77
(Selamassakul et al. 2016). In vivo, the encoded BAPs can be isolated through gastrointestinal (GI) digestion because of the enzymatic action of certain enzymes such as
trypsin or other microbial enzymes. In vitro, BAPs can be released through food
processing or ripening via microbial enzymes such as in Lactobacillus helveticus
(Dziuba and Dziuba 2014). BAPs have been recognized and separated from animal
and plant sources along with the hydrolysates of several other products (Table 5.1).
5.2.1 Bioactive Peptides from Meat Sources
BAPs isolated from different animal proteins have been noted to possess certain
biological effects (Bhat et al. 2015a, b).
Meat by-products and muscle proteins are a promising source of angiotensinconverting enzyme (ACE) inhibiting peptides with both in vitro and in vivo biological activities for hypertension treatment. Katayama et al. (2007) conducted an
investigation and isolated two new ACE inhibiting peptides from the muscles of pig
via treatment with pepsin. The sequence of the peptides was found to be KRQKYD
and EKERERQ. The IC 50 value for ACE inhibition was found to be at 26.2 and
552.5 μ M for KRQKYD and EKERERQ respectively. KRQKYD was administrated orally to spontaneously hypertensive rats (SHR) at a dose of 10 mg/kg of the
animal weight. Temporary hypotensive activity was observed after 3–6 h of administration (Katayama et al. 2007).
In another study, an antihypertensive peptide was identified by hydrolyzing porcine skeletal myosin with enzymatic activity of pepsin. Protein hydrolysate was first
obtained which was further purified with different chromatographic techniques and
afterwards the peptide sequence was identified to be KRVITY. The IC 50 value of the
peptide was determined to be 6.1 μ M. Additionally, the antihypertensive activity of
KRVITY peptide and VKAGF, which was identified (Ukeda et al. 1992), were
investigated in vivo in rats. Both of the peptides, particularly KRVITY, depicted
remarkable reduction in blood pressure (BP) (Muguruma et al. 2009).
A novel BAP was isolated from hoki frame fish that functions as the retarding
agent for the peroxidation of lipids and acts as a free radical scavenger. It depicted
strong anti-oxidizing action greater than α-tocopherol (Kim et al. 2007). Three
dipeptides i.e. Arg-Try, Lys-Tyr, and Tyr-Tyr isolated from royal jelly fish consisting
of Tyr unit at C-side depicted potent hydrogen peroxide, and hydroxyl-radical scavenging action (Kim et al. 2001a; Wu et al. 2003; Guo et al. 2009). Highly antioxidant peptides were also obtained from the muscle of mackerel, Scomber austriasicus
(Wu et al. 2003) It has been considered that protein hydrolysis of the muscle of
yellow stripe trevally, Selaroides leptolepis, via flavoenzyme release functionally
active bio-peptide (Kim et al. 2001a).
In simulated gut digestion study ACE inhibitory peptides were liberated from
pork meat by means of pepsin and pancreatin. The protein hydrolysate was obtained
first from the digest which was further purified with Reversed Phase High
Performance Liquid Chromatography (RP-HPLC) and characterized by means of
5 Bioactive Peptides and Their Natural Sources
(Selamassakul et al. 2016). In vivo, the encoded BAPs can be isolated through gastrointestinal (GI) digestion because of the enzymatic action of certain enzymes such as
trypsin or other microbial enzymes. In vitro, BAPs can be released through food
processing or ripening via microbial enzymes such as in Lactobacillus helveticus
(Dziuba and Dziuba 2014). BAPs have been recognized and separated from animal
and plant sources along with the hydrolysates of several other products (Table 5.1).
5.2.1 Bioactive Peptides from Meat Sources
BAPs isolated from different animal proteins have been noted to possess certain
biological effects (Bhat et al. 2015a, b).
Meat by-products and muscle proteins are a promising source of angiotensinconverting enzyme (ACE) inhibiting peptides with both in vitro and in vivo biological activities for hypertension treatment. Katayama et al. (2007) conducted an
investigation and isolated two new ACE inhibiting peptides from the muscles of pig
via treatment with pepsin. The sequence of the peptides was found to be KRQKYD
and EKERERQ. The IC 50 value for ACE inhibition was found to be at 26.2 and
552.5 μ M for KRQKYD and EKERERQ respectively. KRQKYD was administrated orally to spontaneously hypertensive rats (SHR) at a dose of 10 mg/kg of the
animal weight. Temporary hypotensive activity was observed after 3–6 h of administration (Katayama et al. 2007).
In another study, an antihypertensive peptide was identified by hydrolyzing porcine skeletal myosin with enzymatic activity of pepsin. Protein hydrolysate was first
obtained which was further purified with different chromatographic techniques and
afterwards the peptide sequence was identified to be KRVITY. The IC 50 value of the
peptide was determined to be 6.1 μ M. Additionally, the antihypertensive activity of
KRVITY peptide and VKAGF, which was identified (Ukeda et al. 1992), were
investigated in vivo in rats. Both of the peptides, particularly KRVITY, depicted
remarkable reduction in blood pressure (BP) (Muguruma et al. 2009).
A novel BAP was isolated from hoki frame fish that functions as the retarding
agent for the peroxidation of lipids and acts as a free radical scavenger. It depicted
strong anti-oxidizing action greater than α-tocopherol (Kim et al. 2007). Three
dipeptides i.e. Arg-Try, Lys-Tyr, and Tyr-Tyr isolated from royal jelly fish consisting
of Tyr unit at C-side depicted potent hydrogen peroxide, and hydroxyl-radical scavenging action (Kim et al. 2001a; Wu et al. 2003; Guo et al. 2009). Highly antioxidant peptides were also obtained from the muscle of mackerel, Scomber austriasicus
(Wu et al. 2003) It has been considered that protein hydrolysis of the muscle of
yellow stripe trevally, Selaroides leptolepis, via flavoenzyme release functionally
active bio-peptide (Kim et al. 2001a).
In simulated gut digestion study ACE inhibitory peptides were liberated from
pork meat by means of pepsin and pancreatin. The protein hydrolysate was obtained
first from the digest which was further purified with Reversed Phase High
Performance Liquid Chromatography (RP-HPLC) and characterized by means of
5 Bioactive Peptides and Their Natural Sources