81
activity, Dipeptidyl peptidase-4 inhibitor (DPP-IV) inhibition and antioxidant activity (Arrutia et al. 2016a).
A study reported the antioxidant activity of peptides isolated from hydrolysates
of porcine myofibrillar proteins, these peptides were generated by the action of
actinase E or papain and was further purified by Ion Exchange Chromatography
(IEC). The antioxidant activity of the peptide was determined with, DPPH radical
scavenging activity, linoleic acid peroxidation system and metal-chelating activity
assays. The investigation reported five antioxidant peptides with the following
sequences EELDNALN, IEAEGE, DSGVT, VPSIDDQEELM and DAQEKLE. The
peptide with the sequence DAQEKLE from actin protein, exhibited the maximum
antioxidant activity (Saiga et al. 2003).
From the above discussion it is evident that meat from different animal sources
such as mammals, birds, fishes provide a variety of BAPs. The BAPs isolated from
the meat proteins and hydrolysates possess wide-ranging biological activities such
as antihypertensive activity, anti-oxidant activity, antimicrobial activity and certain
enzyme inhibition activity.
5.2.2 Bioactive Peptides from Dairy Sources
Bovine milk, dairy goods, and cheese are the dominant sources of BAPs and bioactive proteins among food sources (Mohanty et al. 2016). Apparently, this may be the
reason of why milk is essential beyond nourishment in the early months of the life
(Moller et al. 2008). Milk proteins have a wide range of biological abilities. For
example, lactoferrin (Lf) exhibits antimicrobial activity where immunoglobulins
have an immune-protective influence. A small number of hormones and certain
growth factors are present in colostrum, which play significant roles in post-natal
development (Park and Nam 2015).
Milk proteins are packed with BAPs, these peptides are separated during food
processing or gastrointestinal digestion (Meisel and FitzGerald 2003). In an investigation, opioid peptide was separated from dairy products, these peptides have
promising pharmacological properties analogous to morphine hence relevant in
some central nervous system (CNS) problems (Haque et al. 2008).
HPLC-MS and tandem mass spectrometry (MS-MS), were used to separate a
different BAP from milk of human mothers of pre- and full-term infants. The isolated peptides were of varying molecular weight such as opioid and phosphopeptides. The isolation of several peptides from human milk confirms that human
milk is susceptible to greater casein proteolysis compared to bovine milk. The
results of the study strengthen the significance of maternal milk for the infants
(Ferranti et al. 2004).
Lactoferrin (Lf), is the milk protein of all mammals. It is glycoprotein in nature
and is known for its iron-binding properties. Other than remarkable iron binding
properties it also depicts antimicrobial and immunomodulating abilities. Peptides
derived from Lf showed remarkable antihypertensive activities. Both Lf and peptides
5 Bioactive Peptides and Their Natural Sources
activity, Dipeptidyl peptidase-4 inhibitor (DPP-IV) inhibition and antioxidant activity (Arrutia et al. 2016a).
A study reported the antioxidant activity of peptides isolated from hydrolysates
of porcine myofibrillar proteins, these peptides were generated by the action of
actinase E or papain and was further purified by Ion Exchange Chromatography
(IEC). The antioxidant activity of the peptide was determined with, DPPH radical
scavenging activity, linoleic acid peroxidation system and metal-chelating activity
assays. The investigation reported five antioxidant peptides with the following
sequences EELDNALN, IEAEGE, DSGVT, VPSIDDQEELM and DAQEKLE. The
peptide with the sequence DAQEKLE from actin protein, exhibited the maximum
antioxidant activity (Saiga et al. 2003).
From the above discussion it is evident that meat from different animal sources
such as mammals, birds, fishes provide a variety of BAPs. The BAPs isolated from
the meat proteins and hydrolysates possess wide-ranging biological activities such
as antihypertensive activity, anti-oxidant activity, antimicrobial activity and certain
enzyme inhibition activity.
5.2.2 Bioactive Peptides from Dairy Sources
Bovine milk, dairy goods, and cheese are the dominant sources of BAPs and bioactive proteins among food sources (Mohanty et al. 2016). Apparently, this may be the
reason of why milk is essential beyond nourishment in the early months of the life
(Moller et al. 2008). Milk proteins have a wide range of biological abilities. For
example, lactoferrin (Lf) exhibits antimicrobial activity where immunoglobulins
have an immune-protective influence. A small number of hormones and certain
growth factors are present in colostrum, which play significant roles in post-natal
development (Park and Nam 2015).
Milk proteins are packed with BAPs, these peptides are separated during food
processing or gastrointestinal digestion (Meisel and FitzGerald 2003). In an investigation, opioid peptide was separated from dairy products, these peptides have
promising pharmacological properties analogous to morphine hence relevant in
some central nervous system (CNS) problems (Haque et al. 2008).
HPLC-MS and tandem mass spectrometry (MS-MS), were used to separate a
different BAP from milk of human mothers of pre- and full-term infants. The isolated peptides were of varying molecular weight such as opioid and phosphopeptides. The isolation of several peptides from human milk confirms that human
milk is susceptible to greater casein proteolysis compared to bovine milk. The
results of the study strengthen the significance of maternal milk for the infants
(Ferranti et al. 2004).
Lactoferrin (Lf), is the milk protein of all mammals. It is glycoprotein in nature
and is known for its iron-binding properties. Other than remarkable iron binding
properties it also depicts antimicrobial and immunomodulating abilities. Peptides
derived from Lf showed remarkable antihypertensive activities. Both Lf and peptides
5 Bioactive Peptides and Their Natural Sources