Analysis and modeling of enhanced green fluorescent protein diffusivity in whey protein gels

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

During gastric digestion, hydrolysis of proteins by pepsin contributes largely to the breakdown of protein-rich food. We hypothesized that the effect of pepsin is limited by its diffusivity, which is co-determined by the food structure and the local pH in the food during digestion. To investigate the principle mechanism of enzyme diffusion in food matrices, we used enhanced green fluorescent protein (EGFP) as probe to study the diffusivity of proteins in whey protein isolate gels, using fluorescence correlation spectroscopy (FCS). Gels made with different ionic strength showed distinctive elastic moduli but did not show differences in diffusivity of EGFP. Some models for diffusion in hydrogels yield good description of the obtained data, and can approximate the enzyme diffusion in diverse food matrices. However, the enzyme pepsin is more complicated than the probe EGFP, to yield more accurate predictions, electrostatic and enzyme-substrate interaction also need to be considered.

LanguageEnglish
Article number10.087
Pages449-455
JournalFood Research International
Volume120
Early online date1 Nov 2018
DOIs
Publication statusPublished - Jun 2019

Fingerprint

pepsin
whey protein
green fluorescent protein
diffusivity
food matrix
Gels
gels
Pepsin A
Food
enzymes
digestion
Enzymes
whey protein isolate
proteins
enzyme substrates
hydrocolloids
ionic strength
Digestion
modulus of elasticity
spectroscopy

Keywords

  • Diffusion
  • FCS
  • Gastric digestion
  • GFP
  • Modeling
  • Pepsin
  • Whey protein gel

Cite this

@article{77a7f298001e4776ba89cfccdc1e6c95,
title = "Analysis and modeling of enhanced green fluorescent protein diffusivity in whey protein gels",
abstract = "During gastric digestion, hydrolysis of proteins by pepsin contributes largely to the breakdown of protein-rich food. We hypothesized that the effect of pepsin is limited by its diffusivity, which is co-determined by the food structure and the local pH in the food during digestion. To investigate the principle mechanism of enzyme diffusion in food matrices, we used enhanced green fluorescent protein (EGFP) as probe to study the diffusivity of proteins in whey protein isolate gels, using fluorescence correlation spectroscopy (FCS). Gels made with different ionic strength showed distinctive elastic moduli but did not show differences in diffusivity of EGFP. Some models for diffusion in hydrogels yield good description of the obtained data, and can approximate the enzyme diffusion in diverse food matrices. However, the enzyme pepsin is more complicated than the probe EGFP, to yield more accurate predictions, electrostatic and enzyme-substrate interaction also need to be considered.",
keywords = "Diffusion, FCS, Gastric digestion, GFP, Modeling, Pepsin, Whey protein gel",
author = "Qi Luo and Erik Sewalt and Borst, {Jan Willem} and Westphal, {Adrie H.} and Boom, {Remko M.} and Janssen, {Anja E.M.}",
year = "2019",
month = "6",
doi = "10.1016/j.foodres.2018.10.087",
language = "English",
volume = "120",
pages = "449--455",
journal = "Food Research International",
issn = "0963-9969",
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}

Analysis and modeling of enhanced green fluorescent protein diffusivity in whey protein gels. / Luo, Qi; Sewalt, Erik; Borst, Jan Willem; Westphal, Adrie H.; Boom, Remko M.; Janssen, Anja E.M.

In: Food Research International, Vol. 120, 10.087, 06.2019, p. 449-455.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Analysis and modeling of enhanced green fluorescent protein diffusivity in whey protein gels

AU - Luo, Qi

AU - Sewalt, Erik

AU - Borst, Jan Willem

AU - Westphal, Adrie H.

AU - Boom, Remko M.

AU - Janssen, Anja E.M.

PY - 2019/6

Y1 - 2019/6

N2 - During gastric digestion, hydrolysis of proteins by pepsin contributes largely to the breakdown of protein-rich food. We hypothesized that the effect of pepsin is limited by its diffusivity, which is co-determined by the food structure and the local pH in the food during digestion. To investigate the principle mechanism of enzyme diffusion in food matrices, we used enhanced green fluorescent protein (EGFP) as probe to study the diffusivity of proteins in whey protein isolate gels, using fluorescence correlation spectroscopy (FCS). Gels made with different ionic strength showed distinctive elastic moduli but did not show differences in diffusivity of EGFP. Some models for diffusion in hydrogels yield good description of the obtained data, and can approximate the enzyme diffusion in diverse food matrices. However, the enzyme pepsin is more complicated than the probe EGFP, to yield more accurate predictions, electrostatic and enzyme-substrate interaction also need to be considered.

AB - During gastric digestion, hydrolysis of proteins by pepsin contributes largely to the breakdown of protein-rich food. We hypothesized that the effect of pepsin is limited by its diffusivity, which is co-determined by the food structure and the local pH in the food during digestion. To investigate the principle mechanism of enzyme diffusion in food matrices, we used enhanced green fluorescent protein (EGFP) as probe to study the diffusivity of proteins in whey protein isolate gels, using fluorescence correlation spectroscopy (FCS). Gels made with different ionic strength showed distinctive elastic moduli but did not show differences in diffusivity of EGFP. Some models for diffusion in hydrogels yield good description of the obtained data, and can approximate the enzyme diffusion in diverse food matrices. However, the enzyme pepsin is more complicated than the probe EGFP, to yield more accurate predictions, electrostatic and enzyme-substrate interaction also need to be considered.

KW - Diffusion

KW - FCS

KW - Gastric digestion

KW - GFP

KW - Modeling

KW - Pepsin

KW - Whey protein gel

U2 - 10.1016/j.foodres.2018.10.087

DO - 10.1016/j.foodres.2018.10.087

M3 - Article

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SP - 449

EP - 455

JO - Food Research International

T2 - Food Research International

JF - Food Research International

SN - 0963-9969

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