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Poor vitamin D status is a widespread problem regardless of age and sex, emphasizing the necessity of new food sources to improve vitamin D levels. Currently, approximately 60% of dietary vitamin D consumption occurs via fortified foods. Vitamin D insufficiency (50-90%) is widespread according to age and region, despite different levels of sunlight exposure. The food industry must identify more effective strategies to increase normal dietary vitamin D intake and improve overall health. Strategies for vitamin D fortification include bioaddition, wherein a vitamin D-rich food source is added to staple foods during processes. These bioadditive strategies expand the range of vitamin D-containing foods and appeal to different preferences, cultures, and economic statuses. In several countries, vitamin D deficiency places athletes at a high risk of disease susceptibility. Due to low sun exposure, athletes in countries with higher and lower levels of sunlight have similar risks of vitamin D deficiency. In this review, we summarize recent technical advances to promote vitamin D utilization by humans during sports activities and in relation to the normal practices of athletes.
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Autism spectrum disorder (ASD) is characterised by problems with social interaction, verbal and nonverbal communication and repetitive behaviour. In mice, the 14th postnatal day is believed to correspond to the third trimester of human embryonic development and is considered a vital period for central nervous system development. It has been shown that ASD affects 2 to 3 times more male than female individuals. In the present study, ASD was induced in 14 postnatal day (PND) BALB/c mice using valproic acid (VPA). VPA administration brought about substantial differences in the histoarchitecture of the brain in both male and female mice, linked to behavioural deficits. We observed that both male and female mice showed similar morphological changes in the prefrontal cortex, hippocampus and Purkinje cells. We also observed hair loss from PND 17 to 25, which was again similar between male and female mice. However, there were higher rates of change in the cerebral cortex, frontal cortex and temporal lobe and hippocampus in VPA-treated male animals. With respect to the cerebellum, we did not observe any alterations by haematoxylin and eosin (H&E) staining, but detailed morphological observation using scanning electron microscopy (SEM) showed a higher rate of phenotype changes in VPA-treated male animals. Moreover, 5-HT2A receptor protein levels were upregulated in the cerebral cortex, hippocampus and Purkinje cells in VPA-treated male mice compared with control animals and VPA-treated female mice, as shown by immunohistochemical analysis. Based on all these findings, we conclude that male animals are more susceptible to VPA-induced ASD than females.
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Peanut worms (Sipunculids) are unsegmented marine worms that usually inhabit shallow waters. Peanut worms are good source of bioactive compounds including peptides and polysaccharides. Many recent studies have investigated the bioactive properties of peptides and polysaccharides derived from peanut worms in order to enhance their applications in food and pharmaceutical industries. The peptides and polysaccharides isolated from peanut worms have been reported to possess anti-hypertensive, anti-oxidant, immunomodulatory, anti-inflammatory, anti-cancer, anti-hypoxia and wound healing activities through the modulation of various molecular mechanisms. Most researchers used in vitro, cell culture and animal models for the determination of bioactivities of peanut worm derived compounds. However, studies in humans have not been performed considerably. Therefore, it is important to conduct more human studies for better utilization of marine bioactive compounds (peptides and polysaccharides) derived from peanut worms. This review mainly focuses on the bioactive properties of peptides and polysaccharides of peanut worms and their molecular mechanisms.
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Anélidos , Péptidos/farmacología , Polisacáridos/farmacología , Animales , Péptidos/química , Polisacáridos/químicaRESUMEN
Inflammatory bowel disease, a typical chronic inflammatory disease of the gastrointestinal tract, make up a growing share of the global disease burden. This study firstly evaluated the anti-inflammatory effects of corn protein hydrolysate (CPH) using a cell model of tumor cell necrosis factor-α (TNF-α)-induced inflammation and a mouse model of colitis induced by dextran sodium sulfate. CPH digests significantly inhibited the expression of cyclooxygenase-2 and inducible nitric oxide synthase, and reduced the secretion of interleukin-8 in TNF-α-induced inflammation in Caco-2 cells. In mice, CPH digests significantly improved the body weight loss, clinical scores, shortening of the colon and histological symptoms, and decreased the myeloperoxidase activity, and down regulated the expression of TNF-α, and interleukin-6 in the colon. The above results indicate that the CPH can potentially be used as a health food/nutraceutical for the treatment/management of intestinal inflammation.
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Collagen hydrolysates (peptides) derived from food processing byproducts have been used to produce commercially valuable food ingredients due to their potential to trigger certain desirable physiological responses in the body. Low-molecular-weight (LMW) collagen hydrolysates are generally thought to exert better bioactivities than their larger counterparts. However, the preparation of LMW collagen hydrolysates is often impeded by their special structure, cross-linking, and hydroxyproline. This review briefly introduces the motivation of the food industry to prepare LMW collagen hydrolysate from food processing byproducts. We further summarize recent progress on the preparation of LMW collagen hydrolysates and methods to determine the molecular weight. We then discuss the challenges and then provide perspectives on future directions in preparing LMW collagen hydrolysates.
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Colágeno/química , Industria de Procesamiento de Alimentos/métodos , Hidrolisados de Proteína/química , Animales , Hidroxiprolina/química , Peso Molecular , Péptidos/químicaRESUMEN
In this study, resveratrol was successfully encapsulated using zein-chitosan complex coacervation. The encapsulation efficiency was markedly improved (51.4%) after chitosan coating at 1:2.5 zein/chitosan ratio, compared with 38.6% using native zein. Analysis of multi-model frequency ultrasound treatment effects on resveratrol encapsulation using zein-chitosan complex coacervation showed that 28/40â¯kHz dual-frequency ultrasound led to the highest encapsulation efficiency (65.2%; 31.9% increase) and loading capacity (5.9%; 31.1% increase) of resveratrol, followed by multi-frequency ultrasound at 20/28/40â¯kHz (17.8% encapsulation efficiency increase; 17.8% loading capacity increase). Dual-frequency ultrasound treatment significantly reduced the zein-chitosan complex coacervation particle size and reduced their distribution, however, did not change the zeta potential. Fourier transform infrared spectroscopy and fluorescence spectroscopy analysis demonstrated that ultrasound treatment had no effect on secondary structure of zein-chitosan complex but markedly decreased the fluorescence emission intensity. Differential scanning calorimetry and X-ray diffraction results indicated that Dual-frequency ultrasound treatment improved the thermal stability of zein-chitosan complex coacervation but had no effect on the crystal structure. Atomic force microscopy and scanning electron microscopy images revealed uniform distribution of zein-chitosan complex coacervation followed by ultrasonic treatment.
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Quitosano/química , Resveratrol/química , Ultrasonido/métodos , Zeína/química , Rastreo Diferencial de Calorimetría , Microscopía de Fuerza Atómica , Microscopía Electrónica de Rastreo , Tamaño de la Partícula , Espectroscopía Infrarroja por Transformada de Fourier , Difracción de Rayos XRESUMEN
In this study, leftover egg yolk granules, a by-product after phosvitin extraction, were evaluated for the physicochemical and functional properties and the results were compared with those of the egg yolk and whole granule with phosvitin. Leftover granule after phosvitin removal accounted for 12.6% of the dried egg yolk and contained 84.5% protein and 7.98% fat. Scanning electron microscopy (SEM) images of leftover granules indicated the dissociation of aggregates of high density lipoprotein-phosvitin complexes. Protein solubility of leftover granules was markedly influenced by pH and sodium chloride (0.5 and 1â¯M). The apparent viscosity of leftover granule was higher than egg yolk and whole granule. Compared to whole granule, leftover granule had significantly (Pâ¯<â¯0.05) superior foaming and emulsifying properties, but, lower than those of egg yolk. These findings are useful for the food industry for utilization of leftover egg yolk granules for the preparation of various food products.
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Yema de Huevo/química , Manipulación de Alimentos/métodos , Fosvitina/química , Cloruro de Sodio , Solubilidad , ViscosidadRESUMEN
Small collagen peptides are associated with various benefits, such as bone and skin health. However, preparation of small collagen peptides from terrestrial vertebrate origins remains a challenge. Here, we show that pretreatment with formic acid enhanced the production of small collagen peptides from spent hen skin. After pretreatment with formic acid, the percentage of small peptides below 2â¯kDa increased to 48.92% and 43.34% from 33.79% and 36.32% for heat-soluble collagen (HSC) and pepsin-soluble collagen (PSC), respectively. Pretreatment with formic acid degraded telopeptides and released the cross-links (pyrrole and pyridinoline), which made hen collagen more susceptible to papain hydrolysis. LC-MS/MS results revealed that none of the peptides identified from HSC-FA (formic acid)-Papain and PSC-FA-Papain were derived from cross-linked telopeptides. These results demonstrated that formic acid assisted the hydrolysis of highly cross-linked collagen of spent hens, and it might also be used to produce small collagen peptides from other aged, vertebrate collagens.
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Pollos , Colágeno/química , Formiatos/química , Fragmentos de Péptidos/química , Aminoácidos/química , Animales , Reactivos de Enlaces Cruzados/química , Electroforesis en Gel de Poliacrilamida , Femenino , Hidrólisis , Papaína/química , Pepsina A/química , Fragmentos de Péptidos/análisis , Piel/química , Espectrometría de Masas en TándemRESUMEN
Chronic inflammation is an underlying contributor to various chronic diseases. The objectives of this study were to investigate the anti-inflammatory activity of zein hydrolysate after simulated gastrointestinal digestion and Caco-2 cell absorption and to identify novel anti-inflammatory peptides after transport across Caco-2 cells. Three zein hydrolysates were prepared and further digested using gastrointestinal proteases; their transports were studied in Caco-2 cells. Anti-inflammatory activity was studied in endothelial EA.hy926 cells. Three zein hydrolysates and their digests significantly decreased the expression of tumor necrosis factor-α (TNF-α) induced pro-inflammatory vascular cell adhesion molecule-1 (VCAM-1) by 37.3-66.0%. Eleven novel peptides with 5-9 amino acid residues were sequenced; three peptides showed strong anti-inflammatory activity by inhibiting the VCAM-1 by 54-38.9% and intercellular cell adhesion molecule-1 (ICAM-1) by 36.5-28.6% at 0.2 mM. A new approach to identify novel anti-inflammatory peptides that could survive gastrointestinal digestion and absorption was developed.
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Antiinflamatorios/análisis , Digestión , Tracto Gastrointestinal/metabolismo , Péptidos/análisis , Zeína/química , Antiinflamatorios/farmacología , Transporte Biológico , Células CACO-2 , Línea Celular , Tracto Gastrointestinal/enzimología , Humanos , Hidrólisis , Molécula 1 de Adhesión Intercelular/efectos de los fármacos , Péptido Hidrolasas/metabolismo , Péptidos/metabolismo , Péptidos/farmacología , Factor de Necrosis Tumoral alfa/antagonistas & inhibidores , Molécula 1 de Adhesión Celular Vascular/antagonistas & inhibidores , Zeína/metabolismoRESUMEN
Bioactive peptides are oligopeptides that consist of 2-20 amino acids that can exert beneficial effects on human health in addition to basic nutritional effects. Food derived protein hydrolysates or peptides with immunomodulatory and anticancer activities have been reported from a variety of food protein sources such as milk, egg, fish, rice, soybean, pea, chlorella, spirulina, oyster and mussel. In vitro hydrolysis of food proteins using commercial proteolytic enzymes is the most commonly employed process for the production of immunomodulatory and anticancer food protein hydrolysates. The immunomodulatory and anticancer activities of food derived protein hydrolysates or peptides are related to the amino acid composition, sequence and length. Most immunomodulatory and anticancer food protein hydrolysates or peptides were tested using cell culture and animal models, while a few involved clinical trials. This review provides a comprehensive overview of immunomodulatory and anticancer food derived protein hydrolysates or peptides, their production and mechanisms of action.
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Antineoplásicos/farmacología , Alimentos , Factores Inmunológicos/farmacología , Hidrolisados de Proteína/inmunología , Hidrolisados de Proteína/farmacología , Aminoácidos/análisis , Animales , Chlorella/química , Productos Lácteos , Humanos , Péptidos/química , Péptidos/inmunología , Péptidos/farmacología , Proteínas de Plantas/química , Proteínas de Plantas/farmacología , Hidrolisados de Proteína/química , Alimentos MarinosRESUMEN
The low-molecular-weight (LMW) peptides derived from collagen have shown a potential for various nutritional and pharmaceutical applications. However, production of LMW peptides from vertebrate collagen remains a challenge. Herein, we report a new method to produce LMW collagen peptides using pepsin pretreatment that removed cross-linked telopeptides in collagen molecules. After the pretreatment, the proportion of LMW collagen peptides (<1.4 kDa) that were obtained from pepsin-soluble collagen increased to 32.59% compared to heat-soluble collagen peptides (16.10%). Fourier transform infrared spectroscopy results indicated that telopeptide cleavage retained the triple-helical conformation of collagen. Liquid chromatography-tandem mass spectrometry analysis suggested that Gly-X-Y (X is often proline, while Y is either hydroxyproline or hydroxylysine) repeats were not the main factors that hindered the enzymatic hydrolysis of collagen molecules. However, cross-link quantification demonstrated that trivalent cross-links that included pyridinolines and pyrroles were the primary obstacles to producing small peptides from collagen of spent hens. This study demonstrated for the first time that removing cross-linked telopeptides could enhance the production of LMW peptides from spent hen collagen, which is also of interest to manufacturers who produce LMW collagen peptides from other vertebrate animals, such as bovids and porcids.