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: 3.45). 02/2007; 13(8):829-43. DOI: 10.2174/138161207780363112
Source: PubMed


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 particular, lactoferrin, a glycoprotein (80 kDa) member of the transferrin family in milk, consists of 673 amino acid residues. Lactoferrin and its peptides play an important role in innate defense against antimicrobial and antiviral activities (Kitts and Weiler, 2003), antioxidant activities (Korhonen and Pihlanto, 2007), and immunomodulating and cell growth effects (Swart et al., 1998; Mercier et al., 2004). Because of its positive charge at neutral pH, lactoferrin has been shown to form nanoparticles and coacervates (Shimoni et al., 2013) that could be utilized as delivery systems. "
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    ABSTRACT: Milk is composed of a wide variety of molecules with nutritional and multiple biological functionalities. The two main examples of colloidal structures in milk with multiple functions are fat globules and protein assemblies, referred to as casein micelles. Both assemblies are examples of how nature has resolved the task of delivering nutrients. They are often studied as a model of how to create structures in foods with enhanced functionality during consumption and digestion. Proteins and lipid aggregates in milk encode bioactive structures that will become important once digested, and will serve protective roles in the gut, for example, by regulating the immune system, by serving as cell differentiation factors, or by showing symbiotic functions with beneficial microorganisms. The milk components can form supramolecular structures that can be employed for the delivery of additional health benefits. The current knowledge of such structures present in milk, their changes during processing and digestion, and their relationship to biological functions in the gastrointestinal tract are outlined in this chapter. Recent findings in this area have created a paradigm shift in how we process and design new dairy foods aimed at providing additional health benefits to consumers.
    Full-text · Chapter · Jun 2014
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    • "Besides providing essential amino acids, colostrum and to a lesser extent milk proteins can exhibit different biological activities (Korhonen and Pihlanto 2007). For instance, lactoferrin (Lf) present in the milk or colostrum of various species of mammals exerts antimicrobial activities (Farnaud and Evans 2003). "
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    ABSTRACT: Camelmilk and colostrumare known to be a rich source of bioactive proteins. Camel milk, colostrum and colostral whey proteins were successively hydrolysed by pepsin and pancreatin using an in vitro protocol mimicking gastro-intestinal digestion. The degradation of proteins was characterised by electrophoresis and reversed-phase ultra-high performance liquid chromatography. Two whey proteins, α-lactalbumin and immunoglobulins G, weremore resistant to the digestive proteolytic enzymes than other camel milk and colostrum proteins. Undigested and digested samples were assayed for their antioxidant, angiotensin I-converting enzyme inhibitory and antimicrobial
    Full-text · Article · Jan 2014
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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.
    Full-text · Chapter · May 2012
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