How processing may affect milk protein digestion and overall physiological outcomes: A systematic review

van Lieshout, Glenn A. A.; Lambers, Tim T.; Bragt, Marjolijn C. E.; Hettinga, Kasper A.

doi:10.1080/10408398.2019.1646703

Cited by 254Proteins in Food SystemsProtein Hydrolysis and Bioactive PeptidesFood and Agricultural Sciences

How processing may affect milk protein digestion and overall physiological outcomes: A systematic review

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van Lieshout, Glenn A. A., Lambers, Tim T., Bragt, Marjolijn C. E., Hettinga, Kasper A.·2020·Critical Reviews in Food Science and Nutrition

DOI 10.1080/10408398.2019.1646703

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Abstract

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.

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The decline in pH 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.
“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
The Physiological consequences section (page unavailable) says that protein fermentation in the lower gastrointestinal tract can produce ammonia, lending limited support to one proposed mechanism. It does not link that process to a rise in dairy-product pH, or address the d 0–20 decline, residual lactose conversion to lactic acid, or the d 20–30 rise. (LLM, conf=0.75)
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BackgroundMethodInfluential
Structural mechanism and kinetics of in vitro gastric digestion are affected by process-induced changes in bovine milk
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BackgroundMethodInfluential
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Method
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Background
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Background
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Background
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BackgroundMethodInfluential
Digestibility of protein and amino acids in selected foods as determined by a rat balance method
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Background
Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder
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BackgroundMethodInfluential
Ultra High Temperature Treatment, but Not Pasteurization, Affects the Postprandial Kinetics of Milk Proteins in Humans
Lacroix, M., Bon, C., Bos, C., Léonil, J., Benamouzig, R., Luengo, C., Fauquant, J., Tomé, D., & Gaudichon, C. (2008) · Journal of Nutrition · doi:10.3945/jn.108.096990 · Cited by 78 · see citing works
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Background
Characterization and in Vitro Digestibility of Bovine β-Lactoglobulin Glycated with Galactooligosaccharides
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“In a milk matrix, several in vitro studies show that, comparable to the gastric hydrolysis results, heating of liquid milk results in (small) increases of protein hydrolysis by pancreatic enzymes (Carbonaro et al. 1997; Rinaldi et al. 2015).”
Result
Effect of Maillard induced glycation on protein hydrolysis by lysine/arginine and non-lysine/arginine specific proteases
Deng, Y., Wierenga, P. A., Schols, H. A., Sforza, S., & Gruppen, H. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2017.02.007 · Cited by 72 · cited 1× · see citing works
“Although progress has been made to establish a more quantitative relation between glycation and digestion (Deng et al. 2017), a harmonized in vitro digestion procedure would also allow to assess better the quantitative relation between processing-induced protein modifications and digestion among…”
Background
Dairy products and bone health: how strong is the scientific evidence?
van den Heuvel, E. G. H. M., & Steijns, J. M. (2018) · Nutrition Research Reviews · doi:10.1017/s095442241800001x · Cited by 70 · see citing works
Whey Protein Processing Influences Formula-Induced Gut Maturation in Preterm Pigs
Li, Y., Østergaard, M. V., Pingping, J., Chatterton, D. E. W., Thymann, T., Kvistgaard, A. S., & Sangild, P. T. (2013) · Journal of Nutrition · doi:10.3945/jn.113.182931 · Cited by 63 · see citing works
Antioxidant activity of bovine alpha lactalbumin Maillard products and evaluation of their in vitro gastro-duodenal digestive proteolysis
Joubran, Y., Moscovici, A., & Lesmes, U. (2015) · Food & Function · doi:10.1039/c4fo01165a · Cited by 62 · cited 1× · see citing works
“This was seen for WPI and a-lactalbumin (Cattaneo et al. 2017; Hiller and Lorenzen 2010; Joubran, Moscovici, and Lesmes 2015).”
Background
Effect of heat treatment and enzymatic digestion on the B cell epitopes of cow's milk proteins
Morisawa, Y., Kitamura, A., Ujihara, T., Zushi, N., Kuzume, K., Shimanouchi, Y., TAMURA, S., Wakiguchi, H., Saito, H., & Matsumoto, K. (2009) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2009.03203.x · Cited by 57 · cited 1× · see citing works
“These results are more or less in line with results using human derived basophils and sera from cows milk allergic patients (Morisawa et al. 2009).”
Result
Heat Treatment of Milk During Powder Manufacture Increases Casein Resistance to Simulated Infant Digestion
Dupont, D., Boutrou, R., Ménard, O., Jardin, J., Tanguy, G., Schuck, P., Haab, B. B., & Léonil, J. (2010) · Food Digestion · doi:10.1007/s13228-010-0003-0 · Cited by 57 · see citing works
Effects of Industrial Heating Processes of Milk-Based Enteral Formulas on Site-Specific Protein Modifications and Their Relationship to in Vitro and in Vivo Protein Digestibility
Wada, Y., & Lönnerdal, B. (2015) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5b02189 · Cited by 57 · see citing works
Influence of dairy matrices on nutrient release in a simulated gastrointestinal environment.
Lamothe, S., Rémillard, N., Tremblay, J., & Britten, M. (2017) · Food Research International · doi:10.1016/j.foodres.2016.12.026 · Cited by 57 · see citing works
Cross-Linking of β-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing
Stojadinović, M., Pieters, R. H. H., Smit, J. J., & Veličković, T. Ć. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu062 · Cited by 54 · see citing works
Implications of the Maillard reaction on bovine alpha-lactalbumin and its proteolysis during in vitro infant digestion
Joubran, Y., Moscovici, A., Portmann, R., & Lesmes, U. (2017) · Food & Function · doi:10.1039/c7fo00588a · Cited by 54 · see citing works
Heat Markers and Quality Indexes of Industrially Heat-Treated [15N] Milk Protein Measured in Rats
Lacroix, M., Léonil, J., Bos, C., Henry, G., Airinei, G., Fauquant, J., Tomé, D., & Gaudichon, C. (2006) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf051304d · Cited by 50 · cited 4× · see citing works
“Post absorption, nitrogen metabolism may be affected by processing-induced protein modifications and result in a larger splanchnic extraction, as demonstrated in rats fed differentially processed milk protein preparations (Lacroix et al. 2006).”
BackgroundMethodInfluential
Protein-Bound D-Amino Acids, and to a Lesser Extent Lysinoalanine, Decrease True Ileal Protein Digestibility in Minipigs as Determined with 15N-Labeling
de Vrese, M., Frik, R., Roos, N., & Hagemeister, H. (2000) · Journal of Nutrition · doi:10.1093/jn/130.8.2026 · Cited by 49 · cited 3× · see citing works
“This may affect other amino acids in the peptides as well, resulting in a decreased ileal protein digestibility (de Vrese et al. 2000).”
Background
Application of a New Method for Determining Digestible Reactive Lysine to Variably Heated Protein Sources
Rutherfurd, S. M., & Moughan, P. J. (1997) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf960788y · Cited by 48 · see citing works
Absorption of Lysine and Deoxyketosyllysine in an Early-Maillard Browned Casein by the Growing Pig
Moughan, P. J., Gall, M. P. J., & Rutherfurd, S. M. (1996) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf950428v · Cited by 46 · cited 1× · see citing works
“…it is of major importance to distinguish between total and reactive lysine levels as standard methodology may not always distinguish between both, leading to an overestimated lysine content that could result in an underestimated lysine digestibility coefficient (Moughan and Rutherfurd 1996).”
Background
Protein breakdown and release of β-casomorphins during in vitro gastro-intestinal digestion of sterilised model systems of liquid infant formula
Cattaneo, S., Stuknytė, M., Masotti, F., & Noni, I. D. (2016) · Food Chemistry · doi:10.1016/j.foodchem.2016.08.128 · Cited by 46 · cited 3× · see citing works
“However, an in vitro infant digestion of infant formula model systems suggested that different protein crosslinking as assessed by LAL content did not change protein hydrolysis (Cattaneo et al. 2017).”
Background
Assessing the effects of severe heat treatment of milk on calcium bioavailability: In vitro and in vivo studies
Seiquer, I., Delgado‐Andrade, C., Haro, A., & Navarro, M. P. (2010) · Journal of Dairy Science · doi:10.3168/jds.2010-3469 · Cited by 45 · cited 1× · see citing works
“In a more recent study from the same authors, UHT milk was compared with overheated milk (3 severe sterilization heatings, 16minutes at 116 C) both in vitro and in vivo (Seiquer et al. 2010).”
Background
In Vitro Digestion of Proteins in Human Milk Fortifiers and in Preterm Formula
Lindberg, T., Engberg, S., Sjöberg, L. B., & Lönnerdal, B. L. (1998) · Journal of Pediatric Gastroenterology and Nutrition · doi:10.1097/00005176-199807000-00006 · Cited by 45 · cited 3× · see citing works
“(Lindberg et al. 1998) In vitro static digestion with duodenal juice from adults WPCs WPC freeze-dried: 0% denaturation WPC spray-dried: 26% denaturation WPC heated 80 C 15 sec, freeze-dried: 55% denaturation WPC heated 80 C 30min, freeze-dried: 97% denaturation Digestion via polyacramide gradient…”
BackgroundMethod
Release of pyrraline in absorbable peptides during simulated digestion of casein glycated by 3-deoxyglucosone
Hellwig, M., & Henle, T. (2013) · European Food Research and Technology · doi:10.1007/s00217-013-2027-5 · Cited by 43 · see citing works
Digestibility and antigenicity of β-lactoglobulin as affected by heat, pH and applied shear
Rahaman, T., Vasiljevic, T., & Ramchandran, L. (2016) · Food Chemistry · doi:10.1016/j.foodchem.2016.08.129 · Cited by 42 · see citing works
Differences in protein digestibility and quality of liquid concentrate and powder forms of milk-based infant formulas fed to rats
Sarwar, G., Peace, R. W., & Botting, H. G. (1989) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/49.5.806 · Cited by 41 · cited 1× · see citing works
“For example, protein digestibility of powdered infant formula was significantly higher than liquid concentrates of the same manufacturer in a rat balance study (Sarwar, Peace, and Botting 1989).”
Background
Aspects of physical and chemical alterations to proteins during food processing – some implications for nutrition
Gerrard, J. A., Lassé, M., Cottam, J. R. A., Healy, J. P., Fayle, S. E., Rasiah, I. A., Brown, P. K., BinYasir, S. M., Sutton, K. H., & Larsen, N. G. (2012) · British Journal Of Nutrition · doi:10.1017/s000711451200236x · Cited by 40 · see citing works
Estimation of lysine damage in heated whey proteins by furosine determinations in conjunction with the digestion cell technique
Desrosiers, T., Savoie, L., Bergeron, G., & Parent, G. (1989) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00089a039 · Cited by 39 · see citing works
Effect of heat denaturation on beta-lactoglobulin-induced gastrointestinal sensitization in rats: Denatured βLG induces a more intensive local immunologic response than native βLG
Rytkönen, J., Karttunen, T. J., Karttunen, R. A., Valkonen, K. H., Jenmalm, M. C., Alatossava, T., Björkstén, B., & Kokkonen, J. (2002) · Pediatric Allergy and Immunology · doi:10.1034/j.1399-3038.2002.01028.x · Cited by 39 · see citing works
PROTEIN QUALITY IN COMMERCIAL MILK‐BASED INFANT FORMULAS
POMPEI, C., Rossi, M., & MARÈ, F. (1988) · Journal of Food Quality · doi:10.1111/j.1745-4557.1988.tb00298.x · Cited by 38 · cited 1× · see citing works
“In another study, in vitro digestion of different infant formulas showed no direct correlation between digestibility and LAL content, lysine blockage, or HMF content (Pompei, Rossi, and Mare 1988).”
Background
Specific effects of denaturation, hydrolysis and exposure to Lactococcus lactis on bovine β‐lactoglobulin transepithelial transport, antigenicity and allergenicity
Bernasconi, E., Fritsché, R., & Corthésy, B. (2006) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2006.02504.x · Cited by 37 · cited 1× · see citing works
“Epithelial degradation and transport of heating induced modified b-lactoglobulin may be affected, as demonstrated by in vitro studies using different intestinal epithelial cell-models (Bernasconi, Fritsch e, and Corth esy 2006; Rytk€onen et al. 2006).”
Background
Influence of Diets Rich in Maillard Reaction Products on Calcium Bioavailability. Assays in Male Adolescents and in Caco-2 Cells
Mesías, M., Seiquer, I., & Navarro, M. P. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf9018646 · Cited by 35 · see citing works
Short-term effects of dietary advanced glycation end products in rats
Poulsen, M. W., Andersen, J. M., Hedegaard, R. V., Madsen, A. N., Krath, B. N., Monošík, R., Bak, M. J., Nielsen, J., Holst, B., Skibsted, L. H., et al. (2015) · British Journal Of Nutrition · doi:10.1017/s0007114515004833 · Cited by 35 · see citing works
Generation of Soluble Advanced Glycation End Products Receptor (sRAGE)-Binding Ligands during Extensive Heat Treatment of Whey Protein/Lactose Mixtures Is Dependent on Glycation and Aggregation
Liu, F., Teodorowicz, M., Wichers, H. J., van Boekel, M. A. J. S., & Hettinga, K. A. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6b02674 · Cited by 35 · see citing works
Self-citation
Does processing of a powder or in-bottle-sterilized liquid infant formula affect calcium bioavailability?
Sarriá, B., López‐Fandiño, R., & Vaquero, M. P. (2001) · Nutrition · doi:10.1016/s0899-9007(00)00585-2 · Cited by 34 · see citing works
Spray Dried, Pasteurised Bovine Colostrum Protects Against Gut Dysfunction and Inflammation in Preterm Pigs
Støy, A. C. F., Sangild, P. T., Skovgaard, K., Thymann, T., Bjerre, M., Chatterton, D. E. W., Purup, S., Boyé, M., & Heegaard, P. M. H. (2015) · Journal of Pediatric Gastroenterology and Nutrition · doi:10.1097/mpg.0000000000001056 · Cited by 34 · see citing works
Enterocyte and M-Cell Transport of Native and Heat-Denatured Bovine β-Lactoglobulin: Significance of Heat Denaturation
Rytkönen, J., Valkonen, K. H., Virtanen, V. T., Foxwell, R., Kyd, J. M., Cripps, A. W., & Karttunen, T. J. (2006) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf052309d · Cited by 33 · see citing works
Disulfide Reactivity and In Vitro Protein Digestibility of Different Thermal-Treated Milk Samples and Whey Proteins
Carbonaro, M., Cappelloni, M., Sabbadini, S., & Carnovale, E. (1997) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf950828i · Cited by 31 · cited 5× · see citing works
“…al. (1998) showed that severe heating of whey protein extracts or WPC above a critical temperature ( 75 C) decreased overall digestibility of its proteins, probably due to formation of more compact whey proteins and aggregates (Carbonaro et al. 1997; Lindberg et al. 1998; Wada and L€onnerdal 2014).”
BackgroundResultInfluential
Effects of Heat Treatment of Casein in the Presence of Reducing Sugars on Calcium Bioavailability: in Vitro and in Vivo Assays
Seiquer, I., Aspe, T., Vaquero, M. P., & Navarro, P. (2001) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf001008v · Cited by 29 · cited 1× · see citing works
“In vitro experiments using heated casein-glucosefructose solutions revealed that calcium solubility was lowered which resulted in a decreased in vitro absorption of calcium (Seiquer et al. 2001).”
Background
Bioactive Whey Protein Concentrate and Lactose Stimulate Gut Function in Formula‐fed Preterm Pigs
Li, Y., Nguyen, D. N., Obelitz‐Ryom, K., Andersen, A. D., Thymann, T., Chatterton, D. E. W., Purup, S., Heckmann, A. B., Bering, S. B., & Sangild, P. T. (2017) · Journal of Pediatric Gastroenterology and Nutrition · doi:10.1097/mpg.0000000000001699 · Cited by 29 · cited 4× · see citing works
“Immaturity of the gut predisposes these animals to gut complications and milk protein preparations (particular sow milk or minimally processed bovine milk protein preparations and colostrum) have been demonstrated to reduce the risk for such complications (Li, Ostergaard, et al. 2013; Li et al. 2018; Støy et al. 2016).”
BackgroundInfluential
Quantity and carbohydrate content of glycomacropeptide fractions isolated from raw and heat-treated milk
Taylor, C. M., & Woonton, B. W. (2009) · International Dairy Journal · doi:10.1016/j.idairyj.2009.06.010 · Cited by 28 · see citing works
Effect of Oxidation of Dietary Proteins with Performic Acid on True Ileal Amino Acid Digestibility As Determined in the Growing Rat
Rutherfurd, S. M., Montoya, C. A., & Moughan, P. J. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf403146u · Cited by 28 · cited 2× · see citing works
“To date, several studies applying different experimental oxidation strategies have demonstrated effects of oxidation on digestibility and protein quality (Chang and Zhao 2012; Feng et al. 2015; Rutherfurd, Montoya, and Moughan 2014).”
BackgroundMethod
Isoenergic modification of whey protein structure by denaturation and crosslinking using transglutaminase
Stender, E. G. P., Koutina, G., Almdal, K., Hassenkam, T., Mackie, A. R., Ipsen, R., & Svensson, B. (2018) · Food & Function · doi:10.1039/c7fo01451a · Cited by 28 · see citing works
Upregulation of oxidative stress markers in human microvascular endothelial cells by complexes of serum albumin and digestion products of glycated casein
Deo, P., Glenn, J. V., Powell, L. A., Stitt, A. W., & Ames, J. M. (2009) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.20301 · Cited by 25 · cited 1× · see citing works
“In an in vitro setting, Deo et al. (2009) demonstrated that digested dietary AGE, as prepared by dry-heating casein and glucose, complexed with serum albumin, may regulate expression of RAGE (receptor for AGE) and downstream inflammatory pathways.”
Background
In vitro Digestibility of Whey Protein/ K ‐Casein Complexes Isolated from Heated Concentrated Milk
Singh, H., & Creamer, L. K. (1993) · Journal of Food Science · doi:10.1111/j.1365-2621.1993.tb04260.x · Cited by 24 · see citing works
Effect of heat treatment on the nutritional quality of milk proteins
Efigênia, M., Povoa, B., & Moraes-Santos, T. (1997) · International Dairy Journal · doi:10.1016/s0958-6946(97)00049-6 · Cited by 24 · cited 2× · see citing works
“…score Heat treatment increased plasma IAA bioavailability; made b-lactoglobulin more susceptible for hydrolysis; increased stomach retention time (Efigenia, Povoa, and Moraes-Santos 1997) In vivo digestion in Weanler Holtzman male rats Whole milk Raw milk Pasteurized milk (72 C for 15 sec)…”
BackgroundMethod
Revision: Indicadores del deterioro de la calidad proteica y del valor nutritivo de la leche / Review: Indicators of damage of protein quality and nutritional value of milk
Ferrer, E., Alegrı́a, A., FARRÉ, R., Abellán, P., & Romero, F. (1999) · Food Science and Technology International · doi:10.1177/108201329900500602 · Cited by 23 · see citing works
Processing of whey modulates proliferative and immune functions in intestinal epithelial cells
Nguyen, D. N., Sangild, P. T., Li, Y., Bering, S. B., & Chatterton, D. E. W. (2015) · Journal of Dairy Science · doi:10.3168/jds.2015-9965 · Cited by 22 · cited 1× · see citing works
“Further in vitro work by the same group demonstrates that, at least in part, these observations could be explained by direct effects of the preparations on intestinal epithelial cells (Nguyen et al. 2016).”
Background
The effect of various heat treatments on the antioxidant capacity of milk before and after simulated gastrointestinal digestion
Aloğlu, H. Ş. (2012) · International Journal of Dairy Technology · doi:10.1111/1471-0307.12021 · Cited by 21 · see citing works
Digestibility of Modified Milk Proteins: Nutritional Implications
Swaisgood, H. E., & Catignani, G. L. (1985) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(85)81166-8 · Cited by 20 · see citing works
Extent of damage to amino acid availability of whey protein heated with sugar
Desrosiers, T., & Savoie, L. (1991) · Journal of Dairy Research · doi:10.1017/s002202990003003x · Cited by 20 · see citing works
In vitro digestibility and rheological properties of caseinates treated by an oxidative system containing horseradish peroxidase, glucose oxidase and glucose
Chang, C., & Zhao, X. (2012) · International Dairy Journal · doi:10.1016/j.idairyj.2012.07.004 · Cited by 19 · see citing works
Protein nutritive utilization in rats fed powder and liquid infant formulas / Utilización nutritiva de la proteína en ratas alimentadas con formulas infantiles en polvo y líquidas
Sarriá, B., López‐Fandiño, R., & Vaquero, M. P. (2000) · Food Science and Technology International · doi:10.1177/108201320000600102 · Cited by 19 · see citing works
Changes in the Digestibility of Dried Casein and Glucose Mixtures Occurring During Storage at Different Temperatures and Water Activities
Culver, C. A., & Swaisgood, H. E. (1989) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(89)79442-x · Cited by 19 · see citing works
Characterization of caseinomacropeptides released from renneted raw and UHT treated milks
Ferron-Baumy, C., Mollé, D., Garric, G., & Maubois, J. (1992) · Le Lait · doi:10.1051/lait:1992211 · Cited by 19 · see citing works
Trends in infant formulas: a dairy perspective
Floris, R., Lambers, T. T., Alting, A. C., & Kiers, J. L. (2010) · Elsevier eBooks · doi:10.1533/9781845699437.3.454 · Cited by 18 · see citing works
Self-citation
Effect of glycation of bovine β-lactoglobulin with galactooligosaccharides on the growth of human faecal bacteria
Hernández‐Hernández, O., Moreno, F. J., Kolida, S., Rastall, R. A., & Sanz, M. L. (2011) · International Dairy Journal · doi:10.1016/j.idairyj.2011.06.002 · Cited by 18 · cited 2× · see citing works
“Hernandez-Hernandez et al. (2011) demonstrated that b-lactoglobulin conjugated with GOS showed similar fecal fermentation effects as purified GOS.”
Background
Dietary protein precipitation properties have effects on gastric emptying in healthy volunteers
Fox, M. R., Georgi, G., Boehm, G., Menne, D., Fried, M., & Thumshirn, M. (2003) · Clinical Nutrition · doi:10.1016/j.clnu.2003.10.013 · Cited by 18 · see citing works
Digestive diversity and kinetic intrigue among heated and unheated β-lactoglobulin species
Loveday, S. M., Peram, M. R., Singh, H., Ye, A., & Jameson, G. B. (2014) · Food & Function · doi:10.1039/c4fo00362d · Cited by 17 · cited 3× · see citing works
“Above a critical temperature (approximately 75 C) irreversible conformational changes occur as a result of initiated aggregation processes (Loveday et al. 2014).”
BackgroundMethod
Differential influence of the degree of processing on immunogenicity following proteolysis of casein and β-lactoglobulin
Sletten, G. B. G., Holden, L., Egaas, E., & Fæste, C. K. (2008) · Food and Agricultural Immunology · doi:10.1080/09540100802350963 · Cited by 15 · see citing works
Balance Experiments on Human Volunteers with ε-Fructoselysine (FL) and Lysinoalanine (LAL)
Lee, K., & Erbersdobler, H. F. (2005) · Elsevier eBooks · doi:10.1533/9781845698393.4.358 · Cited by 14 · see citing works
Effect of Maillard reaction conditions on antigenicity of β-lactoglobulin and the properties of glycated whey protein during simulated gastric digestion
Li, Z., Luo, Y., Feng, L., & Liao, P. (2012) · Food and Agricultural Immunology · doi:10.1080/09540105.2012.712951 · Cited by 14 · see citing works
Effect of Elevated Temperature Storage on the Digestible Reactive Lysine Content of Unhydrolyzed- and Hydrolyzed-Lactose Milk-Based Products
Rutherfurd, S. M., & Moughan, P. J. (2008) · Journal of Dairy Science · doi:10.3168/jds.2007-0612 · Cited by 14 · cited 1× · see citing works
“Most research on storage-induced changes in protein modification has been done on dried dairy products and to a lesser extent sterilized products (Erbersdobler 1989; Ferrer et al. 1999; Mehta and Deeth 2016; Rutherfurd and Moughan 2008).”
Background
Prior lactose glycation of caseinate via the Maillard reaction affects in vitro activities of the pepsin-trypsin digest toward intestinal epithelial cells
Wang, X. P., & Zhao, X. (2017) · Journal of Dairy Science · doi:10.3168/jds.2016-12491 · Cited by 11 · see citing works
An evaluation of skim milk powders subjected to different heating conditions during processing as dietary protein sources for the young pig
Moughan, P. J., Wilson, M. N., Smits, C. H. M., & Smith, W. C. (1989) · Animal Feed Science and Technology · doi:10.1016/0377-8401(89)90062-x · Cited by 7 · see citing works
Nutrition and Health | Effects of Processing on Protein Quality of Milk and Milk Products
Pellegrino, L., Cattaneo, S., & Noni, I. D. (2011) · Encyclopedia of Dairy Sciences · doi:10.1016/b978-0-12-374407-4.00383-6 · Cited by 6 · see citing works
ORIGINAL ARTICLE: Bioavailability of lysine for kittens in overheated casein is underestimated by the rat growth assay method*,†
Larsen, J. A., Fascetti, A. J., Calvert, C. C., & Rogers, Q. R. (2010) · Journal of Animal Physiology and Animal Nutrition · doi:10.1111/j.1439-0396.2010.00988.x · Cited by 6 · see citing works
Portal absorption of 45Ca from labelled milk, yoghurt or heat treated yoghurt in the growing pig
Mpassi, D., Rychen, G., Mertès, P., & Laurent, F. (2001) · International Dairy Journal · doi:10.1016/s0958-6946(01)00107-8 · Cited by 2 · cited 3× · see citing works
“When comparing milk, yoghurt, and heated yoghurt, overall nitrogen absorption determined by portal labeled nitrogen absorption was similar in growing pigs (Mpassi et al. 2001).”
BackgroundInfluential
Solubility and digestibility of milk proteins in different forms of infant formulas
Liusuwan, R. A., & Lönnerdal, B. L. (1996) · The FASEB Journal · Cited by 1 · see citing works

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Sarriá, B., R. López-Fandiño, and M. P. Vaquero. 2000. Protein nutritive utilization in rats fed powder and liquid infant formulas.. Food Science and Technology International 9 (1):9–16.

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Adhikari, S., Schop, M., de Boer, I. J. M., & Huppertz, T. (2022) · Nutrients · doi:10.3390/nu14050947 · Cited by 250 · see citing works
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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 · see citing works
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“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…”
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Bielecka, M. M., Cichosz, G., & Czeczot, H. (2021) · International Dairy Journal · doi:10.1016/j.idairyj.2021.105208 · Cited by 132 · see citing works
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 · see citing works
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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 · see citing works
“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).”
Background
Integration of environment and nutrition in life cycle assessment of food Items: opportunities and challenges
McLaren, 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 98 · see citing works
Alternatives to Cow’s Milk-Based Infant Formulas in the Prevention and Management of Cow’s Milk Allergy
Maryniak, N. Z., Sancho, A. I., Hansen, E. B., & Bøgh, K. L. (2022) · Foods · doi:10.3390/foods11070926 · Cited by 89 · see citing works
Gastric colloidal behaviour of milk protein as a tool for manipulating nutrient digestion in dairy products and protein emulsions
Ye, A. (2021) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.106599 · Cited by 75 · see citing works
Lysine blockage of milk proteins in infant formula impairs overall protein digestibility and peptide release
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 · see citing works
Self-citation
Thermal 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 · see citing works
Spot test for fast determination of hydrogen peroxide as a milk adulterant by smartphone-based digital image colorimetry
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 · see citing works
Structural properties of food proteins underlying stability or susceptibility to human gastrointestinal digestion
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 · see citing works
Milk Processing Affects Structure, Bioavailability and Immunogenicity of β-lactoglobulin
Broersen, K. (2020) · Foods · doi:10.3390/foods9070874 · Cited by 66 · see citing works
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 · see citing works
“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).”
Gastrointestinal digestion of dietary advanced glycation endproducts using an in vitro model of the gastrointestinal tract (TIM-1)
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 · see citing works
Adverse Effects of Thermal Food Processing on the Structural, Nutritional, and Biological Properties of Proteins
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 · see citing works
Structural and functional properties of milk proteins as affected by heating, high pressure, Gamma and ultraviolet irradiation: a review
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 · see citing works
“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.”
Background
The effect of low vs. high temperature dry heating on solubility and digestibility of cow's milk protein
Zenker, 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 · see citing works
Self-citation
The 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 · see citing works
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 · see citing works
“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).”
Background
Impacts 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 58 · see citing works
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 · see citing works
“Different drying process conditions lead to various effects on protein digestion (van Lieshout et al., 2020).”
Background
Postprandial blood amino acid concentrations in older adults after consumption of dairy products: The role of the dairy matrix
Horstman, 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 · see citing works
Receptor Mediated Effects of Advanced Glycation End Products (AGEs) on Innate and Adaptative Immunity: Relevance for Food Allergy
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 · see citing works
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 56 · see citing works
“…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).”
BackgroundInfluential
Impact 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 60 · see citing works
A review of alternative proteins for vegan diets: Sources, physico-chemical properties, nutritional equivalency, and consumer acceptance
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 · see citing works
“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).”
Thermal or membrane processing for Infant Milk Formula: Effects on protein digestion and integrity of the intestinal barrier
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 · see citing works
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 · see citing works
Self-citation
Invited review: Bovine colostrum, a promising ingredient for humans and animals—Properties, processing technologies, and uses
Costa, 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 49 · see citing works
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 · see citing works
“[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., Moughan, P. J., Wolfe, R. R., Ferrando, A., & Church, D. D. (2025) · Journal of NutriLife · doi:10.1016/j.tjnut.2025.07.005 · Cited by 45 · see citing works
“Whey proteins are soluble globular proteins that do not form micelles or gels, and their compact structure allows for rapid digestion and absorption [96].”
Processing affects beta-casomorphin peptide formation during simulated gastrointestinal digestion in both A1 and A2 milk
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 47 · see citing works
Self-citation
Kinetics 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 · see citing works
Effect of glycation degree on the in vitro simulated gastrointestinal digestion: A promising formulation for egg white gel with controlled digestibility
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 · see citing works
Novel animal product substitutes: A new category of plant‐based alternatives to meat, seafood, egg, and dairy products
McClements, D. J. (2024) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.13330 · Cited by 44 · see citing works
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 · see citing works
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 · see citing works
Influence of Lactose on the Maillard Reaction and Dehydroalanine-Mediated Protein Cross-Linking in Casein and Whey
Nielsen, S. D.-H., Knudsen, L. J., Bækgaard, L. T., Rauh, V., & Larsen, L. B. (2022) · Foods · doi:10.3390/foods11070897 · Cited by 41 · see citing works
“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].”
Background
Effect of Processing of Whey Protein Ingredient on Maillard Reactions and Protein Structural Changes in Powdered Infant Formula
Lund, P., Bechshøft, M. R., Ray, C., & Lund, M. N. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c05612 · Cited by 40 · see citing works
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 · see citing works
Self-citation
Structural and rheological properties of the clots formed by ruminant milks during dynamic in vitro gastric digestion: Effects of processing and species
Li, 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 · see citing works
Casein Protein Processing Strongly Modulates Post-Prandial Plasma Amino Acid Responses In Vivo in Humans
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 37 · see citing works
Dietary protein considerations for muscle protein synthesis and muscle mass preservation in older adults
Olaniyan, E. T., O’Halloran, F., & McCarthy, A. L. (2020) · Nutrition Research Reviews · doi:10.1017/s0954422420000219 · Cited by 39 · see citing works
“ofproteins, affectingdigestionkinetics(84).”
BackgroundInfluential
Dynamic in vitro gastric digestion behavior of goat milk: Effects of homogenization and heat treatments
Li, 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 · see citing works
Structural and chemical changes induced by temperature and pH hinder the digestibility of whey proteins
Accardo, F., Leni, G., Tedeschi, T., Prandi, B., & Sforza, S. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.132884 · Cited by 37 · see citing works
New insight on dietary strategies to increase insulin sensitivity and reduce diabetes prevalence: an expert perspective and recommendation
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 41 · see citing works
“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 · see citing works
Self-citation
Dietary 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 35 · see citing works
“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].”
Background
Comparing the effects of hydrostatic high-pressure processing vs holder pasteurisation on the microbial, biochemical and digestion properties of donor human milk
Zhang, 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 · see citing works
Comparative study on microbiological, physicochemical and nutritional properties of whole cow milk by thermal and non-thermal processing technologies
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 · see citing works
In Vitro Assessment of the Impact of Industrial Processes on the Gastrointestinal Digestion of Milk Protein Matrices Using the INFOGEST Protocol
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 · see citing works
“Processes such as heating, for example, are known to denature whey proteins, making them more digestible [6].”
Background
Formation of structured clots, gastric emptying and hydrolysis kinetics of yak milk during in vitro dynamic gastrointestinal digestion: Impact of different heat treatments
Liu, 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 · see citing works
Nutritional Value of Yogurt as a Protein Source: Digestibility/Absorbability and Effects on Skeletal Muscle
Sumi, K., Tagawa, R., Yamazaki, K., Nakayama, K., Ichimura, T., Sanbongi, C., & Nakazato, K. (2023) · Nutrients · doi:10.3390/nu15204366 · Cited by 31 · see citing works
Thermally-Induced Lactosylation of Whey Proteins: Identification and Synthesis of Lactosylated β-lactoglobulin Epitope
Gasparini, A., Bühler, S., Faccini, A., Sforza, S., & Tedeschi, T. (2020) · Molecules · doi:10.3390/molecules25061294 · Cited by 30 · see citing works
Milk as a Complex Multiphase Polydisperse System: Approaches for the Quantitative and Qualitative Analysis
Smirnova, A., Коноплев, Г., Mukhin, N. V., Stepanova, O. S., & Steinmann, U. (2020) · Journal of Composites Science · doi:10.3390/jcs4040151 · Cited by 30 · see citing works
Identifying glycation hot-spots in bovine milk proteins during production and storage of skim milk powder
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 29 · see citing works
Distribution and variation in proteins of casein micellar fractions response to heat-treatment from five dairy species
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 · see citing works
Postprandial metabolism and gut permeability in calves fed milk replacer with different macronutrient profiles or a whole milk powder
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 · see citing works
“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).”
Background
Does the Nutritional Composition of Dairy Milk Based Recovery Beverages Influence Post-exercise Gastrointestinal and Immune Status, and Subsequent Markers of Recovery Optimisation in Response to High Intensity Interval Exercise?
Russo, 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 · see citing works
Protein ingredient quality of infant formulas impacts their structure and kinetics of proteolysis under in vitro dynamic digestion
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 · see citing works
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 · see citing works
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 · see citing works
Enhanced Uptake of Processed Bovine β‐Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity
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 22 · see citing works
Self-citation
Digestibility of polymerized whey protein using in vitro digestion model and antioxidative property of its hydrolysate
Zhong, W., Li, J., Dai, J., Wang, C., & Zhang, T. (2021) · Food Bioscience · doi:10.1016/j.fbio.2021.101109 · Cited by 22 · see citing works
Ultra‐High Temperature Treatment and Storage of Infant Formula Induces Dietary Protein Modifications, Gut Dysfunction, and Inflammation in Preterm Pigs
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 · see citing works
Circulating Branched Chain Amino Acid Concentrations Are Higher in Dairy-Avoiding Females Following an Equal Volume of Sheep Milk Relative to Cow Milk: A Randomized Controlled Trial
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 · see citing works
Gastric clot formation and digestion of milk proteins in static in vitro infant gastric digestion models representing different ages
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 · see citing works
Self-citation
From lab‐based to in‐line: Analytical tools for the characterization of whey protein denaturation and aggregation–A review
Finnegan, 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 · see citing works
Factors affecting the modification of bovine milk proteins in high hydrostatic pressure processing: An updated review
Gharbi, N., Marciniak, A., & Doyen, A. (2022) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.13012 · Cited by 18 · see citing works
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 · see citing works
Self-citation
Influence of storage time on protein composition and simulated digestion of UHT milk and centrifugation presterilized UHT milk in vitro
Sun, Y., Wang, R., Li, Q., & Ma, Y. (2023) · Journal of Dairy Science · doi:10.3168/jds.2022-22602 · Cited by 18 · see citing works
Assessment of Stress Levels in Lactating Cattle: Analyzing Cortisol Residues in Commercial Milk Products in Relation to the Temperature-Humidity Index
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 · see citing works
Exploration of Calocybe indica mushroom phenolic acid-kidney bean protein complex: Functional properties, amino acid profiles, in-vitro digestibility, and application in vegan product development
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 · see citing works
Impact of UHT treatment and storage on liquid infant formula: Complex structural changes uncovered by centrifugal field-flow fractionation with multi-angle light scattering
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 · see citing works
Heat Treatment of Milk: A Rapid Review of the Impacts on Postprandial Protein and Lipid Kinetics in Human Adults
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 · see citing works
Development in Maillard Reaction and Dehydroalanine Pathway Markers during Storage of UHT Milk Representing Differences in Casein Micelle Size and Sedimentation
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 17 · see citing works
“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].”
Background
Current progress of emerging technologies in human and animals’ milk processing: Retention of immune‐active components and microbial safety
Liu, 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 · see citing works
Self-citation
Effect of glycation derived from α-dicarbonyl compounds on the in vitro digestibility of ovalbumin: Tracing of advanced glycation end-products and immuno-active peptides
Huang, 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 16 · see citing works
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 · see citing works
Donkey milk and fermented donkey milk: are there differences in the nutritional value and physicochemical characteristics?
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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.
ORCID: Lambers, Tim T.
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
DOI: 10.1080/10408398.2019.1646703
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: cc-by-nc-nd
creativecommons.org/licenses/by-nc-nd/4.0/ (vor)
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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
Life Sciences › Agricultural and Biological Sciences › Food Science › Food and Agricultural Sciences
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

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How processing may affect milk protein digestion and overall physiological outcomes: A systematic review

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