Water redistribution determined by time domain NMR explains rheological properties of dense fibrous protein blends at high temperature

Floor K.G. Schreuders, Igor Bodnár, Philipp Erni, Remko M. Boom, Atze Jan van der Goot*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Blends of different plant proteins can form excellent basis for meat analogues by subjecting those to shear and heating. We here want to obtain more information of the internal structure of pea protein-gluten and soy protein-gluten blends, by using the polymer blending law to explain rheological responses. For this polymer blending law the water distribution over the two phases is the blend was obtained with time domain 1H NMR measurements using the NMR measurements of individual protein phases and on the blend. By matching the relaxation rate (R2) of the individual phases with those of the blend, the water distribution over the two phases could be obtained. Water is preferentially taken up by the soy or pea protein phase leaving less water for gluten, which effect strongly changes the volume fractions of the phases. Rheological properties of the separate phases as function of their hydration resulted in higher apparent modulus for the wheat gluten phase, and a lower one for the pea and soy protein phase. From the results, it was concluded that both blends show signs of a bi-continuous morphology. The SPI-WG blend showed an intermediate value between bi-continuous and SPI continuous. PPI-WG at lower temperatures showed a bi-continuous structure, while at higher processing temperatures and time was probably WG continuous.
Original languageEnglish
Article number105562
JournalFood Hydrocolloids
Volume101
DOIs
Publication statusPublished - 1 Apr 2020

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Scleroproteins
Glutens
blended foods
rheological properties
Peas
Nuclear magnetic resonance
Proteins
Soybean Proteins
Temperature
Water
pea protein
soy protein
gluten
Polymers
temperature
proteins
water
Plant Proteins
water distribution
Meats

Cite this

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title = "Water redistribution determined by time domain NMR explains rheological properties of dense fibrous protein blends at high temperature",
abstract = "Blends of different plant proteins can form excellent basis for meat analogues by subjecting those to shear and heating. We here want to obtain more information of the internal structure of pea protein-gluten and soy protein-gluten blends, by using the polymer blending law to explain rheological responses. For this polymer blending law the water distribution over the two phases is the blend was obtained with time domain 1H NMR measurements using the NMR measurements of individual protein phases and on the blend. By matching the relaxation rate (R2) of the individual phases with those of the blend, the water distribution over the two phases could be obtained. Water is preferentially taken up by the soy or pea protein phase leaving less water for gluten, which effect strongly changes the volume fractions of the phases. Rheological properties of the separate phases as function of their hydration resulted in higher apparent modulus for the wheat gluten phase, and a lower one for the pea and soy protein phase. From the results, it was concluded that both blends show signs of a bi-continuous morphology. The SPI-WG blend showed an intermediate value between bi-continuous and SPI continuous. PPI-WG at lower temperatures showed a bi-continuous structure, while at higher processing temperatures and time was probably WG continuous.",
author = "Schreuders, {Floor K.G.} and Igor Bodn{\'a}r and Philipp Erni and Boom, {Remko M.} and {van der Goot}, {Atze Jan}",
year = "2020",
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doi = "10.1016/j.foodhyd.2019.105562",
language = "English",
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journal = "Food Hydrocolloids",
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Water redistribution determined by time domain NMR explains rheological properties of dense fibrous protein blends at high temperature. / Schreuders, Floor K.G.; Bodnár, Igor; Erni, Philipp; Boom, Remko M.; van der Goot, Atze Jan.

In: Food Hydrocolloids, Vol. 101, 105562, 01.04.2020.

Research output: Contribution to journalArticleAcademicpeer-review

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AU - Schreuders, Floor K.G.

AU - Bodnár, Igor

AU - Erni, Philipp

AU - Boom, Remko M.

AU - van der Goot, Atze Jan

PY - 2020/4/1

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N2 - Blends of different plant proteins can form excellent basis for meat analogues by subjecting those to shear and heating. We here want to obtain more information of the internal structure of pea protein-gluten and soy protein-gluten blends, by using the polymer blending law to explain rheological responses. For this polymer blending law the water distribution over the two phases is the blend was obtained with time domain 1H NMR measurements using the NMR measurements of individual protein phases and on the blend. By matching the relaxation rate (R2) of the individual phases with those of the blend, the water distribution over the two phases could be obtained. Water is preferentially taken up by the soy or pea protein phase leaving less water for gluten, which effect strongly changes the volume fractions of the phases. Rheological properties of the separate phases as function of their hydration resulted in higher apparent modulus for the wheat gluten phase, and a lower one for the pea and soy protein phase. From the results, it was concluded that both blends show signs of a bi-continuous morphology. The SPI-WG blend showed an intermediate value between bi-continuous and SPI continuous. PPI-WG at lower temperatures showed a bi-continuous structure, while at higher processing temperatures and time was probably WG continuous.

AB - Blends of different plant proteins can form excellent basis for meat analogues by subjecting those to shear and heating. We here want to obtain more information of the internal structure of pea protein-gluten and soy protein-gluten blends, by using the polymer blending law to explain rheological responses. For this polymer blending law the water distribution over the two phases is the blend was obtained with time domain 1H NMR measurements using the NMR measurements of individual protein phases and on the blend. By matching the relaxation rate (R2) of the individual phases with those of the blend, the water distribution over the two phases could be obtained. Water is preferentially taken up by the soy or pea protein phase leaving less water for gluten, which effect strongly changes the volume fractions of the phases. Rheological properties of the separate phases as function of their hydration resulted in higher apparent modulus for the wheat gluten phase, and a lower one for the pea and soy protein phase. From the results, it was concluded that both blends show signs of a bi-continuous morphology. The SPI-WG blend showed an intermediate value between bi-continuous and SPI continuous. PPI-WG at lower temperatures showed a bi-continuous structure, while at higher processing temperatures and time was probably WG continuous.

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