Antioxidative peptides from food proteins: A review.
Bahareh H. Sarmadia, Amin Ismail. Peptides, 2010, 31(10): 1949–1956.
Bioactive peptides, as products of hydrolysis of diverse food proteins, are the focus of current research. They exert various biological roles, one of the most crucial of which is the antioxidant activity. Reverse relationship between antioxidant intake and diseases has been approved through plenty of studies. Antioxidant activity of bioactive peptides can be attributed to their radical scavenging, inhibition of lipid peroxidation and metal ion chelation properties of peptides. It also has been proposed that peptide structure and its amino acid sequence can affect its antioxidative properties. This paper reviews bioactive peptides from food sources concerning their antioxidant activities. Additionally, specific characteristics of antioxidative bioactive peptides, enzymatic production, methods to evaluate antioxidant capacity, bioavailability, and safety concerns of peptides are reviewed.
Bioactive peptides derived from food proteins preventing lifestyle-related diseases.
Masaaki Yoshikawa, Hiroyuki Fujita, Nobuyuki Matoba, Yasuyuki Takenaka, Taichi Yamamoto, Rena Yamauchi, Hirotaka Tsuruki, Kyoya Takahata. BioFactors, 2000, 12(1-4): 143–146.
Many kinds of bioactive peptides which might prevent lifestyle-related diseases are released from food proteins after enzymatic digestion. Inhibitory peptides for angiotensin I-converting enzyme (ACE) having anti-hypertensive effect have been isolated from enzymatic digests of various food proteins. LKPNM, which was isolated from the thermolysin digest of dried bonito was activated 8-fold by ACE itself and showed a prolonged effect after oral administration. Two vasorelaxing peptides, ovokinin and ovokinin(2--7), showing antihypertensive effect after oral administration were obtained from ovalbumin digests. We found that low molecular weight peptides derived from food proteins lowered serum cholesterol without increasing excretion of cholesterol and bile acids. An immunostimulating peptide isolated from an enzymatic digest of soybean protein prevented alopecia induced by cancer chemotherapy.
The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease.
Kati Erdmann, Belinda W.Y. Cheung, Henning Schröder. The Journal of Nutritional Biochemistry, 2008, 19(10): 643–654.
Vascular diseases such as atherosclerosis, stroke or myocardial infarction are a significant public health problem worldwide. Attempts to prevent vascular diseases often imply modifications and improvement of causative risk factors such as high blood pressure, obesity, an unfavorable profile of blood lipids or insulin resistance. In addition to numerous preventive and therapeutic drug regimens, there has been increased focus on identifying dietary compounds that may contribute to cardiovascular health in recent years. Food-derived bioactive peptides represent one such source of health-enhancing components. They can be released during gastrointestinal digestion or food processing from a multitude of plant and animal proteins, especially milk, soy or fish proteins. Biologically active peptides are considered to promote diverse activities, including opiate-like, mineral binding, immunomodulatory, antimicrobial, antioxidant, antithrombotic, hypocholesterolemic and antihypertensive actions. By modulating and improving physiological functions, bioactive peptides may provide new therapeutic applications for the prevention or treatment of chronic diseases. As components of functional foods or nutraceuticals with certain health claims, bioactive peptides are of commercial interest as well. The current review centers on bioactive peptides with properties relevant to cardiovascular health.
Angiotensin I-converting enzyme inhibitory activity of low-molecular-weight peptides from Atlantic salmon (Salmo salar L.) skin.
Rui-Zeng Gu, Chen-Yue Li, Wen-Ying Liu, Wei-Xue Yi, Mu-Yi Cai. Food Research International 2011, 44(5): 1536–1540.
Collagen extracted from Atlantic salmon (Salmo salar L.) skin (which is normally discarded in the process of manufacture) was hydrolyzed with Alcalase and papain, and treated by multistage separation. The salmon skin collagen peptides (SSCP) obtained had high protein content (91.20±1.03%) and low molecular weights, 90.79% of which were less than 1000 Da. SSCP was then separated by reversed-phase high performance liquid chromatography. Eleven major fractions were collected and their angiotensin I-converting enzyme (ACE) inhibitory activitywas assayed. Fractions 5 and 7 displaying higherACE inhibitory activitywere subjected tomass spectrometer to identify the ACE inhibitory peptides. A total of eleven peptide sequenceswere identified, and two dipeptides, Ala-Pro and Val-Arg, were selected for further ACE inhibitory activity analysis. The ACE inhibitory activities of Ala-Pro (IC50=0.060±0.001 mg/ml) and Val-Arg (IC50=0.332±0.005 mg/ml) were found to be approximately 20- and 4-fold higher than that of SSCP (1.165±0.087 mg/ml), respectively.
Pilot-scale production of low molecular weight peptides from corn wet milling byproducts and the antihypertensive effects in vivo and in vitro.
A pilot-scale production was developed to enhance the value of proteins from corn gluten meal (CGM). Corn protein isolate (CPI) with high protein content (90.68%) was obtained through heat treatment of CGM (150 kg) in aqueous alkaline solution. Two-step enzymatic hydrolysis and multistage separation were applied to enrich corn oligopeptides (COP) with low molecular weights, 96.77% of which were less than 1000 Da. The greatest antihypertensive effect of COP treatment in spontaneously hypertensive rats (SHR) was observed at a dose of 0.45 g/kg. One major ACE-inhibitory peptide, Ala-Tyr, was identified and quantified (9.16 ± 0.08 mg/g) from COP. The ACE inhibitory activity of Ala-Tyr (IC50 = 0.037 mg/ml) was over 27 times higher than that of COP (IC50 = 1.020 mg/ml). The results indicate that COP may be a source of natural antihypertensive compounds that could be used for drugs or functional food ingredients.
Gluten exorphin C: A novel opioid peptide derived from wheat gluten.
A novel opioid peptide, Tyr-Pro-Ile-Ser-Leu, was isolated from the pepsin-trypsin-chymotrypsin digest of wheat gluten. Its IC50 values were 40 μM and 13.5 μM in the GPI and MVD assays, respectively. This peptide was named gluten exorphin C. Gluten exorphin C had a structure quite different from any of the endogenous and exogenous opioid peptides ever reported in that the N-terminal Tyr was the only aromatic amino acid. The analogs containing Tyr-Pro-X-Ser-Leu were synthesized to study its structure-activity relationship. Peptides in which X was an aromatic amino acid or an aliphatic hydrophobic amino acid had opioid activity.