Angiotensin-converting enzyme inhibition and free-radical scavenging properties of cationic peptides derived from soybean protein hydrolysates

References

• Aluko RE, Monu E. Functional and bioactive properties of quinoa protein hydrolysates. J Food Sci 2003; 68: 1254–1258
   Web of Science ®Google Scholar
• Ariyoshi Y. Angiotensin-converting enzyme inhibitors derived from food proteins. Trends Food Sci Technol 1993; 4: 139–144
   Web of Science ®Google Scholar
• Chang C-Y, Wu K-C, Chiang S-H. Antioxidant properties and protein compositions of porcine haemoglobin hydrolysates. Food Chem 2007; 100: 1537–1543
   Web of Science ®Google Scholar
• Chen JR, Okada T, Muramoto K, Suetsuna K, Yang SC. Identification of angiotensin I-converting enzyme inhibitory peptides derived from the peptic digest of soybean protein. J Food Biochem 2003; 26: 543–554
   Web of Science ®Google Scholar
• Cushman DW, Cheung HS. Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem Pharmacol 1971; 20: 1637–1648
   PubMed Web of Science ®Google Scholar
• Fujita H, Yokoyama K, Yoshikawa M. Classification and antihypertensive activity of angiotensin I-converting enzyme inhibitory peptides derived from food proteins. J Food Sci 2000; 65: 564–569
   Web of Science ®Google Scholar
• Hernandez-Ledesma B, Amigo L, Ramos M, Recio I. Angiotensin converting enzyme inhibitory activity in commercial fermented products. Formation of peptides under simulated gastrointestinal digestion. J Agric Food Chem 2004; 52: 1504–1510
   PubMed Web of Science ®Google Scholar
• Kamath V, Niketh S, Chandrashekar A, Rajini PS. Chymotryptic hydrolysates of α-kafirin, the storage protein of sorghum (Sorghum bicolor) exhibited angiotensin converting enzyme inhibitory activity. Food Chem 2007; 100: 306–311
   Web of Science ®Google Scholar
• Katayama K, Fuchu H, Sakata A, Kawahara S, Yamauchi K, Kawamura Y, Muguruma M. Angiotensin I-converting enzyme inhibitory activities of porcine skeletal muscle proteins following enzyme digestion. Asian–Aust J Anim Sci 2003; 16: 417–424
   Google Scholar
• Kohama Y, Matsumoto S, Oka H, Teramoto T, Okabe M, Mimura Y. Isolation of angiotensin-converting enzyme-inhibitor from tuna muscle. Biochem Biophys Res Commun 1988; 155: 332–337
   PubMed Web of Science ®Google Scholar
• Korhonen H, Pihlanto-Leppälä A, Rantamäki P, Tupasela T. Impact of processing on bioactive proteins and peptides. Trends Food Sci Technol 1998; 9: 307–319
   Web of Science ®Google Scholar
• Li H, Aluko RE. Kinetics of the inhibition of calcium/calmodulin-dependent protein kinase II by pea protein-derived peptides. J Nutr Biochem 2005; 16: 656–662
   PubMed Web of Science ®Google Scholar
• Li H, Aluko RE. Structural modulation of calmodulin and calmodulin-dependent protein kinase II by pea protein hydrolysates. Int J Food Sci Nutr 2006; 57: 178–189
   PubMed Web of Science ®Google Scholar
• Lo WM, Li-Chan EC. Angiotensin I converting enzyme inhibitory peptides from in vitro pepsin-pancreatin digestion of soy protein. J Agric Food Chem 2005; 53: 3369–3376
   PubMed Web of Science ®Google Scholar
• Markwell MAC, Haas SM, Biebar LL, Tolbert NE. A modification of the Lowry procedure to simplify protein determination in membrane and in protein samples. Anal Biochem 1978; 87: 206–211
   PubMed Web of Science ®Google Scholar
• Matsui T, Li CH, Osajima Y. Preparation and characterization of novel bioactive peptides responsible for angiotensin I-converting enzyme inhibition from wheat germ. J Pept Sci 1999; 5: 289–297
   PubMed Web of Science ®Google Scholar
• Meisel H. Multifunctional peptides encrypted in milk proteins. Biofactors 2004; 21: 55–61
   PubMed Web of Science ®Google Scholar
• Miyoshi S, Ishikawa H, Kaneko T, Fukui F, Tanaka H, Maruyama S. Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate. Agric Biol Chem 1991; 55: 1313–1318
   PubMed Web of Science ®Google Scholar
• Nakano D, Ogura K, Miyakoshi M, Ishii F, Kawanishi H, Kurumazuka D, Kwak C, Ikemura K, Takaoka M, Moriguchi S, et al. Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides from sesame protein hydrolysate in spontaneously hypertensive rats. Biosci Biotechnol Biochem 2006; 70: 1118–1126
   PubMed Web of Science ®Google Scholar
• Ono S, Hosokawa M, Miyashita K, Takahashi K. Isolation of peptides with angiotensin I-converting enzyme inhibitory effect derived from hydrolysate of upstream chum salmon muscle. J Food Sci 2003; 68: 1611–1614
   Web of Science ®Google Scholar
• Schmaier AH. The plasma kallikrein–kinin system counterbalances the renin–angiotensin system. J Clin Invest 2002; 109: 1007–1009
   PubMed Web of Science ®Google Scholar
• Seki E, Osajima K, Matsufuji H, Matsui T, Osajima Y. Val-Tyr, an angiotensin-I converting enzyme-inhibitor from sardines that have resistance to gastrointestinal proteases. J Jpn Soc Biosci Biotechol Agrochem 1995; 69: 1013–1020
   Google Scholar
• Seppo L, Jauhiainen T, Poussa T, Korpela R. A fermented milk high in bicactive peptides has a blood pressure-lowering effect in hypertensive subjects. Am J Clin Nutr 2003; 77: 326–330
   PubMed Web of Science ®Google Scholar
• Wu J, Ding X. Hypotensive and physiological effect of angiotensin converting enzyme inhibitory peptides derived from soy protein on spontaneously hypertensive rats. J Agric Food Chem 2001; 49: 501–506
   PubMed Web of Science ®Google Scholar
• Yamamoto N. Antihypertensive peptides derived from food proteins. Biopolymers 1997; 43: 129–134
   PubMed Web of Science ®Google Scholar
• Yu Y, Hu J, Bai X, Du Y, Lin B. Preparation and function of oligopeptide-enriched hydrolysate from globin by pepsin. Process Biochem 2006; 41: 1589–1593
   Google Scholar
• Zhu K, Zhou H, Qian H. Antioxidant and free radical-scavenging activities of wheat germ protein hydrolysates (WGPH) prepared with alcalase. Process Biochem 2006; 41: 1296–1302
   Web of Science ®Google Scholar