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      Formation and Degradation of Beta-casomorphins in Dairy Processing

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          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.

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          Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese.

          Seven kinds of ripened cheeses (8-mo-aged and 24-mo-aged Gouda, Emmental, Blue, Camembert, Edam, and Havarti) were homogenized with distilled water, and water-soluble peptides were prepared by C-18 hydrophobic chromatography. The inhibitory activity to angiotensin I-converting enzyme and decrease in the systolic blood pressure in spontaneously hypertensive rats were measured before and after oral administration of each peptide sample. The strongest depressive effect in the systolic blood pressure (-24.7 mm Hg) and intensive inhibitory activity to angiotensin I-converting enzyme (75.7%) were detected in the peptides from 8-mo-aged Gouda cheese. Four peptides were isolated by HPLC with reverse-phase and gel filtration modes. Their chemical structures and origins, clarified by combination analyses of protein sequencing, amino acid composition, and mass spectrometry, were as follows: peptide A, Arg-Pro-Lys-His-Pro-Ile-Lys-His-Gln [alpha(s1)-casein (CN), B-8P; f 1-9]; peptide B, Arg-Pro-Lys-His-Pro-Ile-Lys-His-Gln-Gly-Leu-Pro-Gln (alpha(s1)-CN, B-8P; f 1-13); peptide F, Tyr-Pro-Phe-Pro-Gly-Pro-Ile-Pro-Asn (beta-CN, A2-5P; f 60-68); and peptide G, Met-Pro-Phe-Pro-Lys-Tyr-Pro-Val-Gln-Pro-Phe (beta-CN, A2-5P; f 109-119). Peptides A and F, which were chemically synthesized, showed potent angiotensin I-converting enzyme inhibitory activity with little antihypertensive effects.
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            Latent bioactive peptides in milk proteins: proteolytic activation and significance in dairy processing.

            After a brief description of the properties of bioactive peptides, the proteolytic activation of the bioactive sequences from milk protein precursors is discussed. The ability of proteolytic enzymes from various sources, especially from lactic acid bacteria, to release bioactive peptides and the physiological and biotechnological significance of these peptides in dairy products are reviewed.
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              Polymorphism of bovine beta-casein and its potential effect on human health.

              Proteins in bovine milk are a common source of bioactive peptides. The peptides are released by the digestion of caseins and whey proteins. In vitro the bioactive peptide beta-casomorphin 7 (BCM-7) is yielded by the successive gastrointestinal proteolytic digestion of bovine beta-casein variants A1 and B, but this was not seen in variant A2. In hydrolysed milk with variant A1 of beta-casein, BCM-7 level is 4-fold higher than in A2 milk. Variants A1 and A2 of beta-casein are common among many dairy cattle breeds. A1 is the most frequent in Holstein-Friesian (0.310-0.660), Ayrshire (0.432-0.720) and Red (0.710) cattle. In contrast, a high frequency of A2 is observed in Guernsey (0.880-0.970) and Jersey (0.490-0.721) cattle. BCM-7 may play a role in the aetiology of human diseases. Epidemiological evidence from New Zealand claims that consumption of beta-casein A1 is associated with higher national mortality rates from ischaemic heart disease. It seems that the populations that consume milk containing high levels of beta-casein A2 have a lower incidence of cardiovascular disease and type 1 diabetes. BCM-7 has also been suggested as a possible cause of sudden infant death syndrome. In addition, neurological disorders, such as autism and schizophrenia, seem to be associated with milk consumption and a higher level of BCM-7. Therefore, careful attention should be paid to that protein polymorphism, and deeper research is needed to verify the range and nature of its interactions with the human gastrointestinal tract and whole organism.
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                Author and article information

                Journal
                Crit Rev Food Sci Nutr
                Crit Rev Food Sci Nutr
                BFSN
                bfsn20
                Critical Reviews in Food Science and Nutrition
                Taylor & Francis
                1040-8398
                1549-7852
                6 December 2015
                10 June 2015
                : 55
                : 14
                : 1955-1967
                Affiliations
                [ a ]Food Science and Technology Program, School of Public Health, Curtin Health Innovation Research Institute, Curtin University , Perth, Western Australia, Australia
                [ b ]Curtin Water Quality Research Centre, Department of Chemistry, Curtin University , Perth, Western Australia, Australia
                Author notes
                Address correspondence to Dr. Vicky Solah, Curtin Health Innovation Research Institute, Curtin University, Food Science and Technology Program , GPO Box U1987, Perth, Western Australia, Australia. E-mail: V.Solah@ 123456curtin.edu.au

                Color versions of one or more of the figures in the article can be found online at www.tandfonline.com/bfsn

                Article
                740102
                10.1080/10408398.2012.740102
                4487594
                25077377
                5a947ebf-ed08-490a-8ff4-94fc93ad346c
                © 2015 Duc Doan Nguyen, Stuart Johnson, Franceso Busetti, and Vicky Solah. Published with license by Taylor & Francis© Duc Doan Nguyen, Stuart Johnson, Franceso Busetti, and Vicky Solah

                This is an Open Access article. Non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly attributed, cited, and is not altered, transformed, or built upon in any way, is permitted. The moral rights of the named author(s) have been asserted.

                History
                Page count
                Figures: 2, Tables: 4, References: 82, Pages: 13
                Categories
                Original Articles

                Nutrition & Dietetics
                beta-casomorphin,cheese,yoghurt,heat treatment,fermentation,ripening
                Nutrition & Dietetics
                beta-casomorphin, cheese, yoghurt, heat treatment, fermentation, ripening

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