In vitro digestion of bovine and caprine milk by human gastric and duodenal enzymes

Almaas, H.; Cases, Anne-Laure; Devold, Tove Gulbrandsen; Holm, Halvor; Langsrud, Thor; Aabakken, Lars; Aadnoey, Tormod; Vegarud, Gerd Elisabeth

doi:10.1016/j.idairyj.2005.10.029

Cited by 127 publications

(86 citation statements)

References 28 publications

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“…The protein content of the respective milks measured by the Kjeldahl method was lying within the range of normal values observed by our earlier studies of individual and batch milk [2], and also reported by others (Tab. I).…”

Section: Milksupporting

confidence: 90%

“…To follow up and extend previous work on in vitro digestion of milk and milk proteins [1][2][3]9], the gastric and duodenal juices employed were obtained from the same person. These juices show enzyme activities that lie within the normal range of pepsin and total proteolytic activities observed in 12 individuals (men and women).…”

Section: Human Digestive Enzymesmentioning

confidence: 99%

“…These results led to the concept of "slow" digested caseins and "fast" digested whey proteins [6,7,17]. On the contrary, our earlier studies using human gastric (HGJ) and duodenal (HDJ) juices for the in vitro digestion of bovine and caprine milk proteins revealed that the whey proteins, α-la and β-lg, were very resistant to hydrolysis and that the caseins were degraded fast [2]. There are many studies performed on in vitro digestion using commercial enzymes, such as purified pepsin and trypsin, in an attempt to reveal peptides with physiological activities [15,28].…”

Section: Introductionmentioning

confidence: 99%

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Comparison of the digestion of caseins and whey proteins in equine, bovine, caprine and human milks by human gastrointestinal enzymes

Inglingstad

Devold

Eriksen

et al. 2010

Dairy Sci. Technol.

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142

104

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-The aim of this study was to compare the digestion of milk proteins from different species using an in vitro gastrointestinal model. Raw and heated milks from bovine, caprine, human and equine species were digested by human digestive enzymes. Digestion was performed in two 30-min sequential steps by digestive juices from the stomach (pH 2.5/37°C) and from the duodenum (pH 8.0/37°C). The degradation patterns of the milk proteins were visualized by SDS-PAGE and quantified using the ImageQuant program. Caseins in the equine milk were rapidly digested by the gastric juice in contrast to the caseins from the other species. During the subsequent digestion by the duodenal juice most of the caseins from all species were degraded within 5 min, and within 30 min only traces of caseins were detected. The mean casein micellar size varied between species in the range of 146.0-311.5 nm (equine > caprine > bovine > human). The α-lactalbumin from all species appeared to be very resistant to both gastric and duodenal digestions. A similar trend was shown for β-lactoglobulin from bovine and caprine milks, of which~60% intact protein remained, while only 25% remained intact in equine milk after total digestion. Equine milk contained a high amount of lysozyme, of which 60% remained intact in the present study. In heated milks from all species, only α-lactalbumin degradation increased approximately 12-20% in comparison to the raw milk. This study shows that equine milk with fast digestible proteins could be considered as a replacement for bovine milk in the diet of people with special needs, such as infants and the elderly. equine milk / bovine milk / caprine milk / human milk / digestion / whey protein / casein Résumé -Comparaison de la digestion des caséines et des protéines de lactosérum du lait équin, bovin, caprin et humain par les enzymes gastro-intestinales humaines. Le but de cette étude était de comparer la digestion des protéines laitières provenant de différentes espèces en utilisant un modèle gastro-intestinal in vitro. Des laits crus et traités thermiquement des espèces bovines, caprines, équines et humaines ont été digérés par des enzymes digestives humaines. La digestion a été réalisée au cours de deux étapes séquentielles de 30 min par des sucs digestifs gastriques (pH 2,5/37°C) et duodénaux (pH 8,0/37°C). Les profils de dégradation des protéines laitières ont été visualisés par SDS-PAGE et quantifiés à l'aide du programme ImageQuant. Les caséines du lait équin étaient rapidement digérées par le suc gastrique contrairement aux caséines des autres espèces. Au cours de la digestion suivante par le suc duodénal, la plupart des caséines de toutes les espèces étaient dégradées en 5 min, et après 30 min seules des traces des caséines étaient détectées. La taille moyenne des micelles de caséines variait de 146,0 à 311,5 nm selon les espèces (équin > caprin > bovin > humain). L'α-lactalbumine de toutes les espèces apparaissait être très résistante à la fois à la digestion gastrique et duodénale. Une tendance simila...

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Section: Milksupporting

confidence: 90%

Section: Human Digestive Enzymesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Comparison of the digestion of caseins and whey proteins in equine, bovine, caprine and human milks by human gastrointestinal enzymes

Inglingstad

Devold

Eriksen

et al. 2010

Dairy Sci. Technol.

Self Cite

142

104

View full text Add to dashboard Cite

show abstract

“…Enzymatically cross-linked -casein decreased their digestibility in comparison with native -casein (Monogioudi et al, 2011). Heat treatment of milk (sterilization) increases protein resistance to the in vitro digestion in comparison with unheated milk, probably because of the structural changes caused by denaturation and aggregation of whey proteins and/or casein with whey proteins through disulfide bounds (Almaas et al, 2006;Dupont et al, 2010). In addition, structuring -lg into fibrils (formed by heating solutions at 80ºC and pH 2.0 for 20 h) induces a more complete digestion by pepsin (Bateman et al, 2010).…”

Section: Proteinsmentioning

confidence: 99%

Improving Nutrition Through the Design of Food Matrices

Zúñiga¹,

Troncoso²

2012

Scientific, Health and Social Aspects of the Food Industry

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“…It has been argued that the lack of α s1 -casein may give the Norwegian goats' milk an advantage from a nutritional point of view because of a possible easier digestion of this milk. However, Almaas et al (2006) investigated in vitro digestion of bovine and caprine milk by human gastric and duodenal enzymes and concluded that no significant differences were observed between the digestion of goats' milk with a high level of α s1 -casein, and milk from typical Norwegian goats lacking this protein.…”

Section: Genetic Polymorphism Of Proteins In Goats' Milkmentioning

confidence: 99%

Milk quality – a future approach from a researcher’s point of view

Abrahamsen¹,

Borge²,

Harstad³

et al. 2007

J. Anim. Feed Sci.

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The approach to the term "milk quality" varies among consumers, dairies and researchers and is therefore very difficult to define. Three main elements of the term are however dealt with in this paper. An increased understanding of the nutritional value of various milk components is necessary. How breeding and feeding can influence the nutritional quality of the milk or whether the processing properties of the milk are changed needs further investigation. A need for documentation of various quality aspects of milk produced in different regions will appear. Further research on the functional effect of genetic variants of proteins on dairy products is necessary if this factor is going to be an element in the breeding programmes.

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In vitro digestion of bovine and caprine milk by human gastric and duodenal enzymes

Cited by 127 publications

References 28 publications

Comparison of the digestion of caseins and whey proteins in equine, bovine, caprine and human milks by human gastrointestinal enzymes

Comparison of the digestion of caseins and whey proteins in equine, bovine, caprine and human milks by human gastrointestinal enzymes

Improving Nutrition Through the Design of Food Matrices

Milk quality – a future approach from a researcher’s point of view

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