Worldwide Research Trends on Milk Containing Only A2 β-Casein: A Bibliometric Study

Jiménez-Montenegro, Lucía; Alfonso, L.; Mendizábal, J. A.; Urrutia, Olaia

doi:10.3390/ani12151909

Cited by 24 publications

(16 citation statements)

References 70 publications

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“…Animal studies have also shown that A1 milk protein takes significantly longer to pass through the gastrointestinal tract during digestion. Additionally, it has been found that BCM‐7, which is produced after digestion, may induce an inflammatory immune response in the intestines (Jiménez‐Montenegro et al., 2022; Liu et al., 2022). Several studies have shown an association between the consumption of dairy products containing the A1 variant or BCM‐7 and an increased risk of type I diabetes mellitus, immune response, digestive dysfunction, autism, and respiratory dysfunction in some infants (Chitra, 2021; Kailash & Anil, 2014; Kamiński et al., 2007; Kaskous, 2020).…”

Section: Bovine Milk Casein and β‐Caseinmentioning

confidence: 99%

Bovine milk β‐casein: Structure, properties, isolation, and targeted application of isolated products

Chen,

Fan,

Wang

et al. 2024

Comp Rev Food Sci Food Safe

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Abstractβ‐Casein, an important protein found in bovine milk, has significant potential for application in the food, pharmaceutical, and other related industries. This review first introduces the composition, structure, and functional properties of β‐casein. It then reviews the techniques for isolating β‐casein. Chemical and enzymatic isolation methods result in inactivity of β‐casein and other components in the milk, and it is difficult to control the production conditions, limiting the utilization range of products. Physical technology not only achieves high product purity and activity but also effectively preserves the biological activity of the components. The isolated β‐casein needs to be utilized effectively and efficiently for various purity products in order to achieve optimal targeted application. Bovine β‐casein, which has a purity higher than or close to that of breast β‐casein, can be used in infant formulas. This is achieved by modifying its structure through dephosphorylation, resulting in a formula that closely mimics the composition of breast milk. Bovine β‐casein, which is lower in purity than breast β‐casein, can be maximized for the preparation of functional peptides and for use as natural carriers. The remaining byproducts can be utilized as food ingredients, emulsifiers, and carriers for encapsulating and delivering active substances. Thus, realizing the intensive processing and utilization of bovine β‐casein isolation. This review can promote the industrial production process of β‐casein, which is beneficial for the sustainable development of β‐casein as a food and material. It also provides valuable insights for the development of other active substances in milk.

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Section: Bovine Milk Casein and β‐Caseinmentioning

confidence: 99%

Bovine milk β‐casein: Structure, properties, isolation, and targeted application of isolated products

Chen,

Fan,

Wang

et al. 2024

Comp Rev Food Sci Food Safe

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“…Only seven of β-CN variants (A1, A2, A3, B, C, I, and E) have been detected in European cattle breeds. Although reported as the second type, the A2 variant is considered as the oldest one from which the others originated via mutation [ 37 ]. The presence of this variant is dominant in African and Asian cattle, where the average A1 and A2 frequency was found at the level of 0.16 and 0.82, respectively [ 15 , 20 , 34 , 35 , 38 ].…”

Section: β-Casein Genementioning

confidence: 99%

Does a Little Difference Make a Big Difference? Bovine β-Casein A1 and A2 Variants and Human Health—An Update

Cieślińska

Fiedorowicz

Rozmus

et al. 2022

IJMS

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For over 20 years, bovine beta-casein has been a subject of increasing scientific interest because its genetic A1 variant during gastrointestinal digestion releases opioid-like peptide β-casomorphin-7 (β-CM-7). Since β-CM-7 is involved in the dysregulation of many physiological processes, there is a growing discussion of whether the consumption of the β-casein A1 variant has an influence on human health. In the last decade, the number of papers dealing with this problem has substantially increased. The newest clinical studies on humans showed a negative effect of variant A1 on serum glutathione level, digestive well-being, cognitive performance score in children, and mood score in women. Scientific reports in this field can affect the policies of dairy cattle breeders and the milk industry, leading to the elimination of allele A1 in dairy cattle populations and promoting milk products based on milk from cows with the A2A2 genotype. More scientific proof, especially in well-designed clinical studies, is necessary to determine whether a little difference in the β-casein amino acid sequence negatively affects the health of milk consumers.

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“…Caseins comprise 80% of milk proteins and, based on the homology of the amino acid sequences, they are classified into α s1 -, α s2 -, β-, and κ-casein. There is a growing amount of interest in the function of milk from cows with genetic variants of β-casein [ 7 , 8 ]. Based on a point mutation in the amino acid at position 67, β-casein is described as A1 and A2 variants.…”

Section: Introductionmentioning

confidence: 99%

Modulatory Effects of A1 Milk, A2 Milk, Soy, and Egg Proteins on Gut Microbiota and Fermentation

Nuomin,

Baek,

Tsuruta

et al. 2023

Microorganisms

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Milk can be divided into A1 and A2 types according to β-casein variants, and there is a debate about whether A1 milk consumption exacerbates gut environments. This study examined the cecum microbiota and fermentation in mice fed A1 casein, A2 casein, mixed casein (commercial casein), soy protein isolate, and egg white. The cecum acetic acid concentration was higher, and the relative abundances of Muribaculaceae and Desulfovibrionaceae were greater in mice fed A1 versus A2 casein. The other parameters of cecum fermentation and microbiota composition were similar among the mice fed A1, A2, and mixed caseins. The differences were more distinctive among the three caseins, soy, and egg feedings. Chao 1 and Shannon indices of the cecum microbiota were lowered in egg white-fed mice, and the microbiota of mice fed milk, soy, and egg proteins were separately grouped by principal coordinate analysis. Mice fed the three caseins were characterized by a high abundance of Lactobacillaceae and Clostridiaceae, those fed soy were characterized by Corynebacteriaceae, Muribaculaceae, and Ruminococcaceae, and those fed egg white were characterized by Eggerthellaceae, Rikenellaceae, and Erysipelatoclostridiaceae. Thus, although several differences can arise between A1 and A2 caseins in terms of their modulatory effects on gut environments, the differences between milk, soy, and egg proteins can be more distinctive and are worth further consideration.

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Worldwide Research Trends on Milk Containing Only A2 β-Casein: A Bibliometric Study

Cited by 24 publications

References 70 publications

Bovine milk β‐casein: Structure, properties, isolation, and targeted application of isolated products

Bovine milk β‐casein: Structure, properties, isolation, and targeted application of isolated products

Does a Little Difference Make a Big Difference? Bovine β-Casein A1 and A2 Variants and Human Health—An Update

Modulatory Effects of A1 Milk, A2 Milk, Soy, and Egg Proteins on Gut Microbiota and Fermentation

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