Effect of food matrix and human gastrointestinal conditions on the in vitro protein hydrolysis of lentil proteins
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Abstract This study aims to evaluate how food matrix, mechanical disintegration, and heat treatment can affect the protein hydrolysis of green lentils during three different in vitro gastrointestinal conditions (infant, late, and early phase adult). The hydrolysed proteins were characterised by sodium dodecyl sulphate–polyacrylamide gel electrophoresis and liquid chromatography coupled to quadrupole time-of-flight mass spectrometry (LC/Q-TOF/MS). In all digestion protocols, protein hydrolysis was higher in the lentil protein isolate compared to lentil flour and cooked lentils. Apart from lentil protein isolate, proteolysis was more efficient in the late-phase intestinal digests of cooked lentils compared to digest of lentil flour. Peptides released during digestion were more frequent and had small molecular weights in cooked lentils and protein isolate. Low enzyme activity in infant digestion negatively affected proteolysis. Peptides released from len c 1.010, which is a well-known allergen during in vitro digestion, showed shared motifs with Pru p 3 from Prunus persica, Ara h 9 from Arachis hypogaea, and nonspecific lipid-transfer protein Cor a 8.0101 from Corylus avellana, which are food allergens.
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Such dense aggregation structure hinders contact between proteases and protein peptide bonds, reducing hydrolysis efficiency and digestibility of proteins.
“Such dense aggregation structure hinders the contact between proteases (e.g., pepsin and trypsin) and protein peptide bonds, thereby reducing the hydrolysis efficiency and digestibility of proteins (T. Li, Han, et al. 2025; Ji et al. 2024; Karakaya and Hassas 2025).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Karakaya and Hassas 2025
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BIOPEP-UWM Database of Bioactive Peptides: Current Opportunities
Minkiewicz, P., Iwaniak, A., & Darewicz, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20235978 · Cited by 958 · see citing works
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Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion
Dong, X., Wang, Y., Chen, X. D., & Selomulya, C. (2026) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.70424 · Cited by 17 · see citing works
“Such dense aggregation structure hinders the contact between proteases (e.g., pepsin and trypsin) and protein peptide bonds, thereby reducing the hydrolysis efficiency and digestibility of proteins (T. Li, Han, et al. 2025 ; Ji et al. 2024 ; Karakaya and Hassas 2025 ).”
- Authors
- Karakaya, S., & Hassas, E.
- Affiliations
- Ege University (TR)
- Corresponding author
- Karakaya, Sibel
- ORCID
- Karakaya, Sibel
- Venue
- International Journal of Food Science and Technology
- Publisher
- Oxford University Press (OUP)
- Published
- 2025-01
- Volume
- 60
- Issue
- 1
- ISSN
- 0950-5423 (ISSN-L)
- 1365-2621
- OpenAlex
- W4406232486
- Cited by
- 0
- References
- 1
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- International Journal of Food Science & Technology (publishedVersion, cc-by)
- Funders
- Ege University Scientific Research Coordination Unit (22680)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Food Science › Food and Agricultural Sciences
- Keywords
- lentil protein, proteolysis, in vitro digestion, food matrix, lentil protein isolate, lentil flour, mechanical disintegration, heat treatment (food and biological processing), infant digestion, food allergens, Pru p 3, Ara h 9, lipid transfer proteins
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