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This current study aims to analyze the potential bioactivities possessed by the enzymatic hydrolysates of commercial bovine, porcine, and tilapia gelatins using bioinformatics in combination with in vitro and in vivo studies. The hydrolysate with superior inhibition of angiotensin converting enzyme (ACE) activity was used to treat the D-galactose (DG)-induced amnesic mice. In silico digestion of the gelatins led to the identification of peptide sequences with potential antioxidant, ACE-inhibitory, and anti-amnestic properties. The results of in vitro digestion revealed that the <1 kDa peptide fraction of porcine gelatin hydrolysate obtained after 1 h digestion with papain (PP) (PP1, <1 kDa) potently inhibited ACE, acetylcholinesterase, and prolyl endopeptidase activities at 87.42%, 21.24%, and 48.07%, respectively. Administering the PP1 to DG-induced amnesic mice ameliorated the spatial cognitive impairment and Morris water maze learning abilities. The dentate area morphology in the PP1-treated mice was relatively similar to the control group. In addition, PP1 enhanced the antioxidant capacity in the DG-induced amnesic mice. This study suggests that PP1 could serve as a potential treatment tool against oxidative stress, hypertension, and neurodegenerative diseases. [ABSTRACT FROM AUTHOR]

Fava beans, renowned for their nutritional value and sustainable cultivation, are pivotal in various food applications. This study examined the implications of varying the particle size on the functional, physicochemical, and in vitro digestibility properties of fava bean flour. Fava bean was milled into 0.14, 0.50, and 1.0 mm particle sizes using a Ferkar multipurpose knife mill. Physicochemical analyses showed that the 0.14 mm flour had more starch damage, but higher protein and fat contents. Functionality assessments revealed that the finer particle sizes had better foaming properties, swelling power, and gelation behavior than the coarse particle size. Emulsion capacity showed that for all the pH conditions, 1.00 mm particle size flour had a significantly higher (p < 0.05) oil droplet size, while the 0.5 and 0.14 mm flours had smaller and similar oil droplet sizes. Moreover, in vitro digestibility assays resulted in improved starch digestion (p ˂ 0.05) with the increase in flour particle size. Varying the particle size of fava bean flour had less impact on the in vitro digestibility of the bread produced from wheat–fava bean composite flour, with an average of 84%. The findings underscore the critical role of particle size in tailoring fava bean flour for specific culinary purposes and nutritional considerations. [ABSTRACT FROM AUTHOR]

Yellow field peas (Pisum sativum L.) hold significant value for producers, researchers, and ingredient manufacturers due to their wealthy composition of protein, starch, and micronutrients. The protein quality in peas is influenced by both intrinsic factors like amino acid composition and spatial conformations and extrinsic factors including growth and processing conditions. The existing literature substantiates that the structural modulation and optimization of functional, organoleptic, and nutritional attributes of pea proteins can be obtained through a combination of chemical, physical, and enzymatic approaches, resulting in superior protein ingredients. This review underscores recent methodologies in pea protein extraction aimed at enhancing yield and functionality for diverse food systems and also delineates existing research gaps related to mitigating off-flavor issues in pea proteins. A comprehensive examination of conventional dry and wet methods is provided, in conjunction with environmentally friendly approaches like ultrafiltration and enzyme-assisted techniques. Additionally, the innovative application of hydrodynamic cavitation technology in protein extraction is explored, focusing on its prospective role in flavor amelioration. This overview offers a nuanced understanding of the advancements in pea protein extraction methods, catering to the interests of varied stakeholders in the field. [ABSTRACT FROM AUTHOR]

Inflammation, hypertension, and negative heart health outcomes including cardiovascular disease are closely linked but the mechanisms by which inflammation can cause high blood pressure are not yet fully elucidated. Cyclooxygenase (COX) enzymes play a role in pain, inflammation, and hypertension development, and inhibition of these enzymes is currently of great interest to researchers and pharmaceutical companies. Non-steroidal anti-inflammatory drugs are the drug of choice in terms of COX inhibition but can have negative side effects for consumers. Functional food ingredients containing cyclooxygenase inhibitors offer a strategy to inhibit cyclooxygenases without negative side effects. Several COX inhibitors have been discovered, to date, from marine and other resources. We describe here, for the first time, the generation and characterization of a bioactive hydrolysate generated using Viscozyme® and Alcalase from the red microalga Porphyridium sp. The hydrolysate demonstrates in vitro COX-1 inhibitory activity and antihypertensive activity in vivo, assessed using spontaneously hypertensive rats (SHRs). Peptides were identified and sequenced using MS and assessed using an in silico computational approach for potential bioactivities. The peptides predicted to be bioactive, including GVDYVRFF, AIPAAPAAPAGPKLY, and LIHADPPGVGL were chemically synthesized and cyclooxygenase inhibition was confirmed. Peptides AIPAAPAAPAGPKLY and LIHADPPGVGL had COX-1 IC50 values of 0.2349 mg/mL (0.16 µM) and 0.2193 mg/mL (0.2 µM), respectively. The hydrolysate was included in a food carrier (jelly candies) and an antihypertensive effect was observed in SHRs. [ABSTRACT FROM AUTHOR]

Amyotrophic lateral sclerosis (ALS) is regarded as a fatal neurodegenerative disease that is featured by progressive damage of the upper and lower motor neurons. To date, over 45 genes have been found to be connected with ALS pathology. The aim of this work was to computationally identify unique sets of protein hydrolysate peptides that could serve as therapeutic agents against ALS. Computational methods which include target prediction, protein-protein interaction, and peptide-protein molecular docking were used. The results showed that the network of critical ALS-associated genes consists of ATG16L2, SCFD1, VAC15, VEGFA, KEAP1, KIF5A, FIG4, TUBA4A, SIGMAR1, SETX, ANXA11, HNRNPL, NEK1, C9orf72, VCP, RPSA, ATP5B, and SOD1 together with predicted kinases such as AKT1, CDK4, DNAPK, MAPK14, and ERK2 in addition to transcription factors such as MYC, RELA, ZMIZ1, EGR1, TRIM28, and FOXA2. The identified molecular targets of the peptides that support multi-metabolic components in ALS pathogenesis include cyclooxygenase-2, angiotensin I-converting enzyme, dipeptidyl peptidase IV, X-linked inhibitor of apoptosis protein 3, and endothelin receptor ET-A. Overall, the results showed that AGL, APL, AVK, IIW, PVI, and VAY peptides are promising candidates for further study. Future work would be needed to validate the therapeutic properties of these hydrolysate peptides by in vitro and in vivo approaches. [ABSTRACT FROM AUTHOR]

This study investigated the efficacy of roasting pre-treatment by air frying to enhance the extraction and recovery of the predominant sinapic acid derivatives (SADs) from roasted canola meal and the antioxidant potential of the methanolic extracts. Canola meal was obtained by air frying canola seed at 160, 170, 180 or 190 °C for 5, 10, 15 or 20 min. Oil was extracted using the Soxhlet method, and the de-oiled meal fraction was air-dried. Phenolic compounds were isolated using ultrasound-assisted extraction with 70% (v/v) methanol and then quantified by high-performance liquid chromatography-diode array detection. The antioxidant potential of the defatted meal methanolic extracts was evaluated using 2,2-diphenyl-1-picrylhydrazyl (DPPH), ferric reducing antioxidant power (FRAP), and metal ion-chelating activity (MIC) assays. The highest total phenolic content of 3.15 mg gallic acid equivalent/g dry weight was recorded in the defatted meal extract from seeds pre-treated with air frying at 190 °C for 15 min. Sinapine, sinapic acid and an unknown compound at a retention time (RT) of 26.6 min were the major sinapates identified in the defatted meal with the highest concentrations of 7572 ± 479.2 µg/g DW, 727 ± 43.45 µg/g DW and 1763 ± 73.5 µg/g DW, respectively, obtained at 160 °C for 5 min. Canolol (151.35 ± 7.65 µg/g DW) was detected after air frying at a temperature of 170 °C for 20 min. The FRAP and MIC correlated positively (r = 0.85) and generally decreased with increased air frying temperature-time conditions. The highest FRAP and MIC values of 0.53 mM and 80% were obtained at 160 °C for 5 and 20 min, respectively. The outcome of this study will contribute new knowledge that could improve the value addition and by-product utilization of canola seeds. [ABSTRACT FROM AUTHOR]

Skin injury causes fibroblast dysfunction and lowers collagen production. Safe, functional ingredients such as vitamin C (Vit C) and fish hydrolyzed collagen (HC) have been used to alleviate this problem. Defatted HC from salmon (Oncorhynchus nerka) skin could be a potential functional ingredient with skin nourishment activity. This study aimed to investigate the combined effects of HC and Vit C on the proliferation and migration of human dermal fibroblast (HDF). Molecular weight ranging from 102 Da to 10,175 Da and high imino acid content were found in HC. HC (0–800 µg/mL) or vitamin C (Vit C) (0.01–100 µg/mL) was applied for HDF treatment. Higher cell proliferation was found by adding HC at 50 µg/mL or Vit C at 0.01 µg/mL compared to the control and those treated with both compounds at other levels (p < 0.05). Cells treated with HC (50 µg/mL) combined with Vit C (0.01 µg/mL) (HC+Vit C) showed higher proliferation, migration, and lamellipodia formation of HDF cells than those treated with HC or Vit C alone. Moreover, all the samples tested could stimulate the proliferation and migration of HDF cells via FAK/Akt and ERK/p38 MAPK signaling pathways. Thus, HC combined with Vit C could be a promising functional ingredient for skin nourishment and would healing. [ABSTRACT FROM AUTHOR]

Milk-derived bioactive peptides (BAPs) possess several potential attributes in terms of therapeutic capacity and their nutritional value. BAPs from milk proteins can be liberated by bacterial fermentation, in vitro enzymatic hydrolysis, food processing, and gastrointestinal digestion. Previous evidence suggested that milk protein-derived BAPs have numerous health-beneficial characteristics, including anti-cancerous activity, anti-microbial activity, anti-oxidative, anti-hypertensive, lipid-lowering, anti-diabetic, and anti-osteogenic. In this literature overview, we briefly discussed the production of milk protein-derived BAPs and their mechanisms of action. Milk protein-derived BAPs are gaining much interest worldwide due to their immense potential as health-promoting agents. These BAPs are now used to formulate products sold in the market, which reflects their safety as natural compounds. However, enhanced commercialization of milk protein-derived BAPs depends on knowledge of their particular functions/attributes and safety confirmation using human intervention trials. We have summarized the therapeutic potentials of these BAPs based on data from in vivo and in vitro studies. [ABSTRACT FROM AUTHOR]

Plant-based foods are rich sources of vitamins and essential micronutrients. For the proper functioning of the human body and their crucial role, trace minerals (iron, zinc, magnesium, manganese, etc.) are required in appropriate amounts. Cereals and pulses are the chief sources of these trace minerals. Despite these minerals, adequate consumption of plant foods cannot fulfill the human body’s total nutrient requirement. Plant foods also contain ample amounts of antinutritional factors such as phytate, tannins, phenols, oxalates, etc. These factors can compromise the bioavailability of several essential micronutrients in plant foods. However, literature reports show that fermentation and related processing methods can improve nutrient and mineral bioavailability of plant foods. In this review, studies related to fermentation methods that can be used to improve micronutrient bioavailability in plant foods are discussed. [ABSTRACT FROM AUTHOR]

The aim of this work was to produce antihypertensive protein hydrolysates through different forms of enzymatic hydrolysis (2% pepsin, 4% pepsin, 1% alcalase, 2% alcalase, 2% papain, and 2% pepsin + pancreatin) of hemp seed proteins (HSP). The hemp seed protein hydrolysates (HPHs) were tested for in vitro inhibitions of renin and angiotensin-converting enzyme (ACE), two of the enzymes that regulate human blood pressure. The HPHs were then administered orally (200 mg/kg body weight) to spontaneously hypertensive rats and systolic blood pressure (SBP)-lowering effects measured over a 24 h period. Size exclusion chromatography mainly showed a 300--9560 Da peptide size range for the HPHs, while amino acid composition data had the 2% pepsin HPH with the highest cysteine content. Fluorescence spectroscopy revealed higher fluorescence intensities for the peptides when compared to the unhydrolyzed hemp seed protein. Overall, the 1% alcalase HPH was the most effective (p < 0.05) SBP-reducing agent (-32.5 ± 0.7 mmHg after 4 h), while the pepsin HPHs produced longer-lasting effects (-23.0 ± 1.4 mmHg after 24 h). We conclude that an optimized combination of the fast-acting HPH (1% alcalase) with the longer-lasting HPHs (2% and 4% pepsin) could provide daily effective SBP reductions. [ABSTRACT FROM AUTHOR]

Thermoase-digested flaxseed protein hydrolysate (FPH) samples and ultrafiltration membrane-separated peptide fractions were initially evaluated for in vitro inhibition of angiotensin I-converting enzyme (ACE) and renin activities. The two most active FPH samples and their corresponding peptide fractions were subsequently tested for in vivo antihypertensive activity in spontaneously hypertensive rats (SHR). The FPH produced with 3% thermoase digestion showed the highest ACE- and renin-inhibitory activities. Whereas membrane ultrafiltration resulted in significant (p < 0.05) increases in ACE inhibition by the <1 and 1-3 kDa peptides, only a marginal improvement in renin-inhibitory activity was observed for virtually all the samples after membrane ultrafiltration. The FPH samples and membrane fractions were also effective in lowering systolic blood pressure (SBP) in SHR with the largest effect occurring after oral administration (200 mg/kg body weight) of the 1-3 kDa peptide fraction of the 2.5% FPH and the 3-5 kDa fraction of the 3% FPH. Such potent SBP-lowering capacity indicates the potential of flaxseed protein-derived bioactive peptides as ingredients for the formulation of antihypertensive functional foods and nutraceuticals. [ABSTRACT FROM AUTHOR]

Enzymatic hydrolysate of African yam bean seed protein isolate was prepared by treatment with alcalase. The hydrolysate was further fractionated into peptide sizes of <1, 1-3, 3-5 and 5-10 kDa using membrane ultrafiltration. The protein hydrolysate (APH) and its membrane ultrafiltration fractions were assayed for in vitro antioxidant activities. The <1 kDa peptides exhibited significantly better (p < 0.05) ferric reducing power, diphenyl-1-picryhydradzyl (DPPH) and hydroxyl radical scavenging activities when compared to peptide fractions of higher molecular weights. The high activity of <1 kDa peptides in these antioxidant assay systems may be related to the high levels of total hydrophobic and aromatic amino acids. In comparison to glutathione (GSH), the APH and its membrane fractions had significantly higher (p < 0.05) ability to chelate metal ions. In contrast, GSH had significantly greater (p < 0.05) ferric reducing power and free radical scavenging activities than APH and its membrane fractions. The APH and its membrane fractions effectively inhibited lipid peroxidation, results that were concentration dependent. The activity of APH and its membrane fractions against linoleic acid oxidation was higher when compared to that of GSH but lower than that of butylated hydroxyl toluene (BHT). The results show potential use of APH and its membrane fractions as antioxidants in the management of oxidative stress-related metabolic disorders and in the prevention of lipid oxidation in food products. [ABSTRACT FROM AUTHOR]

The contributions of individual amino acid residues or groups of amino acids to antioxidant activities of some food protein hydrolysates were investigated using partial least squares (PLS) regression method. PLS models were computed with amino acid composition and 3-z scale descriptors in the X-matrix and antioxidant activities of the samples in the Y-matrix; models were validated by cross-validation and permutation tests. Based on coefficients of the resulting models, it was observed that sulfur-containing (SCAA), acidic and hydrophobic amino acids had strong positive effects on scavenging of 2,2-diphenyl-1-picrylhydrazyl (DPPH) and H2O2 radicals in addition to ferric reducing antioxidant power. For superoxide radicals, only lysine and leucine showed strong positive contributions while SCAA had strong negative contributions to scavenging by the protein hydrolysates. In contrast, positively-charged amino acids strongly contributed negatively to ferric reducing antioxidant power and scavenging of DPPH and H2O2 radicals. Therefore, food protein hydrolysates containing appropriate amounts of amino acids with strong contribution properties could be potential candidates for use as potent antioxidant agents. We conclude that information presented in this work could support the development of low cost methods that will efficiently generate potent antioxidant peptide mixtures from food proteins without the need for costly peptide purification. [ABSTRACT FROM AUTHOR]

The hemp seed contains protein fractions that could serve as useful ingredients for food product development. However, utilization of hemp seed protein fractions in the food industry can only be successful if there is sufficient information on their levels and functional properties. Therefore, this work provides a comparative evaluation of the structural and functional properties of hemp seed protein isolate (HPI) and fractions that contain 2S, 7S, or 11S proteins. HPI and protein fractions were isolated at pH values of least solubility. Results showed that the dominant protein was 11S, with a yield of 72.70 ± 2.30%, while 7S and 2S had values of 1.29 ± 0.11% and 3.92 ± 0.15%, respectively. The 2S contained significantly (p < 0.05) higher contents of sulfhydryl groups at 3.69 µmol/g when compared to 7S (1.51 µmol/g), 11S (1.55 µmol/g), and HPI (1.97 µmol/g). The in vitro protein digestibility of the 2S (72.54 ± 0.52%) was significantly (p < 0.05) lower than those of the other isolated proteins. The intrinsic fluorescence showed that the 11S had a more rigid structure at pH 3.0, which was lost at higher pH values. We conclude that the 2S fraction has superior solubility, foaming capacity, and emulsifying activity when compared to the 7S, 11S, and HPI. [ABSTRACT FROM AUTHOR]

Edible seeds play a significant role in contributing essential nutritional needs and impart several health benefits to improve the quality of human life. Previous literature evidence has confirmed that edible seed proteins, their enzymatic hydrolysates, and bioactive peptides (BAPs) have proven and potential attributes to ameliorate numerous chronic disorders through the modulation of activities of several molecular markers. Edible seed-derived proteins and peptides have gained much interest from researchers worldwide as ingredients to formulate therapeutic functional foods and nutraceuticals. In this review, four main methods are discussed (enzymatic hydrolysis, gastrointestinal digestion, fermentation, and genetic engineering) that are used for the production of BAPs, including their purification and characterization. This article's main aim is to provide current knowledge regarding several health-promoting properties of edible seed BAPs in terms of antihypertensive, anti-cancer, antioxidative, anti-inflammatory, and hypoglycemic activities. [ABSTRACT FROM AUTHOR]

The demand for isolated seed proteins continues to increase but functionality in food systems can be greatly dependent on the extraction method. In this work, we report the physicochemical and functional properties of lentil seed proteins isolated using various protocols. Lentil flour was defatted followed by protein extraction using isoelectric pH precipitation (ISO) as well as NaOH (MEM_NaOH) and NaCl (MEM_NaCl) extractions coupled with membrane ultrafiltration. The MEM_NaCl had significantly (p < 0.05) higher protein content (90.28%) than the ISO (86.13%) and MEM_NaOH (82.55%). At pH 3–5, the ISO was less soluble (2.26–11.84%) when compared to the MEM_NaOH (25.74–27.22%) and MEM_NaCl (27.78–40.98%). However, the ISO had higher yield and protein digestibility (48.45% and 89.82%) than MEM_NaOH (35.05% and 77.87%) and MEM_NaCl (13.35% and 77.61%), respectively. Near-UV circular dichroism spectra showed that the MEM_NaOH had loose tertiary conformation at pH 3, 5, 7 and 9 while ISO and MEM_NaCl had more compact structures at pH 7 and 9. The three protein isolates formed better emulsions (lower oil droplet sizes) at pH 7 and 9 when compared to pH 3 and 5. In contrast, foaming capacity was better at pH 5 than pH 3, 7, and 9. [ABSTRACT FROM AUTHOR]

Antioxidants remain interesting molecules of choice for suppression of the toxic effects of free radicals in foods and human systems. The current practice involves the use of mainly synthetic molecules as potent antioxidant agents. However, due to the potential negative impact on human health, there is an intensive effort within the research community to develop natural alternatives with similar antioxidant efficacy but without the negative side effects of synthetic molecules. Still, the successful development of new molecules depends on the use of reliable chemical or cell culture assays to screen antioxidant properties. Chemical antioxidant assays include the determination of scavenging ability against free radicals such as DPPH, superoxide anion radicals, hydroxyl radicals, hydrogen peroxide, and nitric oxide. Other antioxidant tests include the ability of compounds to bind and sequester prooxidant metal cations, reduce ferric iron, and attenuate the rate of lipid oxidation. Ex vivo tests utilize cell cultures to confirm entry of the molecules into cells and the ability to quench synthetic intracellular free radicals or to stimulate the increased biosynthesis of endogenous antioxidants. In order to assist researchers in their choice of antioxidant evaluation methods, this review presents background scientific information on some of the most commonly used antioxidant assays with a comparative discussion of the relevance of published literature data to food science and human nutrition applications. [ABSTRACT FROM AUTHOR]

Osteoporosis is a serious problem affecting health of the elderly. Drugs (bisphosphonates) applied for treatment are often accompanied by adverse side effects. Thus, fish byproduct-derived peptides, particularly hydrolyzed collagen (HC) from defatted sea bass skin, could be a safe source of anti-osteoporosis agents. This study aimed to examine the effects of HC on proliferation and differentiation of preosteoblast cells. HC prepared using papain before Alcalase hydrolysis was determined for molecular weight (MW) distribution. Thereafter, the resulting HC (50–800 µg/mL) was added to the cell. Proliferation, alkaline phosphatase activity (AP-A) and mineralization of cells were investigated. Moreover, the expression of runt-related transcription factor 2 (RUNX2) and the p-Akt/Akt pathway were also determined using Western blot. The results showed that HC had an MW < 3 kDa. HC (50–200 µg/mL) could promote cell proliferation. Nevertheless, HC at 100 µg/mL (HC-100) had enhanced AP-A and increased mineralization during the first 7 days of culture. Moreover, HC-treated cells had higher calcium depositions than the control (p < 0.05). Additionally, cells treated with HC-100 had higher levels of RUNX2 and p-Akt expressions than control (p < 0.05). Therefore, HC could be a promising functional ingredient to promote osteoblast proliferation and differentiation, which could enhance bone strength. [ABSTRACT FROM AUTHOR]

Solanum macrocarpon (eggplant) leaf protein isolate (ELI) was hydrolyzed using four different enzymes to produce hydrolysates from alcalase (AH), chymotrypsin (CH) pepsin (PH) and trypsin (TH). CH had an overall stronger antioxidant property and was separated using ultrafiltration membranes into <1, 1–3 and 3–5 kDa peptide fractions. Gel-permeation chromatography confirmed conversion of the ELI (average of 22 kDa) into protein hydrolysates that contained smaller peptides (<6 kDa). A total of 23 peptides consisting of tri and tetrapeptides were identified from the CH, which is a wider spectrum when compared to seven for AH and four each for TH and PH. CH exhibited stronger scavenging activities against DPPH and hydroxyl radicals. CH and TH exhibited the strongest inhibitions against angiotensin-converting enzyme. In contrast, AH was the strongest inhibitor of α-amylase while AH and PH had strong inhibitory activities against α-glucosidase when compared with other hydrolysates. Ultrafiltration fractionation produced peptides that were stronger (p < 0.05) scavengers of DPPH, and hydroxyl radicals, in addition to better metal-chelating and enzyme inhibition agents. The study concluded that the eggplant protein hydrolysates and the UF fractions may find applications in tackling oxidative stress-related diseases and conditions involving excessive activities of the metabolic enzymes. [ABSTRACT FROM AUTHOR]

Plant foods are consumed worldwide due to their immense energy density and nutritive value. Their consumption has been following an increasing trend due to several metabolic disorders linked to non-vegetarian diets. In addition to their nutritive value, plant foods contain several bioactive constituents that have been shown to possess health-promoting properties. Plant-derived bioactive compounds, such as biologically active proteins, polyphenols, phytosterols, biogenic amines, carotenoids, etc., have been reported to be beneficial for human health, for instance in cases of cancer, cardiovascular diseases, and diabetes, as well as for people with gut, immune function, and neurodegenerative disorders. Previous studies have reported that bioactive components possess antioxidative, anti-inflammatory, and immunomodulatory properties, in addition to improving intestinal barrier functioning etc., which contribute to their ability to mitigate the pathological impact of various human diseases. This review describes the bioactive components derived from fruit, vegetables, cereals, and other plant sources with health promoting attributes, and the mechanisms responsible for the bioactive properties of some of these plant components. This review mainly compiles the potential of food derived bioactive compounds, providing information for researchers that may be valuable for devising future strategies such as choosing promising bioactive ingredients to make functional foods for various non-communicable disorders. [ABSTRACT FROM AUTHOR]

The aim of this work was to characterize the antioxidant properties of some of the peptides present in bromelain mung bean meal protein hydrolysate (MMPH). The MMPH was subjected to two rounds of bioassay-guided reversed-phase HPLC separation followed by peptide identification in the most potent fractions using tandem mass spectrometry. Twelve antioxidant peptides, namely, HC, CGN, LAN, CTN, LAF, CSGD, MMGW, QFAAD, ERF, EYW, FLQL, and QFAW were identified and assayed for antioxidant properties. CTN, HC, CGN, and CSGD were the most potent (p < 0.05) DPPH radical scavengers with EC50 values of 0.30, 0.29, 0.28, and 0.30 mg/mL, respectively, which are lower than the 0.03 mg/mL obtained for reduced glutathione (GSH). CTN, HC, CGN, and CSGD exhibited the most potent (p < 0.05) scavenging activities against hydroxyl and superoxide radicals with EC50 values that are similar to those of GSH. The cysteine-containing peptides also had stronger ferric reducing antioxidant power and metal chelation activity than peptides devoid of cysteine. In contrast, MMGW, ERF, and EYW had poor radical scavenging and metal chelation activities. We conclude that the availability of the sulfhydryl group may have enhanced antioxidant potency while the presence of bulky groups such phenylalanine and tryptophan had an opposite effect. [ABSTRACT FROM AUTHOR]

An iron-binding mung bean protein hydrolysate (MBPH) was prepared using a continuous enzymatic membrane reactor followed by peptide separation on anion-exchange (AEC) and reverse-phase HPLC (RP-HPLC) columns. Amino acid sequences of peptides present in the RP-HPLC fraction with the strongest iron-binding capacity were identified using mass spectrometry, and ten peptides of 5–8 amino acids synthesized for antioxidant characterization. Five fractions (AF1– AF5) with higher iron-binding capacity (88.86 ± 6.43 to 153.59 ± 2.18 mg/g peptide) when compared to the MBPH (36.81 ± 0.93 mg/g peptide) were obtained from AEC. PAIDL had the significantly (p < 0.05) highest iron-binding capacity, but LLLLG and LLGIL showed the strongest metal chelating activity. However, PAIDL (46.63%) and LLGIL (81.27%) had significantly (p < 0.05) better DPPH radical scavenging activity than the other peptides. PAIDL and LLGIL were also the most effective (p < 0.05) hydroxyl radical neutralizers with an effective concentration that scavenged 50% (EC50) values of 0.09 and 0.37 mM, respectively. PAIDL and AIVIL showed the lowest EC50 values of 0.07 mM each for superoxide radical scavenging activity. We conclude that short chain length in combination with leucine as the C-terminal amino acid residue contributed to the strong antioxidant properties of peptides in this study. [ABSTRACT FROM AUTHOR]

The aim of the study was to determine the in vitro enzyme inhibition activities of aqueous polyphenolic extracts of nine popular Bangladeshi vegetables, namely ash gourd, bitter gourd, brinjal, Indian spinach, kangkong, okra, ridge gourd, snake gourd, and stem amaranth. Polyphenolic glycosides were the major compounds present in the extracts. Inhibition of α-amylase (up to 100% at 1 mg/mL) was stronger than α-glucosidase inhibition (up to 70.78% at 10 mg/mL). The Indian spinach extract was the strongest inhibitor of pancreatic lipase activity (IC50 = 276.77 µg/mL), which was significantly better than that of orlistat (381.16 µg/mL), a drug. Ash gourd (76.51%), brinjal (72.48%), and snake gourd (66.82%) extracts were the most effective inhibitors of angiotensin-converting enzyme (ACE), an enzyme whose excessive activities have been associated with hypertension. Brinjal also had a significantly higher renin-inhibitory activity than the other vegetable extracts. We conclude that the vegetable extracts may have the ability to reduce enzyme activities that have been associated with hyperglycemia, hyperlipidemia, and hypertension. [ABSTRACT FROM AUTHOR]

Being averse to bitter taste is a common phenomenon for humans and other animals, which requires the pharmaceutical and food industries to source compounds that can block bitterness intensity and increase consumer acceptability. In this work, beef protein alcalase hydrolysates (BPAH) and chymotrypsin hydrolysates (BPCH) were reacted with glucose to initiate Maillard reactions that led to the formation of glycated or advanced glycation end products (AGEs), BPAH-AGEs and BPCH-AGEs, respectively. The degree of glycation was higher for the BPAH-AGEs (47–55%) than the BPCH-AGEs (30–38%). Analysis by an electronic tongue instrument showed that BPAH-AGEs and BPCH-AGEs had bitterness scores that were significantly (p < 0.05) less than quinine. The addition of BPAH-AGEs or BPCH-AGEs to quinine led to significant (p < 0.05) reductions (up to 38%) in bitterness intensity of quinine. The use of 3% hydrolysate to react with glucose yielded glycated peptides with a stronger ability to reduce quinine bitterness than when 1% was used. Calcium release from HEK293T cells stably expressing the T2R4 human bitter taste receptor was significantly (p < 0.05) attenuated by BPAH-AGEs (up to 96%) and BPCH-AGEs (up to 92%) when compared to the BPAH (62%) and BPCH (3%) or quinine (0%). We concluded that BPAH-AGEs and BPCH-AGEs may be used as bitter taste blockers to formulate better tasting foods. [ABSTRACT FROM AUTHOR]

Bitter taste receptors (T2Rs) are expressed in several tissues of the body and are involved in a variety of roles apart from bitter taste perception. Advanced glycation end-products (AGEs) are produced by glycation of amino acids in proteins. There are varying sources of AGEs, including dietary food products, as well as endogenous reactions within our body. Whether these AGEs are T2R ligands remains to be characterized. In this study, we selected two AGEs, namely, glyoxal-derived lysine dimer (GOLD) and carboxymethyllysine (CML), based on their predicted interaction with the well-studied T2R4, and its physiochemical properties. Results showed predicted binding affinities (Kd) for GOLD and CML towards T2R4 in the nM and μM range, respectively. Calcium mobilization assays showed that GOLD inhibited quinine activation of T2R4 with IC50 10.52 ± 4.7 μM, whilst CML was less effective with IC50 32.62 ± 9.5 μM. To characterize whether this antagonism was specific to quinine activated T2R4 or applicable to other T2Rs, we selected T2R14 and T2R20, which are expressed at significant levels in different human tissues. A similar effect of GOLD was observed with T2R14; and in contrast, GOLD and CML activated T2R20 with an EC50 of 79.35 ± 29.16 μM and 65.31 ± 17.79 μM, respectively. In this study, we identified AGEs as novel T2R ligands that caused either activation or inhibition of different T2Rs. [ABSTRACT FROM AUTHOR]

In this work, we report the potency of enzymatic hydrolysates of pea proteins against trypsin and chymotrypsin. Pea protein concentrate was digested with each of alcalase, chymotrypsin, pepsin, and trypsin, followed by membrane separation of the protein hydrolysates into peptide fractions (<1, 1–3, 3–5, and 5–10 kDa). Peptide size profiling with size-exclusion gel chromatography indicated the narrowest size range (0.85–4.98 kDa) for alcalase. Trypsin activity was strongly (p < 0.05) inhibited by the ultrafiltration fractions (mean IC50 = 2.2 mg/mL) obtained from the trypsin hydrolysate when compared to the unfractionated hydrolysate (IC50 = 6.8 mg/mL). Similarly, ultrafiltration also enhanced trypsin inhibition by the alcalase-digested peptides with an IC50 of 21.4 mg/mL for the unfractionated hydrolysate in comparison to 3.1–4.7 mg/mL for the fractions. However, ultrafiltration did not enhance trypsin inhibitory activity of chymotrypsin-digested peptides, while the peptide separation reduced efficacy of pepsin-digested peptides. In contrast, chymotrypsin inhibition by all the enzymatic digests was significantly (p < 0.05) enhanced by ultrafiltration, especially peptide sizes >3 kDa. Kinetics of enzyme inhibition indicate peptides were bound to the enzyme active site in a competitive mode that led to reduced catalysis. We conclude that the pea peptides could function as useful tools to promote human health and as a preservative during food processing and storage. [ABSTRACT FROM AUTHOR]