Formation and Degradation of Beta-casomorphins in Dairy Processing

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 b-casein variants. Beta-casomorphin 7 (BCM7) has been demonstrated to be enzymatically released from the A1 or B b-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.

Meta‐Analysis for Correlating Structure of Bioactive Peptides in Foods of Animal Origin with Regard to Effect and Stability

“…Pretreatment heat can enhance existing health effects of bioactive peptides: Adjonu, Doran, Torley, and Agboola (2013) found that pretreatment at temperatures higher than 90°C enhanced ACE-inhibiting activity of a β-lactoglobulin fragment. Results of Jayatilake et al (2014) imply that treatment at low temperatures could also enhance the anti-inflammatory action of whey proteins, due to higher retention of immunoactive proteins and factors, such as immunoglobulins, lactoferrin, and growth factors (Nguyen et al, 2015). Other factors that could be important include the type of heat source: Gomaa (2010) found that microwave heating not only enhanced antioxidative activity of β-lactoglobulin hydrolysate, but the same hydrolysate also presented unique proteins, an indication that microwave treatment may have exposed new cleavage sites within the protein.…”

“…Several review papers list various health effects of bioactive peptides from foods of animal origin (Aneiros & Garateix, 2004;Bhopale, 2016;Lafarga & Hayes, 2014;Nguyen, Johnson, Busetti, & Solah, 2015;Udenigwe & Howard, 2013;Yu, Yin, Zhao, Chen, & Liu, 2014;Zambrowicz et al, 2015) and these characterized bioactive peptides have been incorporated into databases such as BIOPEP (Table S1). However, most of these databases cover peptides of specific length, origin, and/or health effect.…”

99mTc Bağlı Yeni Bir Peptid: Ratlarda 99m Tc β-Kazomorphin 6 Molekülünün Biyodistrübisyon ve Görüntüleme Çalışması

“…Animal studies clearly show that β-casomorphins opioid-like peptides are derived from β-casein [19][20][21][22][23][24][25][26] . β-Casomorphins are exogenous opioid peptides derivatives containing the common N-terminal amino acid sequence Tyr-Pro-Phe-Pro and have preferential μ-receptor agonistic activity [25] .…”

“…After mixing 500 µL octanol, 500 µL 0.9% NaCl or H 2 O and 10 microcurie 99m Tc labeled peptide in a vortex mixer for 1 min, they were centrifuged at 4.000 rpm. Low phase and upper phase radioactivity were counted in dose calibrator and phases were rationed and logarithm was calculated [22,24,25] . The lipophilicity was calculated using the formula logP = A0/Aw Besides, theoretical lipophilicity values were compared with experimental values using ACD chemsketch computer program (Table 2).…”

“…N terminal amino acid chain mainly tyr-pro-phe-pro structured exogen opioid peptid type beta casomorphin are receptör agonistic activity with priority [21,22] .…”