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Quantification of the electrostatic and covalent interaction between whey proteins and low methoxyl pectin using PFG-NMR diffusometry

Arima Diah Setiowati (UGent) , Lien Vermeir (UGent) , Lorenz De Neve (UGent) , Ali Sedaghat Doost (UGent) , Davy Sinnaeve (UGent) and Paul Van der Meeren (UGent)
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Abstract
As interaction between proteins and polysaccharides is expected to change the average diffusion coefficient and the distribution width, it is believed that NMR diffusometry can be a useful tool to study and quantify the interaction between whey protein isolate (WPI) and low methoxyl pectin (LMP). For this purpose, the influence of pH, dry-heat-treatment duration, and WPI to LMP ratio on WPI and LMP interaction was evaluated using pulsed field gradient NMR. At pH5.0 and 5.5, approximately 40-50% of the WPI present in the mixture interacted with LMP through electrostatic interaction. Hence, it is important to measure the degree of covalent interaction at a pH where electrostatic interaction between WPI and LMP is limited. The diffusion coefficient of WPI gradually decreased as the mixtures of WPI and LMP were incubated for 1, 2, 8, and 16days, which was accompanied by an increase in the distribution width. With regard to the LMP concentration, the higher the LMP concentration, the higher the amount of WPI bound to LMP and the smaller the diffusion coefficient of WPI. Overall, the results indicate that NMR diffusometry enables the quantification of the interaction in biopolymer mixtures. Whereas the results showed a similar trend as that obtained via chemical analysis, pulsed field gradient NMR does not require any sample pretreatment.
Keywords
conjugates, complexes, H-1, degree of interaction, diffusion coefficient, dry-heat treatment, low methoxyl pectin, NMR, whey protein isolate, NUCLEAR-MAGNETIC-RESONANCE, IMPROVED HEAT-STABILITY, BETA-LACTOGLOBULIN, SELF-DIFFUSION, MAILLARD REACTION, SPIN-ECHO, EMULSIONS, WATER, DEXTRAN, COMPLEX

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MLA
Diah Setiowati, Arima, et al. “Quantification of the Electrostatic and Covalent Interaction between Whey Proteins and Low Methoxyl Pectin Using PFG-NMR Diffusometry.” MAGNETIC RESONANCE IN CHEMISTRY, vol. 57, no. 9, 2019, pp. 719–29.
APA
Diah Setiowati, A., Vermeir, L., De Neve, L., Sedaghat Doost, A., Sinnaeve, D., & Van der Meeren, P. (2019). Quantification of the electrostatic and covalent interaction between whey proteins and low methoxyl pectin using PFG-NMR diffusometry. MAGNETIC RESONANCE IN CHEMISTRY, 57(9), 719–729.
Chicago author-date
Diah Setiowati, Arima, Lien Vermeir, Lorenz De Neve, Ali Sedaghat Doost, Davy Sinnaeve, and Paul Van der Meeren. 2019. “Quantification of the Electrostatic and Covalent Interaction between Whey Proteins and Low Methoxyl Pectin Using PFG-NMR Diffusometry.” MAGNETIC RESONANCE IN CHEMISTRY 57 (9): 719–29.
Chicago author-date (all authors)
Diah Setiowati, Arima, Lien Vermeir, Lorenz De Neve, Ali Sedaghat Doost, Davy Sinnaeve, and Paul Van der Meeren. 2019. “Quantification of the Electrostatic and Covalent Interaction between Whey Proteins and Low Methoxyl Pectin Using PFG-NMR Diffusometry.” MAGNETIC RESONANCE IN CHEMISTRY 57 (9): 719–729.
Vancouver
1.
Diah Setiowati A, Vermeir L, De Neve L, Sedaghat Doost A, Sinnaeve D, Van der Meeren P. Quantification of the electrostatic and covalent interaction between whey proteins and low methoxyl pectin using PFG-NMR diffusometry. MAGNETIC RESONANCE IN CHEMISTRY. 2019;57(9):719–29.
IEEE
[1]
A. Diah Setiowati, L. Vermeir, L. De Neve, A. Sedaghat Doost, D. Sinnaeve, and P. Van der Meeren, “Quantification of the electrostatic and covalent interaction between whey proteins and low methoxyl pectin using PFG-NMR diffusometry,” MAGNETIC RESONANCE IN CHEMISTRY, vol. 57, no. 9, pp. 719–729, 2019.
@article{8585154,
  abstract     = {As interaction between proteins and polysaccharides is expected to change the average diffusion coefficient and the distribution width, it is believed that NMR diffusometry can be a useful tool to study and quantify the interaction between whey protein isolate (WPI) and low methoxyl pectin (LMP). For this purpose, the influence of pH, dry-heat-treatment duration, and WPI to LMP ratio on WPI and LMP interaction was evaluated using pulsed field gradient NMR. At pH5.0 and 5.5, approximately 40-50% of the WPI present in the mixture interacted with LMP through electrostatic interaction. Hence, it is important to measure the degree of covalent interaction at a pH where electrostatic interaction between WPI and LMP is limited. The diffusion coefficient of WPI gradually decreased as the mixtures of WPI and LMP were incubated for 1, 2, 8, and 16days, which was accompanied by an increase in the distribution width. With regard to the LMP concentration, the higher the LMP concentration, the higher the amount of WPI bound to LMP and the smaller the diffusion coefficient of WPI. Overall, the results indicate that NMR diffusometry enables the quantification of the interaction in biopolymer mixtures. Whereas the results showed a similar trend as that obtained via chemical analysis, pulsed field gradient NMR does not require any sample pretreatment.},
  author       = {Diah Setiowati, Arima and Vermeir, Lien and De Neve, Lorenz and Sedaghat Doost, Ali and Sinnaeve, Davy and Van der Meeren, Paul},
  issn         = {0749-1581},
  journal      = {MAGNETIC RESONANCE IN CHEMISTRY},
  keywords     = {conjugates,complexes,H-1,degree of interaction,diffusion coefficient,dry-heat treatment,low methoxyl pectin,NMR,whey protein isolate,NUCLEAR-MAGNETIC-RESONANCE,IMPROVED HEAT-STABILITY,BETA-LACTOGLOBULIN,SELF-DIFFUSION,MAILLARD REACTION,SPIN-ECHO,EMULSIONS,WATER,DEXTRAN,COMPLEX},
  language     = {eng},
  number       = {9},
  pages        = {719--729},
  title        = {Quantification of the electrostatic and covalent interaction between whey proteins and low methoxyl pectin using PFG-NMR diffusometry},
  url          = {http://dx.doi.org/10.1002/mrc.4812},
  volume       = {57},
  year         = {2019},
}

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