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Protein-protein interactions of a whey-pea protein co-precipitate

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Protein-protein interactions of a whey-pea protein co-precipitate. / Kristensen, Heidi Thorgaard; Christensen, Mette; Hansen, Mikka Stenholdt; Hammershoj, Marianne; Dalsgaard, Trine Kastrup.

In: International Journal of Food Science and Technology, 06.2021.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Kristensen, HT, Christensen, M, Hansen, MS, Hammershoj, M & Dalsgaard, TK 2021, 'Protein-protein interactions of a whey-pea protein co-precipitate', International Journal of Food Science and Technology. https://doi.org/10.1111/ijfs.15165

APA

Kristensen, H. T., Christensen, M., Hansen, M. S., Hammershoj, M., & Dalsgaard, T. K. (2021). Protein-protein interactions of a whey-pea protein co-precipitate. International Journal of Food Science and Technology. https://doi.org/10.1111/ijfs.15165

CBE

Kristensen HT, Christensen M, Hansen MS, Hammershoj M, Dalsgaard TK. 2021. Protein-protein interactions of a whey-pea protein co-precipitate. International Journal of Food Science and Technology. https://doi.org/10.1111/ijfs.15165

MLA

Kristensen, Heidi Thorgaard et al. "Protein-protein interactions of a whey-pea protein co-precipitate". International Journal of Food Science and Technology. 2021. https://doi.org/10.1111/ijfs.15165

Vancouver

Kristensen HT, Christensen M, Hansen MS, Hammershoj M, Dalsgaard TK. Protein-protein interactions of a whey-pea protein co-precipitate. International Journal of Food Science and Technology. 2021 Jun. https://doi.org/10.1111/ijfs.15165

Author

Kristensen, Heidi Thorgaard ; Christensen, Mette ; Hansen, Mikka Stenholdt ; Hammershoj, Marianne ; Dalsgaard, Trine Kastrup. / Protein-protein interactions of a whey-pea protein co-precipitate. In: International Journal of Food Science and Technology. 2021.

Bibtex

@article{87fd48bc864742ed80eeb459d24f4a37,
title = "Protein-protein interactions of a whey-pea protein co-precipitate",
abstract = "The aim of this study was to investigate the mechanisms behind protein-protein interactions in a co-precipitate of whey protein isolate (WPI) and pea protein isolate (PPI). A co-precipitate and blend, consisting of 80% WPI and 20% PPI, were compared. Covalent disulphide interactions were studied by blocking of free thiols with N-Ethylmaleimide (NEM), while electrostatic interactions were studied in systems with 0.5 m NaCl and hydrophobic interactions with 0.2% SDS. Protein solubility, stability and secondary, tertiary and quaternary protein structures were analysed. Co-precipitation did not introduce different protein-protein interactions than the direct blending of proteins. SDS affected solubility (P < 0.05), secondary and tertiary structure. However, the effects of NEM and NaCl were significant greater (P < 0.05) on the same parameters and thermal stability, especially when combined (P < 0.01). Thus, the protein-protein interactions in a whey-pea co-precipitate and protein blend consisted of disulphide bonds and electrostatic interactions.",
keywords = "co-precipitates, pea protein isolate, Pisum sativum L, protein-protein interactions, whey protein isolate, SODIUM DODECYL-SULFATE, BETA-LACTOGLOBULIN-A, ALPHA-LACTALBUMIN, THERMAL-STABILITY, SECONDARY STRUCTURE, N-ETHYLMALEIMIDE, MILK, AGGREGATION, MECHANISMS, ISOLATE",
author = "Kristensen, {Heidi Thorgaard} and Mette Christensen and Hansen, {Mikka Stenholdt} and Marianne Hammershoj and Dalsgaard, {Trine Kastrup}",
year = "2021",
month = jun,
doi = "10.1111/ijfs.15165",
language = "English",
journal = "International Journal of Food Science and Technology",
issn = "0950-5423",
publisher = "Wiley-Blackwell Publishing Ltd.",

}

RIS

TY - JOUR

T1 - Protein-protein interactions of a whey-pea protein co-precipitate

AU - Kristensen, Heidi Thorgaard

AU - Christensen, Mette

AU - Hansen, Mikka Stenholdt

AU - Hammershoj, Marianne

AU - Dalsgaard, Trine Kastrup

PY - 2021/6

Y1 - 2021/6

N2 - The aim of this study was to investigate the mechanisms behind protein-protein interactions in a co-precipitate of whey protein isolate (WPI) and pea protein isolate (PPI). A co-precipitate and blend, consisting of 80% WPI and 20% PPI, were compared. Covalent disulphide interactions were studied by blocking of free thiols with N-Ethylmaleimide (NEM), while electrostatic interactions were studied in systems with 0.5 m NaCl and hydrophobic interactions with 0.2% SDS. Protein solubility, stability and secondary, tertiary and quaternary protein structures were analysed. Co-precipitation did not introduce different protein-protein interactions than the direct blending of proteins. SDS affected solubility (P < 0.05), secondary and tertiary structure. However, the effects of NEM and NaCl were significant greater (P < 0.05) on the same parameters and thermal stability, especially when combined (P < 0.01). Thus, the protein-protein interactions in a whey-pea co-precipitate and protein blend consisted of disulphide bonds and electrostatic interactions.

AB - The aim of this study was to investigate the mechanisms behind protein-protein interactions in a co-precipitate of whey protein isolate (WPI) and pea protein isolate (PPI). A co-precipitate and blend, consisting of 80% WPI and 20% PPI, were compared. Covalent disulphide interactions were studied by blocking of free thiols with N-Ethylmaleimide (NEM), while electrostatic interactions were studied in systems with 0.5 m NaCl and hydrophobic interactions with 0.2% SDS. Protein solubility, stability and secondary, tertiary and quaternary protein structures were analysed. Co-precipitation did not introduce different protein-protein interactions than the direct blending of proteins. SDS affected solubility (P < 0.05), secondary and tertiary structure. However, the effects of NEM and NaCl were significant greater (P < 0.05) on the same parameters and thermal stability, especially when combined (P < 0.01). Thus, the protein-protein interactions in a whey-pea co-precipitate and protein blend consisted of disulphide bonds and electrostatic interactions.

KW - co-precipitates

KW - pea protein isolate

KW - Pisum sativum L

KW - protein-protein interactions

KW - whey protein isolate

KW - SODIUM DODECYL-SULFATE

KW - BETA-LACTOGLOBULIN-A

KW - ALPHA-LACTALBUMIN

KW - THERMAL-STABILITY

KW - SECONDARY STRUCTURE

KW - N-ETHYLMALEIMIDE

KW - MILK

KW - AGGREGATION

KW - MECHANISMS

KW - ISOLATE

U2 - 10.1111/ijfs.15165

DO - 10.1111/ijfs.15165

M3 - Journal article

JO - International Journal of Food Science and Technology

JF - International Journal of Food Science and Technology

SN - 0950-5423

ER -