• Food Science of Animal Resources
• /
• v.43 no.1
• /
• pp.184-194
• /
• 2023

Recently, interest in food-derived bioactive peptides as promising ingredients for the prevention and improvement of hypertension is increasing. The purpose of this study was to determine the structure and antihypertensive effect of an antioxidant peptide purified from velvet antler in a previous study and evaluate its potential as a various bioactive peptide. Molecular weight (MW) and amino acid sequences of the purified peptide were determined by quadrupole time-of-flight electrospray ionization mass spectroscopy. The angiotensin I-converting enzyme (ACE) inhibition activity of the purified peptide was assessed by enzyme reaction methods and in silico molecular docking analysis to determine the interaction between the purified peptide and ACE. Also, antihypertensive effect of the purified peptide in spontaneously hypertensive rats (SHRs) was investigated. The purified antioxidant peptide was identified to be a pentapeptide Asp-Asn-Arg-Tyr-Tyr with a MW of 730.31 Da. This pentapeptide showed potent inhibition activity against ACE (IC₅₀ value, 3.72 μM). Molecular docking studies revealed a good and stable binding affinity between purified peptide and ACE and indicated that the purified peptide could interact with HOH2570, ARG522, ARG124, GLU143, HIS387, TRP357, and GLU403 residues of ACE. Furthermore, oral administration of the pentapeptide significantly reduced blood pressure in SHRs. The pentapeptide derived from enzymatic hydrolysate of velvet antler is an excellent ACE inhibitor. It might be effectively applied as an animal-based functional food ingredient.

• Journal of Dairy Science and Biotechnology
• /
• v.31 no.2
• /
• pp.109-125
• /
• 2013

Recently, functional foods and bioactive components in foods have drawn the attention and interest of food scientists, nutritionists, health professionals, and general consumers. Bioactive whey protein is a highly concentrated milk serum isolate or concentrate, which is high in protein (80~90% protein by weight), carbohydrate- and sugar-free, and nonfat or very low in fat. Bioactive whey protein enhances both healthy and deficient immune systems. In general, ultrafiltered whey protein contains various whey protein concentrate peptides, which could be used for manufacturing probiotics added to health beverages. Hence, the objective of this paper was to review the published literature on research of new functionally improved health beverages using various bioactive components extracted from milk and dairy products.

• Fisheries and Aquatic Sciences
• /
• v.22 no.10
• /
• pp.22.1-22.7
• /
• 2019

The functional peptides from protein hydrolysates of various fishery sources have been identified such as antioxidant activity. The main intention of this study was purification and characterization of antioxidative peptide from black eelpout muscle. The antioxidative peptides were purified from black eelpout (Lycodes diapterus) muscle using different proteases. Antioxidant activity of black eelpout hydrolysates was evaluated using DPPH radical scavenging activity. Among six hydrolysates, the pepsin hydrolysate had the highest antioxidant activity compared to the other hydrolysates. Therefore, it was further purified and a peptide with seven amino acid residues of DLVKVEA (784 Da) was identified by amino acid sequence analysis. The EC₅₀ value for scavenging DPPH radicals by purified peptide was 688.77 μM. Additionally, the purified peptide exhibited protective effect against DNA damage induces by oxidation in mouse macrophages (RAW 264.7 cells). The results of this study suggest that black eelpout muscle protein hydrolysate could potentially contribute to development of bioactive peptides in basic research.

• Journal of Microbiology and Biotechnology
• /
• v.30 no.9
• /
• pp.1387-1394
• /
• 2020

Clam worms (Marphysa sanguinea) are a rich source of bioactive components such as the antibacterial peptide, perinerin. In the present study, we explored the physiological activities of a novel NCWPFQGVPLGFQAPP peptide (NCW peptide), which was purified from clam worm extract through high-performance liquid chromatography. Tandem mass spectrometry (MS/MS) revealed that NCW was a new peptide with a molecular weight of 1757.86 kDa. Moreover, NCW peptide exhibited significant antioxidant effects, causing a 50% inhibition of DPPH radical at a concentration of 20 μM without showing any cytotoxicity. These were associated with a reduction in the activity of catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), and malondialdehyde (MDA) in LPS-stimulated RAW264. 7 cells. Furthermore, NCW peptide exhibited anti-inflammatory effects in LPS-stimulated RAW264.7 macrophages via inhibition of the abnormal production of pro-inflammatory cytokines including nitric oxide (NO), inducible nitric oxide synthase (iNOS), and cyclooxygenase-2 (COX-2). These anti-inflammatory effects of NCW peptide were associated with the inhibition of interleukin-1β (IL-1β) and tumor necrosis factor-α (TNF-α). Our results therefore suggest that this novel NCW peptide with antioxidant and anti-inflammatory effects could be a good therapeutic agent against inflammation-related diseases.

• Biomolecules & Therapeutics
• /
• v.19 no.1
• /
• pp.90-96
• /
• 2011

Automated HPLC/SPE/HPLC coupling experiments using the Sepbox system allowed the rapid identification of four bioactive principles reducing the production of amyloid $\beta$-peptide ($A{\beta}$) from two South African plants, Euclea crispa subsp. crispa and Crinum macowanii. The structures of biologically active compounds isolated from the methanol extract of Euclea crispa subsp. crispa were assigned as 3-oxo-oleanolic acid (1) and natalenone (2) based on their NMR and MS data, while lycorine (3) and hamayne (4) were isolated from the dichloromethane-methanol (1:1) extract of Crinum macowanii. These compounds were shown to inhibit the production of $A{\beta}$ from HeLa cells stably expressing Swedish mutant form of amyloid precursor protein (APPsw).

• KSBB Journal
• /
• v.26 no.6
• /
• pp.483-490
• /
• 2011

Bioactive peptides (BAP) showed excellent cosmetic activity than bio-materials such as caffeic acid (CA), gallic acid (GA), and nicotinic acid (NA). Caffeoyl tripeptide-1 (CT-1) is a BAP that is stabilized with Gly-His-Lys (GHK) tripeptide and CA by using Fmoc solid phase peptide synthesis. Digalloyl tetrapeptide-19 (DT-19) is stabilized by combining Lys-Glu-Cys-Gly with GA and nicotinoyl tripeptide-1 (NT-1) is synthesized by GHK and NA. According to experiments, CT-1 has an excellent anti-oxidant function even with a very small amount of 10 ppm CT-1. DT-19's tyrosinase inhibition activity has the better effect of about 28.57% in 0.01% and 33.33% in 0.005% of concentration and about 7.89% in 0.001% concentration than vitamin-C. In addition, NT-1 is safer than the NA. Almost BAPs like pal-KTTKS, acetyl hexapeptide, and copper tripeptide-1 have the anti-wrinkle effect while DT-19 and NT-1 are applicable for potential BAPs focused on the whitening effect. The three kinds of BAPs like CT-1, DT-19, and NT-1 consisting of amino acids are safe to the skin, and have more excellent stability than bio-materials which are found to be unstable and cause skin irritation. Due to the high biological activity of BAP in the field of skin care, its utilization will increase constantly.

• Korean Journal of Microbiology
• /
• v.50 no.3
• /
• pp.261-263
• /
• 2014

Chronic inflammation is involved in cancers, rheumatoid arthritis, and Crohn's disease. Inerleukin-6 (IL-6) plays major roles in inflammation. Chungkookjang, fermented soybean contains diverse peptides produced by cleavage of soybean proteins. The peptides can be bioactive compounds. Peptide (Gly-Val-Tyr-Tyr-Met-Tyr was purified from Chungkookjang, and modified to be 6mer H, Glu-Val-Tyr-Tyr-Met-Tyr (EVYYMY). Peptide H's activity to suppress IL-6 expression in a human breast cancer cell, MDA-MB-231 was determined. IL-6 Expression was reduced in the cell treated with peptide H 25 times less than controls which were not treated with peptide H. Proliferation of MDA-MB-231 cells was inhibited by peptide H, which is concentration-dependent. Blocking of IL-6 signals is known to be effective in reducing inflammation in rheumatoid arthritis, Crohn's disease, and cancers. Since peptide H can reduce inflammatory IL-6 expression, application of this study will contribute to drug development for diseases which are caused by excessive IL-6.

• Food Science of Animal Resources
• /
• v.35 no.6
• /
• pp.831-840
• /
• 2015

Functionally and physiologically active peptides are produced from several food proteins during gastrointestinal digestion and fermentation of food materials with lactic acid bacteria. Once bioactive peptides (BPs) are liberated, they exhibit a wide variety of physiological functions in the human body such as gastrointestinal, cardiovascular, immune, endocrine, and nervous systems. These functionalities of the peptides in human health and physiology include antihypertensive, antimicrobial, antioxidative, antithrombotic, opioid, anti-appetizing, immunomodulatory and mineral-binding activities.

• Fisheries and Aquatic Sciences
• /
• v.24 no.4
• /
• pp.163-170
• /
• 2021

Peptides are naturally occurring biological molecules that are found in all living organisms. These biologically active peptides play a key role in various biological processes. The aim of this study is the extraction and the purification of bioactive materials that induce relaxation of an apical muscle from the pyloric caeca of Patiria pectinifera. The acidified pyloric caeca extract was partially separated by the solid phase extraction using a stepwise gradient on Sep-Pak C18 cartridge. Among the fractions, materials eluted with 60% methanol/0.1% trifluoroacetic acid was put a thorough of a series of high performance liquid chromatography (HPLC) steps to isolate a neuropeptide with relaxation activity. The purified compound was eluted at 28% acetonitrile in 0.1% trifluoroacetic acid with retention time of 25.8 min on the CAPCELL-PAK C18 reversed-phase column. To determine the molecular weight and the amino acid sequence of the purified peptide, LC-MS and Edman degradation method were used, respectively. The primary structure of the peptide was determined to be FGMGGAYDPLSAGFTD which corresponded to the amino acid sequence of a starfish myorelaxant peptide (SMP) isotype (SMPb) found in the cDNA sequence encoding SMPa and its isotypes. In this study, a muscle relaxant neuropeptide (SMPb) has been isolated from pyloric caeca of starfish P. pectinifera. This is the first report of SMPb isolation on the protein level from P. pectinifera.

• Journal of Dairy Science and Biotechnology
• /
• v.41 no.1
• /
• pp.34-43
• /
• 2023

Hydrolysis of whey-derived proteins using lactic acid bacteria (LAB) utilizes the mass culture method and fermentation of LAB to produce effective bioactive peptides. Whey protein has the biological potential of its precursors, but the active fragments may not be released depending on the hydrolysis method. As an alternative to these problems, the nutritional and bioactive functionality of the hydrolysis method have been reported to be improved using LAB for whey protein. Peptide fractions were obtained using a sample fast protein liquid chromatography device. Antioxidant activity was verified for each of the five fractions obtained. In vitro cell experiments showed no cytotoxicity and inhibited nitric oxide production. Cytokine (IL [interleukin]-1α, IL-6, tumor necrosis factor-α) production was significantly lower than that of lipopolysaccharides (+). As a result of checking the amino acid content ratio of the fractions selected through the AccQ-Tag system, 17 types of amino acids were identified, and the content of isoleucine, an essential amino acid, was the highest. These properties show their applicability for the production of functional products utilizing dietary supplements and milk. It can be presented as an efficient method in terms of product functionality in the production of uniform-quality whey-derived peptides.