Article

Technological options for the production of health-promoting proteins and peptides derived from milk and colostrum

MTT Agrifood Research Finland, Biotechnology and Food Research, FIN-31600 Jokioinen, Finland.
Current pharmaceutical design (Impact Factor: 3.29). 02/2007; 13(8):829-43. DOI: 10.2174/138161207780363112
Source: PubMed

ABSTRACT Milk proteins are known to exert a wide range of nutritional, functional and biological activities. Apart from being a balanced source of valuable amino acids, milk proteins contribute to the consistency and sensory properties of various dairy products. Furthermore, many milk proteins possess specific biological properties which make them potential ingredients of health-promoting foods. These properties are attributed to both native protein molecules and to physiologically active peptides encrypted in the protein molecules. Considerable progress has been made over the last twenty years in technologies aimed at separation, fractionation and isolation in a purified form of many interesting proteins occurring in bovine colostrum and milk. Industrial-scale methods have been developed for native whey proteins such as immunoglobulins, lactoferrin, lactoperoxidase, alpha-lactalbumin and beta-lactoglobulin. Their large-scale manufacture and commercial exploitation is still limited although validated research data about their physiological health benefits is rapidly accumulating. Promising product concepts and novel fields of use have emerged recently, and some of these molecules have already found commercial applications. The same applies to bioactive peptides derived from different milk proteins. Active peptides can be liberated during gastrointestinal digestion or milk fermentation with proteolytic enzymes. Such peptides may exert a number of physiological effects in vivo on the gastrointestinal, cardiovascular, endocrine, immune, nervous and other body systems. However, at present the industrial-scale production of such peptides is limited by a lack of suitable technologies. On the other hand, a number of bioactive peptides have been identified in fermented dairy products, and there are already a few commercial dairy products enriched with blood pressure-reducing milk protein peptides. There is a need to develop methods to optimise the activity of bioactive peptides in food systems and to enable their optimum utilisation in the body. This review highlights existing modern technologies applicable for the isolation of bioactive native proteins and peptides derived from bovine colostrum, milk and cheese whey, and discusses aspects of their current and potential applications for human nutrition and promotion of human health.

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Available from: Hannu Korhonen, Apr 28, 2015
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    • "In addition the tetra-peptide, α-lactalbumin f(50–53), a-lactorphin (Tyr-Gly-Leu-Phe) which is known to produce an antihypertensive effect in vivo when administered subcutaneously to normotensive Wistar Kyoto strain and spontaneously hypertensive rats (SHR), elicited no effect typical of active opioids in behavioural tests in mice after intraperitoneal administration (Nurminen et al. 2002, Ijaes et al. 2004). Functional peptides have been studied in milk, whey, enzymatic protein hydrolysates and fermented dairy products (Meisel 2005; Korhonen and Pihlanto 2007; Gobbetti et al., 2002; Gobbetti et al., 2007; Hartmann and Meisel 2007; Korhonen 2009; Korhonen 2010). Whey peptides have been studied for anti-clotting, anti-thrombotic and hypotensive activity (Gobbetti et al., 2007), mood regulation and opioid-like activity, antibacterial activity (Clare et al., 2003), immunomodulation, anti-inflammatory activity, anti-carie properties (Martinez et al., 2009), prebiotic activity, mineral binding properties, gastrointestinal health effect, hypocholesterolemic effects, insulinotropic effects, memory and stress effects (Korhonen, 2010). "
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    ABSTRACT: The type and composition of whey at dairy plants mainly depends upon the processing techniques resulting from caseins removal during cheese-making. The content and composition of whey proteins from goat, sheep camel, mare and donkey differ consistently from whey protein content in cow milk. Whey proteins proteolysis generates smaller peptides some of which possess beneficial biological activities, and their total content is influenced by whey origin and composition. The industrial exploitation of whey proteins may follow two approaches. From one side, following the principle of sustainable economy and waste recycling the industry could exploit the high amounts of whey by-products as source of valuable peptides. On the other side, a different approach has been pursued through extraction of individual proteins from milk or whey consisting in chitosan addition to milk, acidification, centrifugation and chromatographic separation using anionic resins added in bulk that exploit different Isoelectric points of each whey protein. Whey bioactives are a valuable source of functional proteins that can be exploited in novel formulations, to be assumed through food ingestion. This chapter discusses the beneficial effects and potential applications of different whey isolates originating from different mammal milks, and the approaches to exploitation of whey protein fractions of different whey types.
    Whey: Types, Composition and Health Implications, Edited by Benitez RM, Ortero GM, 05/2012: chapter Bioactive Peptides with Health Benefit and their Differential Content in Whey of Different Origin: pages 153-168; Nova, Hauppauge, NY., ISBN: 978-1-61942-862-1
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    • "Moreover, some of them were shown to have antihypertensive activity against established hypertension in spontaneously hypertensive rats (Masuda et al., 1996; Nurminen et al., 2000) and in humans (Messaoudi et al., 2005; Mizuno et al., 2005; Cadée et al., 2007). Bioactive peptides, as specific protein fragments, are produced during digestion of milk in the gastrointestinal tract or during food processing (Meisel and Fitzgerald, 2003; Korhonen and Pihlanto, 2007). Their bioactivity is based on inherent amino acid composition and sequence, and the ACE inhibitory activity was mainly attributed to α S1 -and α S2 -casein fractions (Tauzin et al., 2002). "
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    ABSTRACT: A great number of milk-derived peptides have been shown to exhibit angiotensin converting enzyme (ACE) inhibitory properties and thus potential utility in the regulation of blood pressure. The present work aimed to investigate the effects of 2 milk trypsin hydrolysates from alpha(S1)- and alpha(S2)-casein (CH1 and CH2, respectively) on ACE activity evaluated in human umbilical vein endothelial cells (HUVEC) in vitro, rat aortic tissues ex vivo, and renovascular hypertensive rat in vivo. Incubation of HUVEC and rat aortic tissues with CH1 or CH2 induced a concentration-dependent inhibition of hydrolysis of the ACE substrate hippuryl-histidyl-leucine (HHL), the hydrolysates being much less potent than perindopril (an ACE inhibitor). However, in contrast to perindopril, CH1 and CH2 failed to modify angiotensin I-induced aortic ring vasoconstriction. The HPLC profiles of rat plasma after intragastric administration were variable among individuals but none of the observed peaks corresponded to peptides comprising CH1 or CH2 or to fragments of these peptides. During 4 wk of cardiovascular monitoring, in hydrolysate-fed renovascular hypertensive rats, systolic blood pressure weakly decreased compared with the control group. However, the CH1-fed hypertensive rats exhibited a decrease of heart rate during the nocturnal period of activity. To conclude, our results show that CH1 and CH2 inhibited ACE activity in HUVEC and rat aortic tissue but failed to antagonize the aortic-constricting effects of the natural agonist angiotensin I. Moreover, we demonstrated that CH1, to a greater extent than CH2, can slightly affect cardiovascular parameters although the ingested bioactive peptides could not be detected in the blood.
    Journal of Dairy Science 07/2010; 93(7):2906-21. DOI:10.3168/jds.2010-3060 · 2.55 Impact Factor
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