Emulsifying peptides from potato protein predicted by bioinformatics: Stabilization of fish oil-in-water emulsions

Pedro Jesús García Moreno*, Charlotte Jacobsen, Paolo Marcatili, Simon Gregersen, Michael Toft Overgaard, Mogens Larsen Andersen, Ann-Dorit Moltke Sørensen, Egon Bech Hansen

*Corresponding author

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

This work investigated the use of bioinformatics to predict emulsifying peptides embedded in patatin proteins from potato (Solanum tuberosum). Six peptides (23–29 amino acids) with potentially different predominant structure at the oil/water interface (e.g. α-helix, β-strand or unordered) were identified within patatin sequences. The interfacial tension between peptides solutions and fish oil as well as the physical and oxidative stability of 5 wt% fish oil-in-water emulsions (pH 7) stabilized with synthetic predicted peptides were evaluated. The peptides predicted to have lower amphiphilic score (α1 and α2) led to emulsions with creaming after production and with low oxidative stability. On the other hand, a half hydrophobic and half hydrophilic peptide (γ1), which was predicted to have the highest amphiphilic score, showed a superior ability to reduce interfacial tension (even when compared to casein). γ1-Stabilized emulsion was physically stable during storage (48 h at 50 °C) and presented the lowest droplet size (D4,3 = 0.518 ± 0.011 μm). Electron spin resonance (ESR) and Oxygraph results indicated that the type of synthetic peptide used also affected the oxidative stability of fish oil-in-water emulsions differently. Therefore, this study shows the potential of using bioinformatics to predict emulsifying peptides, reducing time and cost of extensive screening hydrolysis processes.
Original languageEnglish
Article number105529
JournalFood Hydrocolloids
Volume101
ISSN0268-005X
DOIs
Publication statusPublished - Apr 2020

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Fish Oils
Bioinformatics
Emulsions
Stabilization
Peptides
Water
Proteins
Surface tension
Bioelectric potentials
Caseins
Paramagnetic resonance
Hydrolysis
Screening
Oils
Amino Acids

Cite this

García Moreno, Pedro Jesús ; Jacobsen, Charlotte ; Marcatili, Paolo ; Gregersen, Simon ; Overgaard, Michael Toft ; Andersen, Mogens Larsen ; Sørensen, Ann-Dorit Moltke ; Hansen, Egon Bech. / Emulsifying peptides from potato protein predicted by bioinformatics: Stabilization of fish oil-in-water emulsions. In: Food Hydrocolloids. 2020 ; Vol. 101.
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title = "Emulsifying peptides from potato protein predicted by bioinformatics: Stabilization of fish oil-in-water emulsions",
abstract = "This work investigated the use of bioinformatics to predict emulsifying peptides embedded in patatin proteins from potato (Solanum tuberosum). Six peptides (23–29 amino acids) with potentially different predominant structure at the oil/water interface (e.g. α-helix, β-strand or unordered) were identified within patatin sequences. The interfacial tension between peptides solutions and fish oil as well as the physical and oxidative stability of 5 wt{\%} fish oil-in-water emulsions (pH 7) stabilized with synthetic predicted peptides were evaluated. The peptides predicted to have lower amphiphilic score (α1 and α2) led to emulsions with creaming after production and with low oxidative stability. On the other hand, a half hydrophobic and half hydrophilic peptide (γ1), which was predicted to have the highest amphiphilic score, showed a superior ability to reduce interfacial tension (even when compared to casein). γ1-Stabilized emulsion was physically stable during storage (48 h at 50 °C) and presented the lowest droplet size (D4,3 = 0.518 ± 0.011 μm). Electron spin resonance (ESR) and Oxygraph results indicated that the type of synthetic peptide used also affected the oxidative stability of fish oil-in-water emulsions differently. Therefore, this study shows the potential of using bioinformatics to predict emulsifying peptides, reducing time and cost of extensive screening hydrolysis processes.",
author = "{Garc{\'i}a Moreno}, {Pedro Jes{\'u}s} and Charlotte Jacobsen and Paolo Marcatili and Simon Gregersen and Overgaard, {Michael Toft} and Andersen, {Mogens Larsen} and S{\o}rensen, {Ann-Dorit Moltke} and Hansen, {Egon Bech}",
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language = "English",
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journal = "Food Hydrocolloids",
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Emulsifying peptides from potato protein predicted by bioinformatics: Stabilization of fish oil-in-water emulsions. / García Moreno, Pedro Jesús; Jacobsen, Charlotte; Marcatili, Paolo; Gregersen, Simon; Overgaard, Michael Toft; Andersen, Mogens Larsen; Sørensen, Ann-Dorit Moltke; Hansen, Egon Bech.

In: Food Hydrocolloids, Vol. 101, 105529, 04.2020.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Emulsifying peptides from potato protein predicted by bioinformatics: Stabilization of fish oil-in-water emulsions

AU - García Moreno, Pedro Jesús

AU - Jacobsen, Charlotte

AU - Marcatili, Paolo

AU - Gregersen, Simon

AU - Overgaard, Michael Toft

AU - Andersen, Mogens Larsen

AU - Sørensen, Ann-Dorit Moltke

AU - Hansen, Egon Bech

PY - 2020/4

Y1 - 2020/4

N2 - This work investigated the use of bioinformatics to predict emulsifying peptides embedded in patatin proteins from potato (Solanum tuberosum). Six peptides (23–29 amino acids) with potentially different predominant structure at the oil/water interface (e.g. α-helix, β-strand or unordered) were identified within patatin sequences. The interfacial tension between peptides solutions and fish oil as well as the physical and oxidative stability of 5 wt% fish oil-in-water emulsions (pH 7) stabilized with synthetic predicted peptides were evaluated. The peptides predicted to have lower amphiphilic score (α1 and α2) led to emulsions with creaming after production and with low oxidative stability. On the other hand, a half hydrophobic and half hydrophilic peptide (γ1), which was predicted to have the highest amphiphilic score, showed a superior ability to reduce interfacial tension (even when compared to casein). γ1-Stabilized emulsion was physically stable during storage (48 h at 50 °C) and presented the lowest droplet size (D4,3 = 0.518 ± 0.011 μm). Electron spin resonance (ESR) and Oxygraph results indicated that the type of synthetic peptide used also affected the oxidative stability of fish oil-in-water emulsions differently. Therefore, this study shows the potential of using bioinformatics to predict emulsifying peptides, reducing time and cost of extensive screening hydrolysis processes.

AB - This work investigated the use of bioinformatics to predict emulsifying peptides embedded in patatin proteins from potato (Solanum tuberosum). Six peptides (23–29 amino acids) with potentially different predominant structure at the oil/water interface (e.g. α-helix, β-strand or unordered) were identified within patatin sequences. The interfacial tension between peptides solutions and fish oil as well as the physical and oxidative stability of 5 wt% fish oil-in-water emulsions (pH 7) stabilized with synthetic predicted peptides were evaluated. The peptides predicted to have lower amphiphilic score (α1 and α2) led to emulsions with creaming after production and with low oxidative stability. On the other hand, a half hydrophobic and half hydrophilic peptide (γ1), which was predicted to have the highest amphiphilic score, showed a superior ability to reduce interfacial tension (even when compared to casein). γ1-Stabilized emulsion was physically stable during storage (48 h at 50 °C) and presented the lowest droplet size (D4,3 = 0.518 ± 0.011 μm). Electron spin resonance (ESR) and Oxygraph results indicated that the type of synthetic peptide used also affected the oxidative stability of fish oil-in-water emulsions differently. Therefore, this study shows the potential of using bioinformatics to predict emulsifying peptides, reducing time and cost of extensive screening hydrolysis processes.

U2 - https://doi.org/10.1016/j.foodhyd.2019.105529

DO - https://doi.org/10.1016/j.foodhyd.2019.105529

M3 - Journal article

VL - 101

JO - Food Hydrocolloids

JF - Food Hydrocolloids

SN - 0268-005X

M1 - 105529

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