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Formation and Degradation of Beta-casomorphins in Dairy Processing.

Nguyen DD, Johnson SK, Busetti F, Solah VA - Crit Rev Food Sci Nutr (2015)

Bottom Line: BCMs have been detected in raw cow's milk and human milk and a variety of commercial cheeses, but their presence has yet to be confirmed in commercial yoghurts.The finding that BCMs are present in cheese suggests they could also form in yoghurt, but be degraded during yoghurt processing.Whether BCMs do form in yoghurt and the amount of BCM forming or degrading at different processing steps needs further investigation and possibly will depend on the heat treatment and fermentation process used, but it remains an intriguing unknown.

View Article: PubMed Central - PubMed

Affiliation: a Food Science and Technology Program, School of Public Health, Curtin Health Innovation Research Institute, Curtin University , Perth , Western Australia , Australia.

ABSTRACT
Milk proteins including casein are sources of peptides with bioactivity. One of these peptides is beta-casomorphin (BCM) which belongs to a group of opioid peptides formed from β-casein variants. Beta-casomorphin 7 (BCM7) has been demonstrated to be enzymatically released from the A1 or B β-casein variant. Epidemiological evidence suggests the peptide BCM 7 is a risk factor for development of human diseases, including increased risk of type 1 diabetes and cardiovascular diseases but this has not been thoroughly substantiated by research studies. High performance liquid chromatography coupled to UV-Vis and mass spectrometry detection as well as enzyme-linked immunosorbent assay (ELISA) has been used to analyze BCMs in dairy products. BCMs have been detected in raw cow's milk and human milk and a variety of commercial cheeses, but their presence has yet to be confirmed in commercial yoghurts. The finding that BCMs are present in cheese suggests they could also form in yoghurt, but be degraded during yoghurt processing. Whether BCMs do form in yoghurt and the amount of BCM forming or degrading at different processing steps needs further investigation and possibly will depend on the heat treatment and fermentation process used, but it remains an intriguing unknown.

No MeSH data available.


Related in: MedlinePlus

The primary structure of β-casein A2 indicating amino acid substitution of the variants (adapted from Swaigood, 2003).
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f0001: The primary structure of β-casein A2 indicating amino acid substitution of the variants (adapted from Swaigood, 2003).

Mentions: Protein in bovine milk contains four caseins αs1, αs2, β, and κ-casein and two major whey proteins, β-lactoglobulin and α-lactoalbumin (Kamiński et al., 2007). In recent years, the 209 amino acid residues in the chains of β-casein (Fig. 1) (Swaigood, 2003; Truswell, 2005) have been studied extensively. It was found that there are 13 variants present in bovine milk including A1, A2, A3, A4, B, C, D, E, F, H1, H2, I, and H (Kamiński et al., 2007), of which A1 and A2 are the most common variants. The primary structure of some variants is showed at Figure 1. Milk from European breeds such as Holstein–Friesian mainly contains A1 β-casein (Tailford et al., 2003), while A2 β-casein is commonly detected in milk from Guernsey and Jersey breeds (Bell et al., 2006; Merriman, 2009). The difference between A1 and A2 variant is a single amino acid at position 67 on the chain; being histidine in A1 and proline in A2 (Truswell, 2005; Kamiński et al., 2007).Figure 1.


Formation and Degradation of Beta-casomorphins in Dairy Processing.

Nguyen DD, Johnson SK, Busetti F, Solah VA - Crit Rev Food Sci Nutr (2015)

The primary structure of β-casein A2 indicating amino acid substitution of the variants (adapted from Swaigood, 2003).
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4487594&req=5

f0001: The primary structure of β-casein A2 indicating amino acid substitution of the variants (adapted from Swaigood, 2003).
Mentions: Protein in bovine milk contains four caseins αs1, αs2, β, and κ-casein and two major whey proteins, β-lactoglobulin and α-lactoalbumin (Kamiński et al., 2007). In recent years, the 209 amino acid residues in the chains of β-casein (Fig. 1) (Swaigood, 2003; Truswell, 2005) have been studied extensively. It was found that there are 13 variants present in bovine milk including A1, A2, A3, A4, B, C, D, E, F, H1, H2, I, and H (Kamiński et al., 2007), of which A1 and A2 are the most common variants. The primary structure of some variants is showed at Figure 1. Milk from European breeds such as Holstein–Friesian mainly contains A1 β-casein (Tailford et al., 2003), while A2 β-casein is commonly detected in milk from Guernsey and Jersey breeds (Bell et al., 2006; Merriman, 2009). The difference between A1 and A2 variant is a single amino acid at position 67 on the chain; being histidine in A1 and proline in A2 (Truswell, 2005; Kamiński et al., 2007).Figure 1.

Bottom Line: BCMs have been detected in raw cow's milk and human milk and a variety of commercial cheeses, but their presence has yet to be confirmed in commercial yoghurts.The finding that BCMs are present in cheese suggests they could also form in yoghurt, but be degraded during yoghurt processing.Whether BCMs do form in yoghurt and the amount of BCM forming or degrading at different processing steps needs further investigation and possibly will depend on the heat treatment and fermentation process used, but it remains an intriguing unknown.

View Article: PubMed Central - PubMed

Affiliation: a Food Science and Technology Program, School of Public Health, Curtin Health Innovation Research Institute, Curtin University , Perth , Western Australia , Australia.

ABSTRACT
Milk proteins including casein are sources of peptides with bioactivity. One of these peptides is beta-casomorphin (BCM) which belongs to a group of opioid peptides formed from β-casein variants. Beta-casomorphin 7 (BCM7) has been demonstrated to be enzymatically released from the A1 or B β-casein variant. Epidemiological evidence suggests the peptide BCM 7 is a risk factor for development of human diseases, including increased risk of type 1 diabetes and cardiovascular diseases but this has not been thoroughly substantiated by research studies. High performance liquid chromatography coupled to UV-Vis and mass spectrometry detection as well as enzyme-linked immunosorbent assay (ELISA) has been used to analyze BCMs in dairy products. BCMs have been detected in raw cow's milk and human milk and a variety of commercial cheeses, but their presence has yet to be confirmed in commercial yoghurts. The finding that BCMs are present in cheese suggests they could also form in yoghurt, but be degraded during yoghurt processing. Whether BCMs do form in yoghurt and the amount of BCM forming or degrading at different processing steps needs further investigation and possibly will depend on the heat treatment and fermentation process used, but it remains an intriguing unknown.

No MeSH data available.


Related in: MedlinePlus