The DOI matches its Crossref record; 127 of the 127 references it cites were found in a registry or an index.
How processing may affect milk protein digestion and overall physiological outcomes: A systematic review
Open accessAbstract
Dairy is one of the main sources for high quality protein in the human diet. Processing may, however, cause denaturation, aggregation, and chemical modifications of its amino acids, which may impact protein quality. This systematic review covers the effect of milk protein modifications as a result of heating, on protein digestion and its physiological impact. A total of 5363 records were retrieved through the Scopus database of which a total of 102 were included. Although the degree of modification highly depends on the exact processing conditions, heating of milk proteins can modify several amino acids. In vitro and animal studies demonstrate that glycation decreases protein digestibility, and hinders amino acid availability, especially for lysine. Other chemical modifications, including oxidation, racemization, dephosphorylation and cross-linking, are less well studied, but may also impact protein digestion, which may result in decreased amino acid bioavailability and functionality. On the other hand, protein denaturation does not affect overall digestibility, but can facilitate gastric hydrolysis, especially of β-lactoglobulin. Protein denaturation can also alter gastric emptying of the protein, consequently affecting digestive kinetics that can eventually result in different post-prandial plasma amino acid appearance. Apart from processing, the kinetics of protein digestion depend on the matrix in which the protein is heated. Altogether, protein modifications may be considered indicative for processing severity. Controlling dairy processing conditions can thus be a powerful way to preserve protein quality or to steer gastrointestinal digestion kinetics and subsequent release of amino acids. Related physiological consequences mainly point towards amino acid bioavailability and immunological consequences.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The decline from d 0 to d 20 likely resulted from the conversion of residual lactose into lactic acid, whereas the subsequent rise from d 20 to d 30 may be due to the formation of alkaline compounds from protein degradation (van Lieshout et al., 2020).”
From Impact of lactic acid bacteria coculture on the quality characteristics of goat cheese during ripening (2025) · cites this paper as van Lieshout et al., 2020
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Preferred Reporting Items for Systematic Reviews and Meta-Analyses: the PRISMA statement
Moher, D., Liberati, A., Tetzlaff, J., Altman, D. G., & for the PRISMA Group (2009) · BMJ · doi:10.1136/bmj.b2535 · Cited by 83,823
Preferred Reporting Items for Systematic Reviews and Meta-Analyses: The PRISMA Statement
Moher, D., Liberati, A., Tetzlaff, J., Altman, D. G., & The PRISMA Group (2009) · PLoS Medicine · doi:10.1371/journal.pmed.1000097 · Cited by 64,042 · cited 1×
“Database search results according the PRISMA statement (Moher et al. 2009).”
INFOGEST static in vitro simulation of gastrointestinal food digestion
Brodkorb, A., Egger, L., Alminger, M., Alvito, P., Assunção, R., Ballance, S., Bohn, T., Bourlieu-Lacanal, C., Boutrou, R., Carrière, F., et al. (2019) · Nature Protocols · doi:10.1038/s41596-018-0119-1 · Cited by 5,199 · cited 1×
“In this respect, it is recommended to adopt a straightforward harmonized approach, as e.g. recently discussed by the INFOGEST network (Brodkorb et al. 2019).”
MethodWalstra, P., Walstra, P., Wouters, J. T. M., & Geurts, T. J. (2005) · doi:10.1201/9781420028010 · Cited by 1,788
Advanced glycation endproducts in food and their effects on health
Poulsen, M. W., Hedegaard, R. V., Andersen, J. M., de Courten, B., Bügel, S., Nielsen, J., Skibsted, L. H., & Dragsted, L. O. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.06.052 · Cited by 751
Scientific Opinion on Dietary Reference Values for protein
EFSA Panel on Dietetic Products, N. A. A. (. (2012) · EFSA Journal · doi:10.2903/j.efsa.2012.2557 · Cited by 739
Effect of heating on Maillard reactions in milk
van Boekel, M. A. J. S. (1998) · Food Chemistry · doi:10.1016/s0308-8146(98)00075-2 · Cited by 578
Towards microbial fermentation metabolites as markers for health benefits of prebiotics
Verbeke, K. A., Boobis, A. R., Chiodini, A., Edwards, C. A., Franck, A., Kleerebezem, M., Nauta, A., Raes, J., van Tol, E. A. F., & Tuohy, K. M. (2015) · Nutrition Research Reviews · doi:10.1017/s0954422415000037 · Cited by 343 · cited 1×
“…fermentation, microbiome protein fermentation is less extensively researched and the toxic potential of these compounds is predominantly derived from in vitro cell-toxicity and animal studies determining effects of purified individual protein fermentation by-products (Verbeke et al. 2015).”
BackgroundThe role of methylglyoxal and the glyoxalase system in diabetes and other age-related diseases
Maessen, D. E., Stehouwer, C. D. A., & Schalkwijk, C. G. (2015) · Clinical Science · doi:10.1042/cs20140683 · Cited by 342 · cited 1×
“The group where RAGE and AGER1 was increased also had the highest urinary excretion of the AGE methylglyoxal-derived hydroimidazolone, which is associated with age-related diseases (Maessen, Stehouwer, and Schalkwijk 2015).”
BackgroundFriedman, M. (1999) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf981000+ · Cited by 339 · cited 1×
“Several reviews already describe the effect of heating on food proteins in general (Friedman 1999; Gerrard et al. 2012; Mauron 1990).”
Background
Research works printed but not linked: 4
- Delorenzi N. J., 2011, Whey: Types, composition and health implications, 169
- Erbersdobler H., 1989, Bibliotheka Nutrio et Dieta, 43, 140
- 10.1021/jf981000 + · DOI
- Liusuwan R. A., 1996, FASEB Journal, 10
Cited by
Sorted by citations
Protein Quality in Perspective: A Review of Protein Quality Metrics and Their Applications
Adhikari, S., Schop, M., de Boer, I. J. M., & Huppertz, T. (2022) · Nutrients · doi:10.3390/nu14050947 · Cited by 265
Kaur, L., Mao, B., Beniwal, A. S., Abhilasha, A., Kaur, R., Chian, F. M., & Singh, J. (2022) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2022.02.021 · Cited by 180
Dairy bioactive proteins and peptides: a narrative review
Auestad, N., & Layman, D. K. (2021) · Nutrition Reviews · doi:10.1093/nutrit/nuab097 · Cited by 153
“A systematic review of descriptive research, in vitro digestibility models, animal studies, and a single human clinical trial(21) found no overall effect of heat treatments used in processing liquid milk on dairy protein digestibility or bioavailability.(21,23) In vitro and animal studies similarly demonstrated no eff…”
Milk protein coagulation under gastric conditions: A review
Huppertz, T., & Chia, L. W. (2020) · International Dairy Journal · doi:10.1016/j.idairyj.2020.104882 · Cited by 146
Protein digestion and absorption: the influence of food processing
Loveday, S. M. (2022) · Nutrition Research Reviews · doi:10.1017/s0954422422000245 · Cited by 163
Bielecka, M. M., Cichosz, G., & Czeczot, H. (2021) · International Dairy Journal · doi:10.1016/j.idairyj.2021.105208 · Cited by 132
Heat-induced denaturation and bioactivity changes of whey proteins
Zhang, L., Zhou, R., Zhang, J., & Zhou, P. (2021) · International Dairy Journal · doi:10.1016/j.idairyj.2021.105175 · Cited by 114
Wang, W., Yang, P., Rao, L., Zhao, L., Wu, X., Wang, Y., & Liao, X. (2022) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.13033 · Cited by 116
Magan, J. B., O’Callaghan, T. F., Kelly, A. L., & McCarthy, N. A. (2021) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12751 · Cited by 108
“However, the level of whey protein denaturation is dependent on the heat load applied during pasteurisation, which is negligible at standard high temperature– short time conditions of 72 ◦C × 15 s (van Lieshout et al., 2020).”
BackgroundMcLaren, S. J., Berardy, A., Henderson, A. D., Holden, N. M., Huppertz, T., Jolliet, O., De Camillis, C., Renouf, M. A., Rugani, B., Saarinen, M., et al. (2021) · FAO eBooks · doi:10.4060/cb8054en · Cited by 106
Maryniak, N. Z., Sancho, A. I., Hansen, E. B., & Bøgh, K. L. (2022) · Foods · doi:10.3390/foods11070926 · Cited by 89
Ye, A. (2021) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.106599 · Cited by 91
Zenker, H. E., van Lieshout, G. A. A., van Gool, M. P., Bragt, M. C. E., & Hettinga, K. A. (2019) · Food & Function · doi:10.1039/c9fo02097g · Cited by 83
Self-citationThermal Denaturation and Aggregation of Whey Proteins
Le, T. T. (2021) · Encyclopedia of Dairy Sciences · doi:10.1016/b978-0-12-818766-1.00314-7 · Cited by 77
Lima, M. J. A., Sasaki, M. K., Marinho, O. R., Freitas, T. A., Faria, R. C., dos Reis, B. F., & Rocha, F. R. P. (2020) · Microchemical Journal · doi:10.1016/j.microc.2020.105042 · Cited by 75
Picariello, G., Siano, F., Stasio, L. D., Mamone, G., Addeo, F., & Ferranti, P. (2023) · Current Opinion in Food Science · doi:10.1016/j.cofs.2023.100992 · Cited by 70
Milk Processing Affects Structure, Bioavailability and Immunogenicity of β-lactoglobulin
Broersen, K. (2020) · Foods · doi:10.3390/foods9070874 · Cited by 66
Digestion of food proteins: the role of pepsin
Yang, M., Yang, Z., Everett, D. W., Gilbert, E. P., Singh, H., & Ye, A. (2025) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2025.2453096 · Cited by 65
“Previous studies on protein digestion fall into four categories: in vivo human studies, in vivo animal studies, static in vitro studies, and (semi)-dynamic in vitro studies (van Lieshout et al. 2020).”
van der Lugt, T., Venema, K., van Leeuwen, S. P. J., Vrolijk, M. F., Opperhuizen, A., & Bast, A. (2020) · Food & Function · doi:10.1039/d0fo00450b · Cited by 64
Zhang, Y., Dong, L., Zhang, J., Shi, J., Wang, Y., & Wang, S. (2021) · Annual Review of Food Science and Technology · doi:10.1146/annurev-food-062320-012215 · Cited by 69
Syed, Q. A., Hassan, A., Sharif, S., Ishaq, A., Saeed, F., Afzaal, M., Hussain, M., & Anjum, F. M. (2021) · International Journal of Food Properties · doi:10.1080/10942912.2021.1937209 · Cited by 62
“Milk contains various types of proteins that play a major role in milk structure.([2]) Milk comprises soluble protein casein which may be α-casein, β-casein, κ-casein and insoluble proteins which are β-lactoglobulin, α-lactalbumin, immunoglobulin and bovine serum albumin.”
BackgroundZenker, H. E., Raupbach, J., Boeren, S. A., Wichers, H. J., & Hettinga, K. A. (2020) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2020.106098 · Cited by 60
Self-citationThe application of polyphenols in food preservation
Wu, Q., & Zhou, J. (2021) · Advances in food and nutrition research · doi:10.1016/bs.afnr.2021.02.005 · Cited by 60
Milk proteins: Processing, gastric coagulation, amino acid availability and muscle protein synthesis
Horstman, A. M. H., & Huppertz, T. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2078782 · Cited by 59
“The above described product-process interactions influence coagulation behavior in the stomach and subsequent protein digestion, amino acid absorption and splanchnic sequestration after dietary protein intake, which has recently been reviewed (Van Lieshout et al. 2020).”
BackgroundImpacts of heat-induced changes on milk protein digestibility: A review
Li, S., Ye, A., & Singh, H. (2021) · International Dairy Journal · doi:10.1016/j.idairyj.2021.105160 · Cited by 60
Production of Bovine Colostrum for Human Consumption to Improve Health
Kaplan, M., Arslan, A., Duman, H., Karyelioğlu, M., Baydemir, B., Günar, B. B., Alkan, M., Bayraktar, A., Tosun, H., Ertürk, M., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.796824 · Cited by 58
“Different drying process conditions lead to various effects on protein digestion (van Lieshout et al., 2020).”
BackgroundHorstman, A. M. H., Ganzevles, R. A., Kudla, U., Kardinaal, A. F. M., van den Borne, J. J. G. C., & Huppertz, T. (2020) · International Dairy Journal · doi:10.1016/j.idairyj.2020.104890 · Cited by 57
Noriega, D. B., Zenker, H. E., Croes, C.-A., Ewaz, A., Ruinemans‐Koerts, J., Savelkoul, H. F. J., van Neerven, R. J. J., & Teodorowicz, M. (2022) · Nutrients · doi:10.3390/nu14020371 · Cited by 58
Intestinal protein uptake and IgE-mediated food allergy
Ballegaard, A. R., & Bøgh, K. L. (2022) · Food Research International · doi:10.1016/j.foodres.2022.112150 · Cited by 62
“…whereas proteolysis of the proteins starts in the stomach, where the proteins are exposed to an acidic environment with a pH of around 1.2 to 3.0, that causes the proteins to denature, rendering them more susceptible for proteolysis by the gastric protease pepsin (van Lieshout et al., 2020).”
BackgroundInfluentialImpact of Sarcopenia on Non-Alcoholic Fatty Liver Disease
Iwaki, M., Kobayashi, T., Nogami, A., Saito, S., Nakajima, A., & Yoneda, M. (2023) · Nutrients · doi:10.3390/nu15040891 · Cited by 61
Ulhas, R. S., Ravindran, R., Malaviya, A., Priyadarshini, A., Tiwari, B. K., & Rajauria, G. (2023) · Food Research International · doi:10.1016/j.foodres.2023.113479 · Cited by 59
“In Whey protein however, glycosylation may either increase or decrease di-gestibility since glycosylation in this case causes not only unfolding but also a steric hindrance and thus the two changes must be balanced to optimise digestibility (van Lieshout et al., 2020).”
Bavaro, S. L., Mamone, G., Picariello, G., Callanan, M. J., Chen, Y., Brodkorb, A., & Giblin, L. M. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.129019 · Cited by 52
Changes in the milk serum proteome after thermal and non-thermal treatment
Liu, Y., Xiong, L. H., Kontopodi, E., Boeren, S. A., Zhang, L., Zhou, P., & Hettinga, K. A. (2020) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2020.102544 · Cited by 51
Self-citationCosta, A., Sneddon, N., Goi, A., Visentin, G., Mammi, L. M. E., Savarino, E. V., Zingone, F., Formigoni, A., Penasa, M., & MARCHI, M. D. (2023) · Journal of Dairy Science · doi:10.3168/jds.2022-23013 · Cited by 52
An overview of the nutritional and therapeutic properties of amaranth
Sattar, M., Saeed, F., Afzaal, M., Rasheed, A., Asif, A., Sharif, S., Hussain, M., Rehman, H. A. U., Raza, M. A., Munir, H., et al. (2024) · International Journal of Food Properties · doi:10.1080/10942912.2024.2304266 · Cited by 47
“[19] In recent studies researchers examined the effect of cooking, popping, toasting, extruding, and milling amaranthus as well as discovered that these treatments decreased the average totals of aromatic compounds by 30% while toasting had been the only process with a substantial reduction in…”
Understanding Dietary Protein Quality: Digestible Indispensable Amino Acid Scores and Beyond
Matthews, J. J., Arentson‐Lantz, E. J., Moughan, P. J., Wolfe, R. R., Ferrando, A. A., & Church, D. D. (2025) · Journal of Nutrition · doi:10.1016/j.tjnut.2025.07.005 · Cited by 51
“Whey proteins are soluble globular proteins that do not form micelles or gels, and their compact structure allows for rapid digestion and absorption [96].”
Lambers, T. T., Broeren, S., Heck, J. M. L., Bragt, M. C. E., & Huppertz, T. (2021) · International Dairy Journal · doi:10.1016/j.idairyj.2021.105099 · Cited by 53
Self-citationKinetics of pepsin-induced hydrolysis and the coagulation of milk proteins
Yang, M., Ye, A., Yang, Z., Everett, D. W., Gilbert, E. P., & Singh, H. (2022) · Journal of Dairy Science · doi:10.3168/jds.2021-21177 · Cited by 47
Yang, M., Liu, J., Yang, X., Li, S., Li, C., Liu, B., Ma, S., Liu, X., Du, Z., Zhang, T., et al. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.129096 · Cited by 44
McClements, D. J. (2024) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.13330 · Cited by 44
Processing technologies for improved digestibility of milk proteins
Bhat, Z. F., Morton, J. D., Bekhit, A. E. A., Kumar, S., & Bhat, H. F. (2021) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2021.09.017 · Cited by 42
Whey Proteins and Bioactive Peptides: Advances in Production, Selection and Bioactivity Profiling
Luparelli, A. V., Trisciuzzi, D., Schirinzi, W. M., Caputo, L., Smiriglia, L., Quintieri, L., Nicolotti, O., & Monaci, L. (2025) · Biomedicines · doi:10.3390/biomedicines13061311 · Cited by 45
Nielsen, S. D.-H., Knudsen, L. J., Bækgaard, L. T., Rauh, V., & Larsen, L. B. (2022) · Foods · doi:10.3390/foods11070897 · Cited by 41
“Aggregate formation is an unwanted quality change in long-shelf-life dairy products [6]; however, it could also lead to further changes in the digestibility of these food proteins [28,29].”
BackgroundLund, P., Bechshøft, M. R., Ray, C., & Lund, M. N. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c05612 · Cited by 41
Characterizing the changes of bovine milk serum proteins after simulated industrial processing
Liu, Y., Zhang, W., Zhang, L., Hettinga, K. A., & Zhou, P. (2020) · LWT · doi:10.1016/j.lwt.2020.110101 · Cited by 39
Self-citationLi, S., Pan, Z., Ye, A., Cui, J. H., Dave, A., & Singh, H. (2021) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.107465 · Cited by 38
Trommelen, J., Weijzen, M. E. G., van Kranenburg, J. M. X., Ganzevles, R. A., Beelen, M., Verdijk, L. B., & van Loon, L. J. C. (2020) · Nutrients · doi:10.3390/nu12082299 · Cited by 39
Olaniyan, E. T., O’Halloran, F., & McCarthy, A. L. (2020) · Nutrition Research Reviews · doi:10.1017/s0954422420000219 · Cited by 39
“ofproteins, affectingdigestionkinetics(84).”
BackgroundInfluentialLi, S., Ye, A., Pan, Z., Cui, J. H., Dave, A., & Singh, H. (2021) · Journal of Dairy Science · doi:10.3168/jds.2021-20980 · Cited by 37
Accardo, F., Leni, G., Tedeschi, T., Prandi, B., & Sforza, S. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.132884 · Cited by 37
Nurkolis, F., Harbuwono, D. S., Taslim, N. A., Soegondo, S., Suastika, K., Sparringa, R. A., Mustika, A., Syam, A. F., Santini, A., Holly, J. M. P., et al. (2025) · Discover Food · doi:10.1007/s44187-025-00422-6 · Cited by 42
“Proteins vary significantly in their digestibility and absorption rates, which in turn influence their metabolic effects [83, 215].”
Gastrointestinal Protein Hydrolysis Kinetics: Opportunities for Further Infant Formula Improvement
Abrahamse, E., Thomassen, G. G. M., Renes, I. B., Wierenga, P. A., & Hettinga, K. A. (2022) · Nutrients · doi:10.3390/nu14071512 · Cited by 36
Self-citationDietary Advanced Glycation Endproducts and the Gastrointestinal Tract
van der Lugt, T., Opperhuizen, A., Bast, A., & Vrolijk, M. F. (2020) · Nutrients · doi:10.3390/nu12092814 · Cited by 36
“Additionally, indirect steric hindrance of the proteolytic cleavage sites can occur through binding to residues close to proteolytic cleavage sites, or it can cause cross-linking that inhibits access for proteases [26].”
BackgroundZhang, J., Lee, N. A., Duley, J. A., Cowley, D. M., Shaw, P. N., & Bansal, N. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.131545 · Cited by 34
Chen, J., Zhang, J., Wang, N., Sun, X., Han, X., Yin, R., Pei, X., Liu, C., Pang, X., Huang, F., et al. (2024) · Food Bioscience · doi:10.1016/j.fbio.2024.104012 · Cited by 33
Atallah, N., Deracinois, B., Boulier, A., Baniel, A., Bouveresse, D. J., Ravallec, R., Flahaut, C., & Cudennec, B. (2020) · Foods · doi:10.3390/foods9111580 · Cited by 32
“Processes such as heating, for example, are known to denature whey proteins, making them more digestible [6].”
BackgroundLiu, Z., Suolang, Q., Wang, J., Li, L., Luo, Z., Shang, P., Chen, X. D., & Wu, P. (2022) · Food Research International · doi:10.1016/j.foodres.2022.111958 · Cited by 32
Sumi, K., Tagawa, R., Yamazaki, K., Nakayama, K., Ichimura, T., Sanbongi, C., & Nakazato, K. (2023) · Nutrients · doi:10.3390/nu15204366 · Cited by 38
Gasparini, A., Bühler, S., Faccini, A., Sforza, S., & Tedeschi, T. (2020) · Molecules · doi:10.3390/molecules25061294 · Cited by 30
Smirnova, A., Коноплев, Г., Mukhin, N. V., Stepanova, O. S., & Steinmann, U. (2020) · Journal of Composites Science · doi:10.3390/jcs4040151 · Cited by 30
Gazi, I., Franc, V., Tamara, S., van Gool, M. P., Huppertz, T., & Heck, A. J. R. (2022) · International Dairy Journal · doi:10.1016/j.idairyj.2022.105340 · Cited by 27
Han, R., Shi, R., Yu, Z., Ho, H., Du, Q., Sun, X., Wang, J., Jiang, H., Fan, R., & Yang, Y. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.130640 · Cited by 27
Wilms, J. N., Ghaffari, M. H., Darani, P. S., Jansen, M., Sauerwein, H., Steele, M. A., Martín‐Tereso, J., & Leal, L. N. (2023) · Journal of Dairy Science · doi:10.3168/jds.2023-23368 · Cited by 26
“Denaturation of the protein fraction leads to a change in the tertiary structure of the protein and other chemical modifications that negatively affect the accessibility of AA to proteolytic enzymes, thus reducing digestibility (van Lieshout et al., 2019).”
BackgroundRusso, I., Gatta, P. A. D., GARNHAM, A. P., Porter, J. A., Burke, L. M., & Costa, R. J. S. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2020.622270 · Cited by 26
Chauvet, L., Ménard, O., Gouar, Y. L., Henry, G., Jardin, J., Hennetier, M., Croguennec, T., van Audenhaege, M., Dupont, D., Lemaire, M., et al. (2023) · Food Research International · doi:10.1016/j.foodres.2023.112883 · Cited by 25
Cross‐linking reactions in food proteins and proteomic approaches for their detection
Renzone, G., Arena, S., & Scaloni, A. (2021) · Mass Spectrometry Reviews · doi:10.1002/mas.21717 · Cited by 24
The Use of Membrane Filtration to Increase Native Whey Proteins in Infant Formula
Chen, Y., Callanan, M. J., Shanahan, C., Tobin, J. T., Gamon, L. F., Davies, M. J., Giblin, L. M., & Brodkorb, A. (2021) · Dairy · doi:10.3390/dairy2040041 · Cited by 23
Teodorowicz, M., Zenker, H. E., Ewaz, A., Tsallis, T., Mauser, A., Gensberger‐Reigl, S., de Jong, N. W., Hettinga, K. A., Wichers, H. J., van Neerven, R. J. J., et al. (2021) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202000834 · Cited by 21
Self-citationZhong, W., Li, J., Dai, J., Wang, C., & Zhang, T. (2021) · Food Bioscience · doi:10.1016/j.fbio.2021.101109 · Cited by 22
Sun, J., Akıllıoğlu, H. G., Aasmul‐Olsen, K., Ye, Y., Lund, P., Zhao, X., Brunse, A., Nielsen, C. F., Chatterton, D. E. W., Sangild, P. T., et al. (2022) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202200132 · Cited by 19
Milan, A. M., Samuelsson, L. M., Shrestha, A., Sharma, P., Day, L., & Cameron‐Smith, D. (2020) · Frontiers in Nutrition · doi:10.3389/fnut.2020.553674 · Cited by 20
Miltenburg, J., Bastiaan‐Net, S., Hoppenbrouwers, T., Wichers, H. J., & Hettinga, K. A. (2023) · Food Chemistry · doi:10.1016/j.foodchem.2023.137209 · Cited by 19
Self-citationFinnegan, E. W., Goulding, D., O’Callaghan, T. F., & O’Mahony, J. A. (2024) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.13289 · Cited by 19
Gharbi, N., Marciniak, A., & Doyen, A. (2022) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.13012 · Cited by 18
Heating affects protein digestion of skimmed goat milk under simulated infant conditions
Ren, Q., Boiani, M., He, T., Wichers, H. J., & Hettinga, K. A. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.134261 · Cited by 18
Self-citationSun, Y., Wang, R., Li, Q., & Ma, Y. (2023) · Journal of Dairy Science · doi:10.3168/jds.2022-22602 · Cited by 18
Ataallahi, M., Cheon, S. N., Park, G.-W., Nugrahaeningtyas, E., Jeon, J.-H., & Park, K.-H. (2023) · Animals · doi:10.3390/ani13152407 · Cited by 18
Patil, N. D., Thakur, S., Bains, A., Kaur, S., Ali, N., Arora, R., Parvez, M. K., Gökşen, G., Janghu, S., & Chawla, P. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.140401 · Cited by 18
Lund, P., Nielsen, S. B., Nielsen, C. F., Ray, C., & Lund, M. N. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.129145 · Cited by 18
Fatih, M., Barnett, M. P. G., Gillies, N. A., & Milan, A. M. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.643350 · Cited by 17
Aguilera-Toro, M., Poulsen, N. A., Akkerman, M., Rauh, V., Larsen, L. B., & Nielsen, S. D.-H. (2022) · Foods · doi:10.3390/foods11101525 · Cited by 16
“However, in this study it was found that milk sediment was associated with late-stage Maillard reaction, which is known to be related to cross-linking [7,8].”
BackgroundLiu, Y., Hettinga, K. A., Liu, D., Zhang, L., & Zhou, P. (2022) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.13019 · Cited by 17
Self-citationHuang, Z., Jiang, Y., Li, H., Li, Q., Gao, Z., Zhang, Y., Zhang, Q., & Fu, L. (2023) · Food Research International · doi:10.1016/j.foodres.2023.112842 · Cited by 18
MRI assessment of pH and coagulation during semi-dynamic in vitro gastric digestion of milk proteins
Mayar, M., de Vries, M., Smeets, P. A. M., van Duynhoven, J., & Terenzi, C. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.109866 · Cited by 16
Cavalcanti, N. S. D. H., Pimentel, T. C., Magnani, M., Pacheco, M. T. B., Alves, S. P., Bessa, R. J. B., Sant’Ana, A. M. D. S., & Queiroga, R. D. C. R. D. E. (2021) · LWT · doi:10.1016/j.lwt.2021.111239 · Cited by 16
Chen, S., Zhao, T., Jiao, W., Zhang, Y., Liu, W., Zhang, Y., Huang, L., & Lv, S. (2022) · LWT · doi:10.1016/j.lwt.2022.114141 · Cited by 15
Zioud, A., Hajji, W., Lobón, S., Joy, M., Bertolín, J. R., Smeti, S., Chabbouh, M., Bellagha, S., & Essid, I. (2023) · Foods · doi:10.3390/foods12203837 · Cited by 15
Ren, Q., Boiani, M., He, T., Wichers, H. J., & Hettinga, K. A. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.109452 · Cited by 15
Self-citationNavis, M., Schwebel, L., Kappel, S. S., Muncan, V., Sangild, P. T., Abrahamse, E., Aunsholt, L., Thymann, T., van Elburg, R. M., & Renes, I. B. (2020) · Nutrients · doi:10.3390/nu12113391 · Cited by 15
“For example, proteins in bovine milk can form aggregates upon heating, which can result in lower protein bioavailability and delayed gastric emptying [14].”
BackgroundInfluentialChun, S., & Lee, K. (2021) · Journal of Dairy Science · doi:10.3168/jds.2021-20681 · Cited by 16
Taher, A. Y., Alizadeh, M., & Aslan, Y. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e32223 · Cited by 14
“This process enhances the digestion and better absorption of proteins in the body [8].”
BackgroundRecent developments in in-vitro assessment of advanced glycation end products
Serin, Y., Akbulut, G., Uğur, H., & Yaman, M. (2021) · Current Opinion in Food Science · doi:10.1016/j.cofs.2021.03.011 · Cited by 14
Ryu, S., Shin, M., Yun, B., Lee, W. J., Choi, H., Kang, M., Oh, S., & Kim, Y. (2021) · Animals · doi:10.3390/ani11051306 · Cited by 13
In vitro 1H MT and CEST MRI mapping of gastro-intestinal milk protein breakdown
Mayar, M., Smeets, P. A. M., van Duynhoven, J., & Terenzi, C. (2023) · Food Structure · doi:10.1016/j.foostr.2023.100314 · Cited by 13
Lee, E.-B., & Shin, W. (2023) · LWT · doi:10.1016/j.lwt.2023.115133 · Cited by 13
Gasparini, A., van Gool, M. P., Bultsma, M., Cutroneo, S., Sforza, S., & Tedeschi, T. (2020) · International Dairy Journal · doi:10.1016/j.idairyj.2020.104765 · Cited by 13
Zhang, Q., Jiang, Y., Li, H., Gao, Z., Yu, G., Xie, H., Wang, Y., & Fu, L. (2023) · Food & Function · doi:10.1039/d2fo03000d · Cited by 12
Maryniak, N. Z., Sancho, A. I., Nielsen, S. D.-H., Larsen, L. B., Gao, Y., Bøgh, K. L., & Hansen, E. B. (2023) · LWT · doi:10.1016/j.lwt.2023.115591 · Cited by 12
Lian, J.-W., Yang, K., Chen, J., & Zhu, Y. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.111695 · Cited by 12
The self-association properties of partially dephosphorylated bovine beta-casein
Song, S., Lin, Y., Zhang, Y., Luo, Y., & Guo, H. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.108019 · Cited by 12
Metadata
- Authors
- van Lieshout, G. A. A., Lambers, T. T., Bragt, M. C. E., & Hettinga, K. A.
- Affiliations
- FrieslandCampina, Amersfoort, the Netherlands
- FrieslandCampina (Netherlands) (NL)
- Wageningen University & Research (NL)
- Corresponding author
- Hettinga, Kasper A.
- Venue
- Critical Reviews in Food Science and Nutrition
- Publisher
- Informa UK Limited
- Published
- 2019-08-22
- Volume
- 60
- Issue
- 14
- Pages
- 2422-2445
- ISSN
- 1040-8398 (ISSN-L)
- 1549-7852
- OpenAlex
- W2969873245
- Cited by
- 254
- References
- 127
- Citations by year
- 2026: 30 · 2025: 40 · 2024: 34 · 2023: 48 · 2022: 41 · 2021: 36 · 2020: 24 · 2019: 1
- FWCI
- 2.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Critical Reviews in Food Science and Nutrition (publishedVersion, cc-by-nc-nd)
- PubMed (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 › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
- Life Sciences › Agricultural and Biological Sciences › Food Science › Food Nutrient Composition and Product Development
- Keywords
- milk protein digestion, dairy processing, heat treatment (food and biological processing), protein denaturation, glycation, amino acid bioavailability, lysine, protein oxidation, protein cross-linking, β-lactoglobulin, gastric emptying, protein quality
- MeSH terms
- Amino Acids, Animals, Digestion, Hot Temperature, Heating, Humans, Milk, Milk Proteins, Protein Denaturation, Pasteurization
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review