminase-containing gel to 0.14 s of the corresponding acidic gel. The reduction was attributed to reduced mobility of protein protons in exchange with water protons in the system. With sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS–PAGE) analysis, more pronounced cross-linking of protein was observed at neutral than at acidic conditions, yet the neutral gel was weak compared with the acidic gel. It was assumed that, because of transglutaminase action, electrostatic repulsion was partially removed from the surface of sodium caseinate particles, allowing, e.g., hydrophobic interactions between the particles and gel formation. The mobility of proteins in the gel network was suggested to be related to its syneresis behaviour.
Original languageEnglish
Pages (from-to)414-421
JournalInternational Dairy Journal
Volume18
Issue number4
DOIs
Publication statusPublished - 2008
MoE publication typeA1 Journal article-refereed

Fingerprint

sodium caseinate
Transglutaminases
protein-glutamine gamma-glutamyltransferase
Caseins
Gels
gels
Porosity
protons
porosity
Protons
Water
Proteins
electrostatic interactions
proteins
water
hydrophobic bonding
Static Electricity
Hydrophobic and Hydrophilic Interactions
crosslinking
Sodium Dodecyl Sulfate

Keywords

  • sodium caseinate
  • gels
  • syneresis
  • pH
  • proton NMR
  • water mobility

Cite this

Partanen, Riitta ; Autio, Karin ; Myllärinen, Päivi ; Lille, Martina ; Buchert, Johanna ; Forssell, Pirkko. / Effect of transglutaminase on structure and syneresis of neutral and acidic sodium caseinate gels. In: International Dairy Journal. 2008 ; Vol. 18, No. 4. pp. 414-421.
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abstract = "The effect of transglutaminase on nuclear magnetic resonance (NMR) relaxation behaviour, porosity, firmness and syneresis of neutral and acidic sodium caseinate gels was studied. A drastic increase in porosity was observed to increase the amount of separating water up to 15{\%} of gel weight, but structural homogeneity at the level of confocal laser scanning microscope (CLSM) resolution did not inhibit water separation in other acidic gels. Spin–spin relaxation time was reduced from 0.32 s (peak value) of the neutral transglutaminase-containing gel to 0.14 s of the corresponding acidic gel. The reduction was attributed to reduced mobility of protein protons in exchange with water protons in the system. With sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS–PAGE) analysis, more pronounced cross-linking of protein was observed at neutral than at acidic conditions, yet the neutral gel was weak compared with the acidic gel. It was assumed that, because of transglutaminase action, electrostatic repulsion was partially removed from the surface of sodium caseinate particles, allowing, e.g., hydrophobic interactions between the particles and gel formation. The mobility of proteins in the gel network was suggested to be related to its syneresis behaviour.",
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Effect of transglutaminase on structure and syneresis of neutral and acidic sodium caseinate gels. / Partanen, Riitta; Autio, Karin; Myllärinen, Päivi; Lille, Martina; Buchert, Johanna; Forssell, Pirkko.

In: International Dairy Journal, Vol. 18, No. 4, 2008, p. 414-421.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Effect of transglutaminase on structure and syneresis of neutral and acidic sodium caseinate gels

AU - Partanen, Riitta

AU - Autio, Karin

AU - Myllärinen, Päivi

AU - Lille, Martina

AU - Buchert, Johanna

AU - Forssell, Pirkko

PY - 2008

Y1 - 2008

N2 - The effect of transglutaminase on nuclear magnetic resonance (NMR) relaxation behaviour, porosity, firmness and syneresis of neutral and acidic sodium caseinate gels was studied. A drastic increase in porosity was observed to increase the amount of separating water up to 15% of gel weight, but structural homogeneity at the level of confocal laser scanning microscope (CLSM) resolution did not inhibit water separation in other acidic gels. Spin–spin relaxation time was reduced from 0.32 s (peak value) of the neutral transglutaminase-containing gel to 0.14 s of the corresponding acidic gel. The reduction was attributed to reduced mobility of protein protons in exchange with water protons in the system. With sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS–PAGE) analysis, more pronounced cross-linking of protein was observed at neutral than at acidic conditions, yet the neutral gel was weak compared with the acidic gel. It was assumed that, because of transglutaminase action, electrostatic repulsion was partially removed from the surface of sodium caseinate particles, allowing, e.g., hydrophobic interactions between the particles and gel formation. The mobility of proteins in the gel network was suggested to be related to its syneresis behaviour.

AB - The effect of transglutaminase on nuclear magnetic resonance (NMR) relaxation behaviour, porosity, firmness and syneresis of neutral and acidic sodium caseinate gels was studied. A drastic increase in porosity was observed to increase the amount of separating water up to 15% of gel weight, but structural homogeneity at the level of confocal laser scanning microscope (CLSM) resolution did not inhibit water separation in other acidic gels. Spin–spin relaxation time was reduced from 0.32 s (peak value) of the neutral transglutaminase-containing gel to 0.14 s of the corresponding acidic gel. The reduction was attributed to reduced mobility of protein protons in exchange with water protons in the system. With sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS–PAGE) analysis, more pronounced cross-linking of protein was observed at neutral than at acidic conditions, yet the neutral gel was weak compared with the acidic gel. It was assumed that, because of transglutaminase action, electrostatic repulsion was partially removed from the surface of sodium caseinate particles, allowing, e.g., hydrophobic interactions between the particles and gel formation. The mobility of proteins in the gel network was suggested to be related to its syneresis behaviour.

KW - sodium caseinate

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KW - syneresis

KW - pH

KW - proton NMR

KW - water mobility

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JO - International Dairy Journal

JF - International Dairy Journal

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