Characterising the effect of particle size and relative humidity on the microstructure and rehydration of milk protein concentrates in real-time using Environmental scanning electron microscopy

Lucille Gallagher, Valeria Cenini, David McSweeney, G McKerr, Noel McCarthy, Barry O'Hagan

Research output: Contribution to conferencePoster

Abstract

The functional and microstructural properties of milk protein concentrate (MPC) powder particles during rehydration are not well described. Currently, there are no published studies that have examined the influence of particle size and storage relative humidity (RH) on MPC microstructure using environmental scanning electron microscopy (ESEM). The aim of this study was to characterise the real-time rehydration of size determined MPC particles stored at varying RHs using ESEM.
Low-(MPC40), medium-(MPC55 and MPC65) and high-(MPC75 and MPC85) protein content MPC powders were manufactured by Teagasc Food Research Centre and stored at 54% and 88% RH, at a constant temperature of 4 oC. Five percentile ranges were determined from particle size distribution data derived from scanning electron microscopy (SEM) analysis of MPC particles. Surface composition was determined using X-ray photoelectron spectroscopy (XPS).
At 54%RH; MPC40 particles displayed a weakening of the external framework leading to their subsequent collapse and in most cases full dissolution. MPC55, MPC65 and MPC75 particles revealed partial dissolution with large breaks on the external skin of powder particles. High-(MPC85) particles displayed a restricted dissolution. At 88%RH, all MPC percentile ranges showed a graded disruption of the external skin of particles with marked changes in their hydration profiles.

Conference

ConferenceDynamic in-situ microscopy relating structure and function
CountryUnited Kingdom
CityLondon
Period21/10/1922/10/19
Internet address

Fingerprint

rehydration
microstructure
particle size
relative humidity
scanning electron microscopy
powders
skin (animal)
X-ray photoelectron spectroscopy
food research
milk protein concentrate
particle size distribution
protein content

Keywords

  • Milk protein concentrate
  • Environmental scanning electron microscopy
  • Rehydration
  • Solubility
  • Relative humidity

Cite this

Gallagher, L., Cenini, V., McSweeney, D., McKerr, G., McCarthy, N., & O'Hagan, B. (Accepted/In press). Characterising the effect of particle size and relative humidity on the microstructure and rehydration of milk protein concentrates in real-time using Environmental scanning electron microscopy. Poster session presented at Dynamic in-situ microscopy relating structure and function, London, United Kingdom.
Gallagher, Lucille ; Cenini, Valeria ; McSweeney, David ; McKerr, G ; McCarthy, Noel ; O'Hagan, Barry. / Characterising the effect of particle size and relative humidity on the microstructure and rehydration of milk protein concentrates in real-time using Environmental scanning electron microscopy. Poster session presented at Dynamic in-situ microscopy relating structure and function, London, United Kingdom.
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title = "Characterising the effect of particle size and relative humidity on the microstructure and rehydration of milk protein concentrates in real-time using Environmental scanning electron microscopy",
abstract = "The functional and microstructural properties of milk protein concentrate (MPC) powder particles during rehydration are not well described. Currently, there are no published studies that have examined the influence of particle size and storage relative humidity (RH) on MPC microstructure using environmental scanning electron microscopy (ESEM). The aim of this study was to characterise the real-time rehydration of size determined MPC particles stored at varying RHs using ESEM.Low-(MPC40), medium-(MPC55 and MPC65) and high-(MPC75 and MPC85) protein content MPC powders were manufactured by Teagasc Food Research Centre and stored at 54{\%} and 88{\%} RH, at a constant temperature of 4 oC. Five percentile ranges were determined from particle size distribution data derived from scanning electron microscopy (SEM) analysis of MPC particles. Surface composition was determined using X-ray photoelectron spectroscopy (XPS).At 54{\%}RH; MPC40 particles displayed a weakening of the external framework leading to their subsequent collapse and in most cases full dissolution. MPC55, MPC65 and MPC75 particles revealed partial dissolution with large breaks on the external skin of powder particles. High-(MPC85) particles displayed a restricted dissolution. At 88{\%}RH, all MPC percentile ranges showed a graded disruption of the external skin of particles with marked changes in their hydration profiles.",
keywords = "Milk protein concentrate, Environmental scanning electron microscopy, Rehydration, Solubility, Relative humidity",
author = "Lucille Gallagher and Valeria Cenini and David McSweeney and G McKerr and Noel McCarthy and Barry O'Hagan",
year = "2019",
month = "10",
day = "22",
language = "English",
note = "Dynamic in-situ microscopy relating structure and function ; Conference date: 21-10-2019 Through 22-10-2019",
url = "https://royalsociety.org/science-events-and-lectures/2019/10/in-situ-microscopy/",

}

Gallagher, L, Cenini, V, McSweeney, D, McKerr, G, McCarthy, N & O'Hagan, B 2019, 'Characterising the effect of particle size and relative humidity on the microstructure and rehydration of milk protein concentrates in real-time using Environmental scanning electron microscopy' Dynamic in-situ microscopy relating structure and function, London, United Kingdom, 21/10/19 - 22/10/19, .

Characterising the effect of particle size and relative humidity on the microstructure and rehydration of milk protein concentrates in real-time using Environmental scanning electron microscopy. / Gallagher, Lucille; Cenini, Valeria; McSweeney, David; McKerr, G; McCarthy, Noel; O'Hagan, Barry.

2019. Poster session presented at Dynamic in-situ microscopy relating structure and function, London, United Kingdom.

Research output: Contribution to conferencePoster

TY - CONF

T1 - Characterising the effect of particle size and relative humidity on the microstructure and rehydration of milk protein concentrates in real-time using Environmental scanning electron microscopy

AU - Gallagher, Lucille

AU - Cenini, Valeria

AU - McSweeney, David

AU - McKerr, G

AU - McCarthy, Noel

AU - O'Hagan, Barry

PY - 2019/10/22

Y1 - 2019/10/22

N2 - The functional and microstructural properties of milk protein concentrate (MPC) powder particles during rehydration are not well described. Currently, there are no published studies that have examined the influence of particle size and storage relative humidity (RH) on MPC microstructure using environmental scanning electron microscopy (ESEM). The aim of this study was to characterise the real-time rehydration of size determined MPC particles stored at varying RHs using ESEM.Low-(MPC40), medium-(MPC55 and MPC65) and high-(MPC75 and MPC85) protein content MPC powders were manufactured by Teagasc Food Research Centre and stored at 54% and 88% RH, at a constant temperature of 4 oC. Five percentile ranges were determined from particle size distribution data derived from scanning electron microscopy (SEM) analysis of MPC particles. Surface composition was determined using X-ray photoelectron spectroscopy (XPS).At 54%RH; MPC40 particles displayed a weakening of the external framework leading to their subsequent collapse and in most cases full dissolution. MPC55, MPC65 and MPC75 particles revealed partial dissolution with large breaks on the external skin of powder particles. High-(MPC85) particles displayed a restricted dissolution. At 88%RH, all MPC percentile ranges showed a graded disruption of the external skin of particles with marked changes in their hydration profiles.

AB - The functional and microstructural properties of milk protein concentrate (MPC) powder particles during rehydration are not well described. Currently, there are no published studies that have examined the influence of particle size and storage relative humidity (RH) on MPC microstructure using environmental scanning electron microscopy (ESEM). The aim of this study was to characterise the real-time rehydration of size determined MPC particles stored at varying RHs using ESEM.Low-(MPC40), medium-(MPC55 and MPC65) and high-(MPC75 and MPC85) protein content MPC powders were manufactured by Teagasc Food Research Centre and stored at 54% and 88% RH, at a constant temperature of 4 oC. Five percentile ranges were determined from particle size distribution data derived from scanning electron microscopy (SEM) analysis of MPC particles. Surface composition was determined using X-ray photoelectron spectroscopy (XPS).At 54%RH; MPC40 particles displayed a weakening of the external framework leading to their subsequent collapse and in most cases full dissolution. MPC55, MPC65 and MPC75 particles revealed partial dissolution with large breaks on the external skin of powder particles. High-(MPC85) particles displayed a restricted dissolution. At 88%RH, all MPC percentile ranges showed a graded disruption of the external skin of particles with marked changes in their hydration profiles.

KW - Milk protein concentrate

KW - Environmental scanning electron microscopy

KW - Rehydration

KW - Solubility

KW - Relative humidity

M3 - Poster

ER -

Gallagher L, Cenini V, McSweeney D, McKerr G, McCarthy N, O'Hagan B. Characterising the effect of particle size and relative humidity on the microstructure and rehydration of milk protein concentrates in real-time using Environmental scanning electron microscopy. 2019. Poster session presented at Dynamic in-situ microscopy relating structure and function, London, United Kingdom.