232
marine (fish, lobsters, prawns, etc.) origin. These sources have been extensively
studied for their potent bioactivity except plant sources, which are gaining momentum for past few years (Korhonen 2009; El-Salam and El-Shibiny 2013; Mohanty
et al. 2016; Park and Nam 2015).
Potential Sources of Bioactive Peptides
Milk and Milk Products
Milk has 3.5% protein, which has been exploited to generate peptides, both from
whole milk protein as well as from its constituents (i.e. casein and whey). Whey
protein in milk has inherent biological activities like immunoglobulins, enzymes,
mineral-binding attributed to its makeup of β-lactoglobulin, α-lactalbumin and
some minor proteins. This makes milk a complex and unique food matrix which is
why more research is being published that contributes to the growing knowledge of
biologically active peptides from milk and lead to their possible incorporation in
functional foods, nutraceuticals, cosmetics, and pharmaceuticals (Panchaud et al.
2012; Mohanty et al. 2016).
Apart from this, it’s reported that naturally occurring protease enzymes like milk
plasmin degrade proteins and liberate bioactive peptides either during food processing or storage (Meisel and FitzGerald 2003). Microbes in the GI tract can also produce biologically active peptides (Saito 2004). Bovine milk proteins and their
peptides have been isolated and characterized to show several biological activities
(Sanchez and Vazquez 2017). Similarly, milk proteins of non-bovine sources like
camel, goat, sheep, buffalo and yak have also been used to obtain bioactive peptides
(El-Salam and El-Shibiny 2013). Although human milk is the most studied source
of bioactive peptides, milk from animals is also of research interest due to its resemblance to human milk. This makes animal milk a possible alternative for infant
consumption (Atanasova and Ivanova 2010; Bidasolo et al. 2012)
Milk products fermented with many types of bacteria are also capable of generating bioactive peptides. For example, hypertensive subjects were administered with
Lactobacillus helveticus fermented milk containing two biologically active tripeptides Val-Pro-Pro and Ile-Pro-Pro. A reduction in blood pressure was observed
(Nakamura et al. 1995). Furthermore, milk proteins have been hydrolyzed to obtain
β-casomorphins and caseino macro-peptide-derived peptides (from casein), and lactorphins (from whey) which demonstrated ACE-inhibitory, opioid and antimicrobial activities (Sipola et al. 2002; Jakala and Vapaatalo 2010; Boutrou et al. 2015).
Finally, bovine and non-bovine colostrum studies are also documented to release
peptides with bioactivities (Park and Nam 2015).
S. Maqsood et al.
marine (fish, lobsters, prawns, etc.) origin. These sources have been extensively
studied for their potent bioactivity except plant sources, which are gaining momentum for past few years (Korhonen 2009; El-Salam and El-Shibiny 2013; Mohanty
et al. 2016; Park and Nam 2015).
Potential Sources of Bioactive Peptides
Milk and Milk Products
Milk has 3.5% protein, which has been exploited to generate peptides, both from
whole milk protein as well as from its constituents (i.e. casein and whey). Whey
protein in milk has inherent biological activities like immunoglobulins, enzymes,
mineral-binding attributed to its makeup of β-lactoglobulin, α-lactalbumin and
some minor proteins. This makes milk a complex and unique food matrix which is
why more research is being published that contributes to the growing knowledge of
biologically active peptides from milk and lead to their possible incorporation in
functional foods, nutraceuticals, cosmetics, and pharmaceuticals (Panchaud et al.
2012; Mohanty et al. 2016).
Apart from this, it’s reported that naturally occurring protease enzymes like milk
plasmin degrade proteins and liberate bioactive peptides either during food processing or storage (Meisel and FitzGerald 2003). Microbes in the GI tract can also produce biologically active peptides (Saito 2004). Bovine milk proteins and their
peptides have been isolated and characterized to show several biological activities
(Sanchez and Vazquez 2017). Similarly, milk proteins of non-bovine sources like
camel, goat, sheep, buffalo and yak have also been used to obtain bioactive peptides
(El-Salam and El-Shibiny 2013). Although human milk is the most studied source
of bioactive peptides, milk from animals is also of research interest due to its resemblance to human milk. This makes animal milk a possible alternative for infant
consumption (Atanasova and Ivanova 2010; Bidasolo et al. 2012)
Milk products fermented with many types of bacteria are also capable of generating bioactive peptides. For example, hypertensive subjects were administered with
Lactobacillus helveticus fermented milk containing two biologically active tripeptides Val-Pro-Pro and Ile-Pro-Pro. A reduction in blood pressure was observed
(Nakamura et al. 1995). Furthermore, milk proteins have been hydrolyzed to obtain
β-casomorphins and caseino macro-peptide-derived peptides (from casein), and lactorphins (from whey) which demonstrated ACE-inhibitory, opioid and antimicrobial activities (Sipola et al. 2002; Jakala and Vapaatalo 2010; Boutrou et al. 2015).
Finally, bovine and non-bovine colostrum studies are also documented to release
peptides with bioactivities (Park and Nam 2015).
S. Maqsood et al.