In vitro cytotoxic and ACE-inhibitory activities of promod 278P hydrolysate of ovotransferrin from chicken egg white.
Peptides released from egg proteins via enzymatic hydrolysis show various bioactivities such as antimicrobial, antioxidant, antihypertensive, and immunomodulatory properties. The objective of this study was to investigate the cytotoxic and Angiotensin Converting Enzyme (ACE)-inhibitory activities of ovotransferrin and its promod 278P enzyme hydrolysate. Ovotransferrin from egg white was hydrolyzed using promod 278P at 45°C for 3 hours. Using the MTT assay, the cytotoxicity of ovotransferrin and promod 278P hydrolysate of ovotransferrin were evaluated in human cancer cell lines of various tissue origins. The ACE-inhibitory activity was determined using the cleavage of a chromogenic substrate -Hip-His-Leu. The promod 278P hydrolysate of ovotransferrin showed a potent cytotoxicity (>90%) at 20 mg/mL in all cancer cell lines tested, but ovotransferrin did not. The IC50 value of the promod 278P hydrolysate of ovotransferrin against 5 different cancer cells were 10.05 ± 1.55, 3.45 ± 0.94, 4.43 ± 1.87, 4.92 ± 0.63, and 10.43 ± 3.91 mg/mL for MCF-7, HeLa, HepG2, HT-29, and LoVo cells, respectively. The promod 278P hydrolysate of ovotransferrin showed a strong ACE-inhibiting activity: at 10 mg/mL level, the hydrolysate showed 76.82 ± 1.28% inhibition to ACE-inhibitory activity, and 73.33 ± 2.56%, 56.85 ± 1.84%, 50.32 ± 3.71%, 17.30 ± 0.13%, and 4.52 ± 6.83% inhibitory activity at 5, 2.5, 1.25, 0.625, and 0.3125 mg/mL level, respectively. The IC50 value of the promod 278P hydrolysate of ovotransferrin was 1.53 ± 0.20 mg/mL. However, ovotransferrin did not show any inhibitory effect to angiotensin-converting enzyme activity. This result indicated that the promod 278P hydrolysate of ovotransferrin has a great potential as an anticancer and antihypertension agent for humans, but the information on the peptides responsible for the functional activities is not available yet.
Department of Animal Science, Iowa State University, Ames, Iowa 50011.
S H
SH
Moon
Department of Food Science and Biotechnology of Animal Resources, Konkuk University, Seoul 143-701, Korea.
J H
JH
Lee
Department of Animal Science, Iowa State University, Ames, Iowa 50011.
J H
JH
Kim
Department of Food Science and Biotechnology of Animal Resources, Konkuk University, Seoul 143-701, Korea.
H-D
HD
Paik
Department of Animal Science, Iowa State University, Ames, Iowa 50011.
D U
DU
Ahn
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000494:pharmacology*; D000818:Animals; D000959:Antihypertensive Agents / Q000494:pharmacology*; D045744:Cell Line, Tumor; D002645:Chickens; D003207:Conalbumin / Q000737:chemistry / Q000494:pharmacology*; D003603:Cytotoxins / Q000737:chemistry / Q000494:pharmacology*; D004527:Egg Proteins / Q000737:chemistry; D004529:Egg White / Q000737:chemistry*; D006801:Humans; D009842:Oligopeptides; D010455:Peptides / Q000737:chemistry; D011492:Protein Hydrolysates / Q000494:pharmacology*
D000806:Angiotensin-Converting Enzyme Inhibitors; D000959:Antihypertensive Agents; D003603:Cytotoxins; D004527:Egg Proteins; D009842:Oligopeptides; D010455:Peptides; D011492:Protein Hydrolysates; D003207:Conalbumin; C010980:hippuryl-histidyl-leucine
ACE-inhibiting activity; anticancer activity; cytotoxicity; hydrolysate; ovotransferrin