Pepsin diffusivity in whey protein gels and its effect on gastric digestion

Luo, Qi; Borst, Jan Willem; Westphal, Adrie H.; Boom, Remko M.; Janssen, Anja E.M.

doi:10.1016/j.foodhyd.2016.11.046

Cited by 123Proteins in Food SystemsProtein Hydrolysis and Bioactive PeptidesFood composition and properties

Pepsin diffusivity in whey protein gels and its effect on gastric digestion

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Luo, Qi, Borst, Jan Willem, Westphal, Adrie H., Boom, Remko M., Janssen, Anja E.M.·2017·Food Hydrocolloids

DOI 10.1016/j.foodhyd.2016.11.046

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Abstract

Protein is essential to human health, but its digestion kinetics in varied structures are not yet well understood. We previously found different kinetics of protein hydrolysis in solution and in gels, and we hypothesized that the difference stemmed from the steric hindrance of gel structure to the diffusion of pepsin and its hydrolysates. To better understand the pepsin diffusivity in food matrices and its effect on digestion, we determined the diffusivity of pepsin in water and in whey protein isolate (WPI) gels by fluorescence correlation spectroscopy (FCS). We estimated the pepsin concentration gradient during digestion based on the determined diffusivity, which showed that the pepsin is constrained within a thin layer from the gel surface. Gel composition analysis confirmed this constraint: peptides as protein fragments were observed only in the first 2 mm of the WPI gels after 6 h of in vitro gastric digestion. Scanning electron microscopy indicated that pepsin loosened the microstructure of whey protein gel surfaces, which may accelerate pepsin diffusion and consequently gel surface disintegration. We conclude that the mode of whey protein gel digestion is determined by the summed effect of diffusion limitation, hydrolysis rate and microstructure transformation.

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Increased gel texture at higher protein content delayed gastric empty and breakdown of gels during digestion, further reducing digestibility.
“Increased gel texture at higher protein content delayed the gastric empty and the breakdown of gels during digestion, further reducing digestibility.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Luo et al. 2017
The available passages labeled Abstract (no page given) contain bibliographic information and keywords, but no findings about protein content, gel texture, gastric emptying, gel breakdown, or digestibility. Searches for those terms returned no passage that addresses the claimed relationship. (LLM, conf=0.75)
Experimental — accuracy not yet measured
Denser microstructure and less porosity of protein gels could delay diffusion of pepsin into gel matrix, showing slower protein hydrolysis.
“The denser microstructure and less porosity of protein gels could delay the diffusion of pepsin into gel matrix, showing slower protein hydrolysis (Luo et al. 2017; Opazo‐Navarrete et al. 2018).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Luo et al. 2017
The available indexed passages identify a paper about pepsin diffusivity in whey protein gels, but contain no results or discussion establishing that denser, less porous gels delay pepsin diffusion and slow hydrolysis. Searches for microstructure, porosity, diffusion, and hydrolysis returned only bibliographic text (no section or page available). (LLM, conf=0.72)
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Influential
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“A certain resistance of emulsions to pepsin might be ascribed to that the hindrance effect of high-viscosity emulsion structures on the diffusion of pepsin hydrolysates [41].”
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Analysis and modeling of enhanced green fluorescent protein diffusivity in whey protein gels
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Floury, J., Bianchi, T., Thévenot, J., Dupont, D., Jamme, F., Lutton, É., Panouillé, M., Boué, F., & Feunteun, S. L. (2016) · HAL
Characterization of egg white gel microstructure and its relationship with pepsin diffusivity
Somaratne, G., Nau, F., Ferrua, M. J., Singh, J., Ye, A., Dupont, D., Singh, R. P., & Floury, J. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.105258 · Cited by 49 · see citing works
Assessment of pepsin diffusion within casein gels by quasi-elastic neutron scattering (QENS) and fluorescence recovery after photobleaching (FRAP)
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Authors: Luo, Q., Borst, J. W., Westphal, A. H., Boom, R. M., & Janssen, A. E. M.
Affiliations: Wageningen University & Research (NL)
Corresponding author: Janssen, Anja E.M.
ORCID: Luo, Qi
Borst, Jan Willem
Westphal, Adrie H.
Boom, Remko M.
Janssen, Anja E.M.
Venue: Food Hydrocolloids
Publisher: Elsevier BV
Published: 2017-05
Volume: 66
Pages: 318-325
ISSN: 0268-005X (ISSN-L)
DOI: 10.1016/j.foodhyd.2016.11.046
OpenAlex: W2558991208
Cited by: 123
References: 34
Citations by year: 2026: 18 · 2025: 11 · 2024: 12 · 2023: 17 · 2022: 8 · 2021: 17 · 2020: 14 · 2019: 16 · 2018: 9 · 2017: 1
FWCI: 10.92
Type: journal article
Language: en
Open access: green
research.wur.nl
Licence: cc-by-nc-nd
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Food Hydrocolloids (publishedVersion)
Socio-Environmental Systems Modeling (acceptedVersion, cc-by-nc-nd)
Data Archiving and Networked Services (DANS) (submittedVersion, cc-by-nc-nd)
Topics: Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
Keywords: gastric digestion, steric hindrance, diffusion limitation, gel microstructure, in vitro digestion

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Pepsin diffusivity in whey protein gels and its effect on gastric digestion

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