Abstract
The aim of this study was to determine the antihypertensive effects of enzymatic hemp seed protein hydrolysate (HPH) and its peptide fractions. Hemp seed protein isolate was digested by the sequential action of pepsin and pancreatin to mimic gastrointestinal digestion in human beings. The resultant HPH was separated by membrane ultrafiltration into peptide fractions with different sizes (<1 and 1–3 kDa). The HPH led to significantly higher (P < 0.05) in vitro inhibition of the activities of angiotensin I-converting enzyme (ACE) and renin, the two main enzymes involved in abnormal blood pressure elevation (hypertension). Kinetic studies showed that HPH and peptide fractions inhibited renin and ACE activities in a mixed-type pattern, indicating binding to areas other than the active site. Oral administration of HPH (200 mg/kg body weight) to spontaneously hypertensive rats led to significant reductions (P < 0.05) in systolic blood pressure (SBP) that reached a maximum of −30 mmHg after 8 h. In contrast, the hypotensive effects of peptide fractions (<1 and 1–3 kDa) had a maximum value of about −15 mmHg after 6–8 h post oral administration. The results suggest a synergistic antihypertensive effect of the peptides present within HPH; this effect was reduced significantly (P < 0.05) upon separation into peptide fractions.
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Hong F, Ming L, Yi S, Zhanxia L, Yongquan W, Chi L (2008) The antihypertensive effect of peptides: A novel alternative to drugs? Peptides 29:1062–1071
Aluko RE (2008) Antihypertensive properties of plant-derived inhibitors of angiotensin I-converting enzyme activity: a review. Recent Prog Med Plants 22:541–561
Atkinson AB, Robertson JIS (1979) Captopril in the treatment of clinical hypertension and cardiac. Lancet 314:836–839
Lahogue V, Rehel K, Taupin L, Haras D, Allaume P (2010) A HPLC-UV method for the determination of angiotensin I-converting enzyme (ACE) inhibitory activity. Food Chem 118:870–875
Erdmann K, Cheung BLY, Schroder H (2008) The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. J Nutr Biochem 19:643–654
Wang XS, Tang CH, Chen L, Yang XQ (2009) Characterization and antioxidant properties of hemp protein hydrolysate obtained with neutrase. Food Technol Biotechnol 47:428–434
Tang CH, Ten Z, Wang XS, Yang XQ (2006) Physicochemial and functional properties of hemp (Cannabis sativa L.) protein isolate. J Agric Food Chem 54:8945–8950
Wang XS, Tang CH, Yang XQ, Gao WR (2008) Characterization amino acid composition and in vitro digestibility of hemp (Cannabis sativa L.) proteins. Food Chem 107:11–18
House JD, Neufeld J, Leson G (2010) Evaluating the quality of protein from hemp seed (Cannabis sativa L.) products through the use of the protein digestibility-corrected amino acid score method. J Agric Food Chem 58:11801–11807
Pihlanto LA, Koskinen P, Piilola K, Tupasela T, Korhonen H (2000) Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides. J Diary Res 67:53–64
Girgih, AT, Udenigwe CC, Aluko RE (2011) In vitro antioxidant properties of hemp seed (Cannabis sativa L.) protein hydrolysate fractions. J Am Oil Chem Soc 88:381–389
FitzGerald RJ, Murray BA, Walsh DJ (2004) Hypotensive peptides from milk proteins. J Nutr 134:9805–9885
Udenigwe CC, Lin YS, Hou WC, Aluko RE (2009) Kinetics of the inhibition of renin and angiotensin I-converting by flaxseed protein hydrolysate fractions. J Funct Foods 1:199–207
Segall L, Covic A, Goldsmith DJA (2007) Direct renin inhibitors: the dawn of a new era, or just a variation on the theme? Nephrol. Dial Transplant 22:2435–2439
Li H, Aluko RE (2010) Identification and inhibitory properties of multifunctional peptides from pea protein hydrolysate. J Agric Food Chem 58:11471–11476
Markwell MAC, Haas SM, Biebar LL, Tolbert NE (1978) A modification of lowry procedure to simplify protein determination in membrane and protein samples. Anal Biochem 87:206–211
Adler-Nissen J (1979) Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J Agric Food Chem 27:1256–1262
Li H, Aluko RE (2005) Kinetics of the inhibition of calcium/calmodulin-dependent protein kinase II by pea protein-derived peptides. J Nutr Biochem 16:656–662
Aukema HM, Gauthier J, Jia Y, Roy M, Li H, Aluko RE (2011). Distinctive effects of plant protein sources on renal disease progression and associated cardiac hypertrophy in experimental kidney disease. Mol Nutr Food Res. doi: 10.1002/mnfr.201000558
Giménez B, Alemán A, Montero P, Gómez-Guillén MC (2009) Antioxidant and functional properties of gelatin hydrolysates obtained from skin of sole and squid. Food Chem 114:976–983
Yin SW, Tang CH, Cao JS, Wen HuEK, QB YangXQ (2008) Effects of limited enzymatic hydrolysis with trypsin on functional properties of hemp (Cannabis sativa L.) protein isolate. Food Chem 106:1004–1013
Barbana C, Boye JI (2010) Angiotensin I-converting enzyme inhibitory activity of chickpea and pea protein hydrolysates. Food Res Int 43:1642–1649
Shahidi F, Han X-Q, Synowiecki J (1995) Production and characteristics of protein hydrolysates from capelin (Mallotus villosus). Food Chem 53:285–293
Benjakul S, Morrissey MT (1997) Protein hydrolysates from pacific whiting solid wastes. J Agric Food Chem 45:3423–3430
Roberts PR, Burney JD, Black KW, Zaloga GP (1999) Effect of chain length on absorption of biologically active peptides from the gastrointestinal tract. Digestion 60:332–337
Haque E, Chand R (2008) Antihypertensive and antimicrobial bioactive peptides from milk proteins. Eur Food Res Technol 277:7–15
Belem MAF, Gibbs BF, Lee BH (1999) Proposing sequences for peptides derived from whey fermentation with potential bioactive sites. J Diary Sci 82:486–493
Jeon Y-J, Byun H-G, Kim S-K (1999) Improvement of functional properties of cod frame protein hydrolysates using ultrafiltration membranes. Process Biochem 35:471–478
Wu J, Aluko RE, Nakai S (2006) Structural requirements of angiotensin I-converting enzyme inhibitory peptides: quantitative structure-and-activity relationship study of di- and tri-peptides. J Agric Food Chem 54:732–738
Stanton A (2003) Potential of renin inhibition in cardiovascular disease. J Renin Angiotensin Aldosterone Syst 4:6–10
Qian ZJ, Je JY, Kim SK (2007) Antihypertensive effect of angiotensin I-converting enzyme-inhibitory peptide from hydrolysates of bigeye tuna dark muscle, Thunnus obesus. J Agric Food Chem 55:8398–8403
Lee S-H, Qian Z-J, Kim S-K (2010) A novel angiotensin I converting enzyme inhibitory peptide from tuna frame protein hydrolysate and its antihypertensive effect in spontaneously hypertensive rats. Food Chem 118:96–102
Wang J, Hu J, Cui J, Bai X, Du Y, Miyaguchi Y, Lin B (2008) Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats. Food Chem 111:302–308
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This work was funded through a Discovery Grant from the Natural Sciences and Engineering Research Council of Canada (NSERC) to R.E.A.
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Girgih, A.T., Udenigwe, C.C., Li, H. et al. Kinetics of Enzyme Inhibition and Antihypertensive Effects of Hemp Seed (Cannabis sativa L.) Protein Hydrolysates. J Am Oil Chem Soc 88, 1767–1774 (2011). https://doi.org/10.1007/s11746-011-1841-9
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DOI: https://doi.org/10.1007/s11746-011-1841-9