Study of oxygen transfer across milk proteins at an air-water interface with scanning electrochemical microscopy

Outi Toikkanen (Corresponding Author), Maija Lähteenmäki, Timo Moisio, Pirkko Forssell, Riitta Partanen, Lasse Murtomäki

Research output: Contribution to journalArticleScientificpeer-review

11 Citations (Scopus)

Abstract

Scanning electrochemical microscopy (SECM) combined with a Langmuir trough was used for studying oxygen transfer across protein films at an air-water interface. The method allows the comparison of the oxygen permeability of different emulsifiers without any concerns of interference of atmospheric oxygen. Two milk proteins, ß-lactoglobulin and ß-casein, were compared, and the permeabilities obtained were for ß-casein PD ≈ 2.2 * 10-7 cm2/s and for ß-lactoglobulin PD ≈ 0.6 * 10-7 cm2/s, which correspond to the lowest limit of the diffusion coefficients and are 2 orders of magnitude lower than the diffusion coefficient of oxygen in water, yet several orders of magnitude higher than previously reported for milk protein films. The method allows characterization of the oxygen barrier properties of liquid interfacial films, which is of crucial importance for understanding the role of the interface in the inhibition of oxygen transport and developing modified interfaces with higher oxygen blocking efficacy
Original languageEnglish
Pages (from-to)2284-2288
Number of pages5
JournalJournal of Agricultural and Food Chemistry
Volume62
Issue number10
DOIs
Publication statusPublished - 2014
MoE publication typeA1 Journal article-refereed

Fingerprint

Electrochemical Scanning Microscopy
Milk Proteins
milk proteins
microscopy
Microscopic examination
Air
Oxygen
Scanning
oxygen
air
Water
lactoglobulins
water
Lactoglobulins
Caseins
diffusivity
casein
Permeability
permeability
emulsifiers

Keywords

  • Diffusion
  • langmuir film
  • mathematical modeling
  • milk proteins
  • SECM

Cite this

Toikkanen, Outi ; Lähteenmäki, Maija ; Moisio, Timo ; Forssell, Pirkko ; Partanen, Riitta ; Murtomäki, Lasse. / Study of oxygen transfer across milk proteins at an air-water interface with scanning electrochemical microscopy. In: Journal of Agricultural and Food Chemistry. 2014 ; Vol. 62, No. 10. pp. 2284-2288.
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title = "Study of oxygen transfer across milk proteins at an air-water interface with scanning electrochemical microscopy",
abstract = "Scanning electrochemical microscopy (SECM) combined with a Langmuir trough was used for studying oxygen transfer across protein films at an air-water interface. The method allows the comparison of the oxygen permeability of different emulsifiers without any concerns of interference of atmospheric oxygen. Two milk proteins, {\ss}-lactoglobulin and {\ss}-casein, were compared, and the permeabilities obtained were for {\ss}-casein PD ≈ 2.2 * 10-7 cm2/s and for {\ss}-lactoglobulin PD ≈ 0.6 * 10-7 cm2/s, which correspond to the lowest limit of the diffusion coefficients and are 2 orders of magnitude lower than the diffusion coefficient of oxygen in water, yet several orders of magnitude higher than previously reported for milk protein films. The method allows characterization of the oxygen barrier properties of liquid interfacial films, which is of crucial importance for understanding the role of the interface in the inhibition of oxygen transport and developing modified interfaces with higher oxygen blocking efficacy",
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author = "Outi Toikkanen and Maija L{\"a}hteenm{\"a}ki and Timo Moisio and Pirkko Forssell and Riitta Partanen and Lasse Murtom{\"a}ki",
year = "2014",
doi = "10.1021/jf5008715",
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Toikkanen, O, Lähteenmäki, M, Moisio, T, Forssell, P, Partanen, R & Murtomäki, L 2014, 'Study of oxygen transfer across milk proteins at an air-water interface with scanning electrochemical microscopy', Journal of Agricultural and Food Chemistry, vol. 62, no. 10, pp. 2284-2288. https://doi.org/10.1021/jf5008715

Study of oxygen transfer across milk proteins at an air-water interface with scanning electrochemical microscopy. / Toikkanen, Outi (Corresponding Author); Lähteenmäki, Maija; Moisio, Timo; Forssell, Pirkko; Partanen, Riitta; Murtomäki, Lasse.

In: Journal of Agricultural and Food Chemistry, Vol. 62, No. 10, 2014, p. 2284-2288.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Study of oxygen transfer across milk proteins at an air-water interface with scanning electrochemical microscopy

AU - Toikkanen, Outi

AU - Lähteenmäki, Maija

AU - Moisio, Timo

AU - Forssell, Pirkko

AU - Partanen, Riitta

AU - Murtomäki, Lasse

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Y1 - 2014

N2 - Scanning electrochemical microscopy (SECM) combined with a Langmuir trough was used for studying oxygen transfer across protein films at an air-water interface. The method allows the comparison of the oxygen permeability of different emulsifiers without any concerns of interference of atmospheric oxygen. Two milk proteins, ß-lactoglobulin and ß-casein, were compared, and the permeabilities obtained were for ß-casein PD ≈ 2.2 * 10-7 cm2/s and for ß-lactoglobulin PD ≈ 0.6 * 10-7 cm2/s, which correspond to the lowest limit of the diffusion coefficients and are 2 orders of magnitude lower than the diffusion coefficient of oxygen in water, yet several orders of magnitude higher than previously reported for milk protein films. The method allows characterization of the oxygen barrier properties of liquid interfacial films, which is of crucial importance for understanding the role of the interface in the inhibition of oxygen transport and developing modified interfaces with higher oxygen blocking efficacy

AB - Scanning electrochemical microscopy (SECM) combined with a Langmuir trough was used for studying oxygen transfer across protein films at an air-water interface. The method allows the comparison of the oxygen permeability of different emulsifiers without any concerns of interference of atmospheric oxygen. Two milk proteins, ß-lactoglobulin and ß-casein, were compared, and the permeabilities obtained were for ß-casein PD ≈ 2.2 * 10-7 cm2/s and for ß-lactoglobulin PD ≈ 0.6 * 10-7 cm2/s, which correspond to the lowest limit of the diffusion coefficients and are 2 orders of magnitude lower than the diffusion coefficient of oxygen in water, yet several orders of magnitude higher than previously reported for milk protein films. The method allows characterization of the oxygen barrier properties of liquid interfacial films, which is of crucial importance for understanding the role of the interface in the inhibition of oxygen transport and developing modified interfaces with higher oxygen blocking efficacy

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KW - langmuir film

KW - mathematical modeling

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KW - SECM

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