Functional ethanol-induced fibrils: Influence of solvents and temperature on amyloid-like aggregation of beta-lactoglobulin

Jil J. Kayser, Philipp Arnold, Anja Steffen-Heins, Karin Schwarz, Julia K. Keppler*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Solvent-induced fibrillar aggregates of beta-lactoglobulin occur only in a certain balance between hydrophobic forces and electrostatic interactions. We hypothesize, that different hydrophobic solvent molecules as well as rising temperatures influence this equilibrium and thus the optimum to produce amyloid aggregates. Dimethyl sulfoxide (DMSO), methanol and ethanol all resulted in polydisperse solutions with worm-like and spherical-aggregates, albeit to different degrees: the volume fraction required for aggregation was DMSO (50%) > methanol (40%) > ethanol (30%) which does not reflect their hydrophobicity. Further solvent addition decreased the fibrillar aggregation again. Increasing the temperature by 10–20 K decreased the solvent concentration needed to induce amyloid-like aggregates. A targeted production of solvent-based amyloid-like aggregates is therefore not only dependent on the hydrophobicity of the solvents, but also on their direct interaction with the protein (denaturation).

Original languageEnglish
Article number109764
JournalJournal of Food Engineering
Volume270
DOIs
Publication statusPublished - Apr 2020

Fingerprint

Lactoglobulins
beta-lactoglobulin
amyloid
Amyloid
protein aggregates
Ethanol
ethanol
Temperature
temperature
dimethyl sulfoxide
Dimethyl Sulfoxide
hydrophobicity
Hydrophobic and Hydrophilic Interactions
Methanol
methanol
Protein Denaturation
electrostatic interactions
Static Electricity

Keywords

  • Amyloid aggregation
  • Ethanol
  • Functional fibrils
  • Lactoglobulin
  • Solvent-induced protein denaturation
  • Whey protein

Cite this

@article{ac50eb24c63942c79d12d6457201039e,
title = "Functional ethanol-induced fibrils: Influence of solvents and temperature on amyloid-like aggregation of beta-lactoglobulin",
abstract = "Solvent-induced fibrillar aggregates of beta-lactoglobulin occur only in a certain balance between hydrophobic forces and electrostatic interactions. We hypothesize, that different hydrophobic solvent molecules as well as rising temperatures influence this equilibrium and thus the optimum to produce amyloid aggregates. Dimethyl sulfoxide (DMSO), methanol and ethanol all resulted in polydisperse solutions with worm-like and spherical-aggregates, albeit to different degrees: the volume fraction required for aggregation was DMSO (50{\%}) > methanol (40{\%}) > ethanol (30{\%}) which does not reflect their hydrophobicity. Further solvent addition decreased the fibrillar aggregation again. Increasing the temperature by 10–20 K decreased the solvent concentration needed to induce amyloid-like aggregates. A targeted production of solvent-based amyloid-like aggregates is therefore not only dependent on the hydrophobicity of the solvents, but also on their direct interaction with the protein (denaturation).",
keywords = "Amyloid aggregation, Ethanol, Functional fibrils, Lactoglobulin, Solvent-induced protein denaturation, Whey protein",
author = "Kayser, {Jil J.} and Philipp Arnold and Anja Steffen-Heins and Karin Schwarz and Keppler, {Julia K.}",
year = "2020",
month = "4",
doi = "10.1016/j.jfoodeng.2019.109764",
language = "English",
volume = "270",
journal = "Journal of Food Engineering",
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}

Functional ethanol-induced fibrils: Influence of solvents and temperature on amyloid-like aggregation of beta-lactoglobulin. / Kayser, Jil J.; Arnold, Philipp; Steffen-Heins, Anja; Schwarz, Karin; Keppler, Julia K.

In: Journal of Food Engineering, Vol. 270, 109764, 04.2020.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Functional ethanol-induced fibrils: Influence of solvents and temperature on amyloid-like aggregation of beta-lactoglobulin

AU - Kayser, Jil J.

AU - Arnold, Philipp

AU - Steffen-Heins, Anja

AU - Schwarz, Karin

AU - Keppler, Julia K.

PY - 2020/4

Y1 - 2020/4

N2 - Solvent-induced fibrillar aggregates of beta-lactoglobulin occur only in a certain balance between hydrophobic forces and electrostatic interactions. We hypothesize, that different hydrophobic solvent molecules as well as rising temperatures influence this equilibrium and thus the optimum to produce amyloid aggregates. Dimethyl sulfoxide (DMSO), methanol and ethanol all resulted in polydisperse solutions with worm-like and spherical-aggregates, albeit to different degrees: the volume fraction required for aggregation was DMSO (50%) > methanol (40%) > ethanol (30%) which does not reflect their hydrophobicity. Further solvent addition decreased the fibrillar aggregation again. Increasing the temperature by 10–20 K decreased the solvent concentration needed to induce amyloid-like aggregates. A targeted production of solvent-based amyloid-like aggregates is therefore not only dependent on the hydrophobicity of the solvents, but also on their direct interaction with the protein (denaturation).

AB - Solvent-induced fibrillar aggregates of beta-lactoglobulin occur only in a certain balance between hydrophobic forces and electrostatic interactions. We hypothesize, that different hydrophobic solvent molecules as well as rising temperatures influence this equilibrium and thus the optimum to produce amyloid aggregates. Dimethyl sulfoxide (DMSO), methanol and ethanol all resulted in polydisperse solutions with worm-like and spherical-aggregates, albeit to different degrees: the volume fraction required for aggregation was DMSO (50%) > methanol (40%) > ethanol (30%) which does not reflect their hydrophobicity. Further solvent addition decreased the fibrillar aggregation again. Increasing the temperature by 10–20 K decreased the solvent concentration needed to induce amyloid-like aggregates. A targeted production of solvent-based amyloid-like aggregates is therefore not only dependent on the hydrophobicity of the solvents, but also on their direct interaction with the protein (denaturation).

KW - Amyloid aggregation

KW - Ethanol

KW - Functional fibrils

KW - Lactoglobulin

KW - Solvent-induced protein denaturation

KW - Whey protein

U2 - 10.1016/j.jfoodeng.2019.109764

DO - 10.1016/j.jfoodeng.2019.109764

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VL - 270

JO - Journal of Food Engineering

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SN - 0260-8774

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