80
Matrix-Assisted Laser Desorption/Ionization-Time of Flight Mass Spectrometer
(MALDI-TOF/TOF MS). In this study 22 different peptides were evaluated in vitro
for ACE inhibition. Among all of them peptides with sequences PTPVP and KAPVA
showed the highest bioactivity with IC 50 values of 256.41 and 46.56 μ M respectively (Escudero et al. 2010).
In one study, BAPs were isolated from chicken dark meat. The isolated peptides were evaluated against hypochlorite ions and peroxyl radicals for their antioxidant potential. The isolated peptides were purified with High-Performance
Liquid Chromatography (HPLC). One of the peptides exhibited remarkable antioxidant activity when evaluated against the peroxyl radical. This amino acid
sequence of the peptide was determined, and the first five amino acids were found
to be YASGR which correspond to amino acid number 143–147 of chicken β-actin
(Fukada et al. 2016).
ACE inhibitory peptide was separated from the dark muscle of tuna (Thunnus
obesus) hydrolysate. The hydrolysate was prepared by treating the muscle with the
enzyme alcalase, neutrase, pepsin, papain, alpha-chymotrypsin, and trypsin, respectively. Amongst all the hydrolysates, the hydrolysate of pepsin showed the maximum ACE inhibitory ability. The peptides obtained from fish also depicted
antihypertensive action. The study concluded that the peptide obtained from the
dark muscle of tuna can serve as useful element for pharmaceuticals and functional
food against hypertension and related ailments (Qian et al. 2007).
Four different peptides with the sequence FHG, DFHING, GFHI and
GLSDGEWQ were isolated from beef sarcoplasmic proteins via commercial
enzymes. The peptides depicted remarkable antihypertensive activities. The IC 50
values of the peptides against ACE inhibition was determined to be 52.9(FHG),
64.3(DFHING), 117(GFHI) and 50.5(GLSDGEWQ) μ g/ml. The peptides were
also investigated for their antimicrobial potential. For this purpose, different bacterial strains such as Escherichia coli, Listeria monocytogenes, Pseudomonas aeruginosa, Staphylococcus aureus, Salmonella typhimurium, and Bacillus cereus were
used. The peptides not only showed antimicrobial activity against at least one of the
above microorganisms but also exhibited cytotoxic effects against carcinogenic
cells (Jang et al. 2008).
Porcine liver was studied for the generation of BAPs. Two potential ACE inhibitors were isolated from protein hydrolysates of the porcine liver. The IC 50 values of
the peptides were found to be at 0.31 and 0.18 mg/ml. Oral administration of the
peptides in SHR indicated significant reduction in the blood pressure of the animal.
The study concluded that both of the peptides have ACE inhibiting and antioxidant
abilities along with the property of lowering the blood pressure (Inoue et al. 2013).
Blood is a remarkable source of proteins and signifies an amazing source of
BAP. Though disposal of blood is a huge problem for meat handlers and because of
this the “serum albumin”, a major blood protein has garnered little interest. In a
study, conducted by Arrutia et al., serum albumin was hydrolyzed via enzymatic
action of trypsin. A biologically active sequence of the peptide was obtained. This
bioactive peptide when evaluated showed the following activities: ACE inhibition
K. Mustafa et al.
Matrix-Assisted Laser Desorption/Ionization-Time of Flight Mass Spectrometer
(MALDI-TOF/TOF MS). In this study 22 different peptides were evaluated in vitro
for ACE inhibition. Among all of them peptides with sequences PTPVP and KAPVA
showed the highest bioactivity with IC 50 values of 256.41 and 46.56 μ M respectively (Escudero et al. 2010).
In one study, BAPs were isolated from chicken dark meat. The isolated peptides were evaluated against hypochlorite ions and peroxyl radicals for their antioxidant potential. The isolated peptides were purified with High-Performance
Liquid Chromatography (HPLC). One of the peptides exhibited remarkable antioxidant activity when evaluated against the peroxyl radical. This amino acid
sequence of the peptide was determined, and the first five amino acids were found
to be YASGR which correspond to amino acid number 143–147 of chicken β-actin
(Fukada et al. 2016).
ACE inhibitory peptide was separated from the dark muscle of tuna (Thunnus
obesus) hydrolysate. The hydrolysate was prepared by treating the muscle with the
enzyme alcalase, neutrase, pepsin, papain, alpha-chymotrypsin, and trypsin, respectively. Amongst all the hydrolysates, the hydrolysate of pepsin showed the maximum ACE inhibitory ability. The peptides obtained from fish also depicted
antihypertensive action. The study concluded that the peptide obtained from the
dark muscle of tuna can serve as useful element for pharmaceuticals and functional
food against hypertension and related ailments (Qian et al. 2007).
Four different peptides with the sequence FHG, DFHING, GFHI and
GLSDGEWQ were isolated from beef sarcoplasmic proteins via commercial
enzymes. The peptides depicted remarkable antihypertensive activities. The IC 50
values of the peptides against ACE inhibition was determined to be 52.9(FHG),
64.3(DFHING), 117(GFHI) and 50.5(GLSDGEWQ) μ g/ml. The peptides were
also investigated for their antimicrobial potential. For this purpose, different bacterial strains such as Escherichia coli, Listeria monocytogenes, Pseudomonas aeruginosa, Staphylococcus aureus, Salmonella typhimurium, and Bacillus cereus were
used. The peptides not only showed antimicrobial activity against at least one of the
above microorganisms but also exhibited cytotoxic effects against carcinogenic
cells (Jang et al. 2008).
Porcine liver was studied for the generation of BAPs. Two potential ACE inhibitors were isolated from protein hydrolysates of the porcine liver. The IC 50 values of
the peptides were found to be at 0.31 and 0.18 mg/ml. Oral administration of the
peptides in SHR indicated significant reduction in the blood pressure of the animal.
The study concluded that both of the peptides have ACE inhibiting and antioxidant
abilities along with the property of lowering the blood pressure (Inoue et al. 2013).
Blood is a remarkable source of proteins and signifies an amazing source of
BAP. Though disposal of blood is a huge problem for meat handlers and because of
this the “serum albumin”, a major blood protein has garnered little interest. In a
study, conducted by Arrutia et al., serum albumin was hydrolyzed via enzymatic
action of trypsin. A biologically active sequence of the peptide was obtained. This
bioactive peptide when evaluated showed the following activities: ACE inhibition
K. Mustafa et al.