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1.
Arch. latinoam. nutr ; 72(3): 196-204, sept. 2022. tab
Artículo en Español | LILACS, LIVECS | ID: biblio-1399277

RESUMEN

Introduction: The use of vegetable proteins as ingredients in food systems is based on their functional properties. The water and oil holding capacity, foaming, and emulsifying capacity/stability, and antioxidant assay of the protein fractions - albumins, globulins 7S/11S, glutelins and prolamins - isolated from Leucaena seed were evaluated. Objective: The objective of this study was to evaluate the functional properties and antioxidant capacity of the concentrate and protein fractions of ripe Leucaena spp. seeds. Materials and methods: Ripe Leucaena seeds were collected and evaluated in Oaxaca, Mexico (16°59'21''N 96°43'26''O) during the months of February-April 2021.The protein concentrate was isolated by isoelectric precipitation (pH=9, pH=4). The albumins, globulins, glutelins and prolamins were isolated based on their solubility properties in different extracting solutions. Results: Glutelins constituted the main protein fraction (75.88%). Prolamins were not found. The glutelins fractions showed the highest oil holding capacity (0.93±0.08 mL g-1). The albumins fraction had the highest water holding capacity (2.53±0.15 mL g-1), foaming capacity and foam stability (71.83±1.26 % and 70.00±0.00%, respectively) and antioxidant capacity (18.09±0.88%). The globulins exhibited the highest emulsifying capacity and emulsion stability (56.83±1.76% and 55.67±1.20%, respectively). Conclusions: The concentrate and protein fraction of Leucaena seeds showed different techno-functional and antioxidant properties of interest for the food industry, like those showed by other commercial vegetable proteins(AU)


Introducción: El uso de proteínas vegetales como ingredientes en sistemas alimentarios se basa en sus propiedades funcionales. Se evaluó la capacidad de retención de agua y aceite, la capacidad/estabilidad espumante y emulsionante y el ensayo antioxidante de las fracciones proteicas -albúminas, globulinas 7S/11S, glutelinas y prolaminas- aisladas de las semillas de Leucaena. Objetivo: El objetivo de este estudio fue evaluar las propiedades funcionales y la capacidad antioxidante del concentrado y las fracciones proteicas de las semillas maduras de Leucaena spp. Materiales y métodos: Las semillas maduras de Leucaena fueron recolectadas y evaluadas en Oaxaca, México (16°59'21''N 96°43'26''O) durante los meses de febrero-abril del año 2021. Se usó harina de Leucaena desgrasada para la preparación de las fracciones proteicas. El concentrado proteico se aisló por precipitación isoeléctrica (pH=9, pH=4). Las albúminas, globulinas, glutelinas y prolaminas se aislaron en función de sus propiedades de solubilidad en diferentes soluciones de extracción. Resultados: Las glutelinas constituyeron la principal fracción proteica (75,88%). No se encontraron prolaminas. La fracción de glutelinas mostró la mayor capacidad de retención de aceite (0.93±0,08 mL g-1). La fracción de albúminas presentó la mayor capacidad de retención de agua (2,53±0,15 mL g-1), capacidad espumante y estabilidad de la espuma (71,83±1,26% y 70,00±0,00%, respectivamente) y capacidad antioxidante (18,09±0,88%). Las globulinas mostraron la mayor capacidad emulsionante y estabilidad de la emulsión (56,83±1,76 y 55,67±1,20%, respectivamente). Conclusiones: El concentrado y las fracciones proteicas de las semillas de Leucaena mostraron diferentes propiedades tecno-funcionales y antioxidantes de interés para la industria alimentaria, similares a los reportados por diversas proteínas vegetales comerciales(AU)


Asunto(s)
Proteínas de Vegetales Comestibles/química , Fabaceae/química , Antioxidantes/química , Semillas , Aceites de Plantas/química , Agua/química , Industria de Alimentos , Albúminas/química , Emulsiones/química , Globulinas/química , Glútenes/química
2.
Food Chem ; 341(Pt 2): 128082, 2021 Mar 30.
Artículo en Inglés | MEDLINE | ID: mdl-33166823

RESUMEN

Potato flour is used in bakery products, extruded products and snacks. However, it displays weaker gel strengths and thus the wholesome utility is curtailed significantly. To improve viscoelastic properties and stability of potato gels, herein potato flour was treated with laccase and peroxidase to create a protein network structure leading to stable gels. The results revealed that the secondary structure of potato proteins altered upon the enzyme treatment. The gels of peroxidase-treated potato flour (PPF) and laccase-treated potato flour (LPF) displayed larger anti-shear ability, thermal stability and stronger three-dimensional network structure compared to the native potato gel. The PPF and LPF gels exhibited stronger viscoelastic properties and structural stability compared to peroxidase-treated potato protein and laccase-treated potato protein gels. The outcome serves as a theoretical basis to improve the properties of potato gels and to promote the designing and the development of novel potato flour based functional food.


Asunto(s)
Harina , Lacasa/química , Peroxidasa/química , Solanum tuberosum/química , Almidón/química , Geles/química , Proteínas de Vegetales Comestibles/química , Espectroscopía Infrarroja por Transformada de Fourier , Viscosidad
3.
Food Chem ; 334: 127613, 2021 Jan 01.
Artículo en Inglés | MEDLINE | ID: mdl-32711281

RESUMEN

The optimization of ultrasound-assisted alkaline extraction and enzymatic deamidation by protein-glutaminase (PG) on evening primrose seed cake (EPSC) protein and its effect on structure (amino acid composition, secondary structure and electrophoresis pattern) and techno-functional properties (water-holding and oil-binding capacities, solubility, emulsifying and foaming properties) of EPSC protein were evaluated. The optimum conditions of the both processes were measured using response surface methodology (RSM). The maximum yield (26.4%) and protein content (86.1%) were reached at the optimized extraction conditions. Optimal conditions of PG deamidation based on reaching a high degree of deamidation (DD) with a simultaneously low degree of hydrolysis (DH). Under these conditions, DD and DH were 39.40 and 2.11%, respectively. Ultrasound-assisted alkaline extraction and enzymatic deamidation by PG have great potential to produce edible EPSC protein with modified techno-functional characteristics that can be used for several aims in the food and pharmaceutical applications.


Asunto(s)
Fraccionamiento Químico/métodos , Oenothera biennis/química , Proteínas de Vegetales Comestibles/química , Amidas/química , Aminoácidos/análisis , Emulsionantes/química , Glutaminasa/química , Hidrólisis , Extractos Vegetales/química , Aceites de Plantas/química , Proteínas de Vegetales Comestibles/aislamiento & purificación , Estructura Secundaria de Proteína , Solubilidad , Ultrasonido
4.
Mol Nutr Food Res ; 64(19): e2000560, 2020 10.
Artículo en Inglés | MEDLINE | ID: mdl-32875712

RESUMEN

SCOPE: Chickpea (Cicer arietinum) allergy has frequently been reported particularly in Spain and India. Nevertheless, chickpea allergens are poorly characterized. The authors aim to identify and characterize potential allergens from chickpea. METHODS AND RESULTS: Candidate proteins are selected by an in silico approach or immunoglobuline E (IgE)-testing. Potential allergens are prepared as recombinant or natural proteins and characterized for structural integrity by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), circular dichroism (CD)-spectroscopy, and mass spectrometry (MS) analysis. IgE-sensitization pattern of Spanish chickpea allergic and German peanut and birch pollen sensitized patients are investigated using chickpea extracts and purified proteins. Chickpea allergic patients show individual and heterogeneous IgE-sensitization profiles with extracts from raw and boiled chickpeas. Chickpea proteins pathogenesis related protein family 10 (PR-10), a late embryogenesis abundant protein (LEA/DC-8), and a vicilin-containing fraction, but not 2S albumin, shows IgE reactivity with sera from chickpea, birch pollen, and peanut sensitized patients. Remarkably, allergenic vicilin, DC-8, and PR-10 are detected in the extract of boiled chickpeas. CONCLUSION: Several IgE-reactive chickpea allergens are identified. For the first time a yet not classified DC-8 protein is characterized as minor allergen (Cic a 1). Finally, the data suggest a potential risk for peanut allergic patients by IgE cross-reactivity with homologous chickpea proteins.


Asunto(s)
Alérgenos/inmunología , Cicer/inmunología , Hipersensibilidad a los Alimentos/inmunología , Proteínas de Vegetales Comestibles/inmunología , Adulto , Alérgenos/química , Niño , Preescolar , Culinaria , Electroforesis en Gel de Poliacrilamida , Femenino , Humanos , Sueros Inmunes , Inmunoglobulina E/inmunología , Masculino , Persona de Mediana Edad , Proteínas de Vegetales Comestibles/química , Polen/inmunología
5.
Food Chem ; 331: 127279, 2020 Nov 30.
Artículo en Inglés | MEDLINE | ID: mdl-32563800

RESUMEN

Stability of protein-polyphenol aggregate particles, created by complexing polyphenols from blueberry and muscadine grape pomaces with a rice-pea protein isolate blend, was evaluated in an in vitro gastrointestinal model. Recovery index (RI; % total phenolics present post-digestion) was 69% and 62% from blueberry and muscadine grape protein-polyphenol particles, compared to 23% and 31% for the respective pomace extracts. Anthocyanins RI was 52% and 42% from particles (6% and 13% from pomace extracts), and proanthocyanidins RI was 77% and 73% from particles (25% and 14% from pomace extracts), from blueberry and grape, respectively. Protein-polyphenol particle digests retained 1.5 to 2-fold higher antioxidant capacity and suppressed the expression of pro-inflammatory cytokines, iNOS, IL6, and IL1ß, compared to unmodified extract digests, which only suppressed IL6. Protein-polyphenol particles as a delivery vehicle in foods may confer better stability during gastrointestinal transit, allow protected polyphenols to reach the gut microbiota, and preserve polyphenol bioactivity.


Asunto(s)
Arándanos Azules (Planta)/química , Polifenoles/farmacocinética , Vitis/química , Animales , Antocianinas/análisis , Antiinflamatorios no Esteroideos/farmacocinética , Antioxidantes/análisis , Digestión , Industria de Procesamiento de Alimentos , Frutas/química , Ratones , Extractos Vegetales/química , Extractos Vegetales/farmacocinética , Proteínas de Vegetales Comestibles/química , Proantocianidinas/análisis , Células RAW 264.7
6.
Sci Rep ; 10(1): 5339, 2020 03 24.
Artículo en Inglés | MEDLINE | ID: mdl-32210349

RESUMEN

Bouillon cubes are widely consumed and when fortified with iron could contribute in preventing iron deficiency. We report the development (part I) and evaluation (current part II) of a novel ferric phytate compound to be used as iron fortificant in condiments such as bouillon. Ferric pyrophosphate (FePP), is the compound of choice due to its high stability in foods, but has a modest absorption in humans. Our objective was to assess iron bioavailability from a novel iron fortificant consisting of ferric iron complexed with phytic acid and hydrolyzed corn protein (Fe-PA-HCP), used in bouillon with and without an inhibitory food matrix. In a randomised single blind, cross-over study, we measured iron absorption in healthy adult women (n = 22). In vitro iron bioaccessibility was assessed using a Caco-2 cell model. Iron absorption from Fe-PA-HCP was 1.5% and 4.1% in bouillon with and without inhibitory matrix, respectively. Relative iron bioavailability to FeSO4 was 2.4 times higher than from FePP in bouillon (17% vs 7%) and 5.2 times higher when consumed with the inhibitory meal (41% vs 8%). Similar results were found in vitro. Fe-PA-HCP has a higher relative bioavailability versus FePP, especially when bouillon is served with an inhibitory food matrix.


Asunto(s)
Compuestos Férricos/farmacocinética , Alimentos Fortificados , Hierro/farmacocinética , Ácido Fítico/química , Adulto , Células CACO-2 , Estudios Cruzados , Femenino , Compuestos Férricos/química , Ferritinas/sangre , Humanos , Hidrólisis , Radioisótopos de Hierro/farmacocinética , Proteínas de Vegetales Comestibles/química , Método Simple Ciego , Adulto Joven , Zea mays/química
7.
Bioprocess Biosyst Eng ; 41(7): 1039-1049, 2018 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-29654357

RESUMEN

Food rest materials have the potential to be used as media components in various types of fermentations. Oleaginous filamentous fungi can utilize those components and generate a high-value lipid-rich biomass, which could be further used for animal and human use. One of the main limitations in this process is the pretreatment of food rest materials, needed to provide homogenization, sterilization and solubilization. In this study, two pretreatment processes-steam explosion and enzymatic hydrolysis-were evaluated for potato and animal protein-rich food rest materials. The pretreated food rest materials were used for the production of fungal lipid-rich biomass in submerged fermentation by the oleaginous fungus Mucor circinelloides. Cultivation media based on malt extract broth and glucose were used as controls of growth and lipid production, respectively. It was observed that media based on food rest materials can support growth and lipid production in M. circinelloides to a similar extent as the control media. More specifically, the use of potato hydrolysate combined with chicken auto-hydrolysate resulted in a higher fungal total biomass weight than using malt extract broth. When the same C/N ratio was used for glucose and rest materials-based media, similar lipid content was obtained or even higher using the latter media.


Asunto(s)
Biomasa , Lípidos/biosíntesis , Mucor/crecimiento & desarrollo , Proteínas de Vegetales Comestibles/química , Solanum tuberosum/química , Animales , Pollos , Hidrólisis
8.
Eur J Nutr ; 57(3): 1157-1168, 2018 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-28324208

RESUMEN

PURPOSE: This study examined the effect of soy proteins with depletion of different subunits of the two major storage proteins, ß-conglycinin and glycinin, on hepatic lipids and proteins involved in lipid metabolism in rats, since the bioactive component of soy responsible for lipid-lowering is unclear. METHODS: Weanling Sprague Dawley rats were fed diets containing either 20% casein protein in the absence (casein) or presence (casein + ISF) of isoflavones or 20% alcohol-washed soy protein isolate (SPI) or 20% soy protein concentrates derived from a conventional (Haro) or 2 soybean lines lacking the α' subunit of ß-conglycinin and the A1-3 (1TF) or A1-5 (1a) subunits of glycinin. After 8 weeks, the rats were necropsied and liver proteins and lipids were extracted and analysed. RESULTS: The results showed that soy protein diets reduced lipid droplet accumulation and content in the liver compared to casein diets. The soy protein diets also decreased the level of hepatic mature SREBP-1 and FAS in males, with significant decreases in diets 1TF and 1a compared to the casein diets. The effect of the soy protein diets on female hepatic mature SREBP-1, FAS, and HMGCR was confounded since casein + ISF decreased these levels compared to casein alone perhaps muting the decrease by soy protein. A reduction in both phosphorylated and total STAT3 in female livers by ISF may account for the gender difference in mechanism in the regulation and protein expression of the lipid modulators. CONCLUSIONS: Overall, soy protein deficient in the α' subunit of ß-conglycinin and A1-5 subunits of glycinin maintain similar hypolipidemic function compared to the conventional soy protein. The exact bioactive component(s) warrant identification.


Asunto(s)
Antígenos de Plantas/uso terapéutico , Globulinas/uso terapéutico , Hiperlipidemias/prevención & control , Metabolismo de los Lípidos , Hígado/metabolismo , Proteínas de Vegetales Comestibles/uso terapéutico , Subunidades de Proteína/uso terapéutico , Proteínas de Almacenamiento de Semillas/uso terapéutico , Proteínas de Soja/uso terapéutico , Animales , Antígenos de Plantas/química , Antígenos de Plantas/genética , Antígenos de Plantas/metabolismo , Caseínas/efectos adversos , Dieta Alta en Grasa/efectos adversos , Femenino , Alimentos Modificados Genéticamente , Globulinas/química , Globulinas/genética , Globulinas/metabolismo , Hiperlipidemias/etiología , Hiperlipidemias/metabolismo , Hiperlipidemias/patología , Gotas Lipídicas/metabolismo , Gotas Lipídicas/patología , Hígado/enzimología , Hígado/patología , Masculino , Fosforilación , Proteínas de Vegetales Comestibles/química , Proteínas de Vegetales Comestibles/genética , Proteínas de Vegetales Comestibles/metabolismo , Plantas Modificadas Genéticamente/genética , Plantas Modificadas Genéticamente/metabolismo , Procesamiento Proteico-Postraduccional , Subunidades de Proteína/química , Subunidades de Proteína/genética , Subunidades de Proteína/metabolismo , Ratas Sprague-Dawley , Factor de Transcripción STAT3/metabolismo , Proteínas de Almacenamiento de Semillas/química , Proteínas de Almacenamiento de Semillas/genética , Proteínas de Almacenamiento de Semillas/metabolismo , Caracteres Sexuales , Proteínas de Soja/química , Proteínas de Soja/genética , Proteínas de Soja/metabolismo , Vacuolas/patología , Destete
9.
J Sci Food Agric ; 97(3): 882-888, 2017 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-27198121

RESUMEN

BACKGROUND: Alfalfa is considered a potential feedstock for biofuels; co-products with value-added uses would enhance process viability. This work evaluated dried alfalfa leaves for protein production and describes the functional properties of the protein. RESULTS: Dried alfalfa leaves contained 260 g kg-1 dry basis (DB) crude protein, with albumins being the major fraction (260 g kg-1 of total protein). Alkali solubilization for 2 h at 50 °C, acid precipitation, dialysis, and freeze-drying produced a protein concentrate (600 g kg-1 DB crude protein). Alfalfa leaf protein concentrate showed moderate solubility (maximum 500 g kg-1 soluble protein from pH 5.5 to 10), excellent emulsifying properties (activity 158-219 m2 g-1 protein, stability 17-49 min) and minimal loss of solubility during heating at pH ≥ 7.0. CONCLUSIONS: It is technically feasible to extract protein with desirable emulsifying and heat stability properties from dried alfalfa leaves; however, the dried form may not be a practical starting material for protein production, given the difficulty of achieving high yields and high-purity protein product. © 2016 Society of Chemical Industry.


Asunto(s)
Producción de Cultivos , Productos Agrícolas/química , Emulsionantes/aislamiento & purificación , Aditivos Alimentarios/aislamiento & purificación , Medicago sativa/química , Hojas de la Planta/química , Proteínas de Vegetales Comestibles/aislamiento & purificación , Precipitación Química , Diálisis , Emulsionantes/química , Estudios de Factibilidad , Aditivos Alimentarios/química , Liofilización , Calor/efectos adversos , Concentración de Iones de Hidrógeno , Medio Oeste de Estados Unidos , Tamaño de la Partícula , Extractos Vegetales/química , Extractos Vegetales/aislamiento & purificación , Proteínas de Vegetales Comestibles/química , Tallos de la Planta/química , Estabilidad Proteica , Solubilidad , Agua/análisis
11.
J Sci Food Agric ; 96(11): 3890-6, 2016 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-26696599

RESUMEN

BACKGROUND: Rice bran protein (RBP) is a valuable plant protein which has unique nutritional and hypoallergenic properties. Whey proteins have wide applications in the food industry, such as in dairy, meat and bakery products. RESULTS: Whey protein concentrate (WPC), RBP and their mixtures at different ratios (1:1, 1:2, 1:5 and 1:10 w/w) were heated from 20 to 90 °C at different heating rates (0.5, 1, 5 and 10 °C min(-1) ). The storage modulus (G') and gelling point (Tgel ) of WPC were higher than those of RBP, indicating the good ability of WPC to develop stiffer networks. By increasing the proportion of WPC in mixed systems, G' was increased and Tgel was reduced. Nevertheless, the elasticity of all binary mixtures was lower than that of WPC alone. Tgel and the final G' of RBP-WPC blends were increased by raising the heating rate. The RBP-WPC mixtures developed more elastic gels than RBP alone at different heating rates. RBP had a fibrillar and lentil-like structure whose fibril assembly had smaller structures than those of WPC. CONCLUSION: The gelling structure of the mixed gel of WPC-RBP was improved by adding WPC. Indeed, by adding WPC, gels tended to show syneresis and had lower water-holding capacity. Furthermore, the gel structure was produced by adding WPC to the non-gelling RBP, which is compatible with whey and can be applied as a functional food for infants and/or adults. © 2015 Society of Chemical Industry.


Asunto(s)
Manipulación de Alimentos/métodos , Residuos Industriales/análisis , Oryza/química , Epidermis de la Planta/química , Proteínas de Vegetales Comestibles/química , Semillas/química , Suero Lácteo/química , Fenómenos Químicos , Suplementos Dietéticos/análisis , Suplementos Dietéticos/economía , Industria de Procesamiento de Alimentos/economía , Alimentos Especializados/análisis , Alimentos Especializados/economía , Geles , Calor/efectos adversos , Humanos , Residuos Industriales/economía , Irán , Fenómenos Mecánicos , Valor Nutritivo , Proteínas de Vegetales Comestibles/economía , Proteínas de Vegetales Comestibles/ultraestructura , Reología/métodos , Factores de Tiempo , Temperatura de Transición , Agua/análisis , Suero Lácteo/economía , Proteína de Suero de Leche/química , Proteína de Suero de Leche/economía , Proteína de Suero de Leche/ultraestructura
12.
J Food Sci ; 80(12): S2950-6, 2015 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-26550775

RESUMEN

The study evaluated panela cheeses made from dairy-plant protein blends, using soybean or peanut protein isolates, supplemented with transglutaminase (TG). Plant proteins were isolated using an alkaline extraction method followed by acid precipitation, and added to the dairy system in order to increase 50% or 100% the protein concentration. The total protein extraction for peanut and soybean isolates was 30.3% and 54.6%, respectively (based on initial protein content of sources), and no impairment of their essential amino acid profile was detected. Cheeses supplemented with TG and soybean showed the highest moisture and crude yield (>67.8% and 20.7%, respectively), whereas protein content was higher in the peanut isolate--added samples without TG (>67.4%). Cheese solids yield (ratio between final and initial solids) was higher for treatments with TG and 100% of plant protein addition (>50.7%). Regarding texture, 4 parameters were measured: hardness, cohesiveness, chewiness, and springiness. All cheeses containing soybean isolates and TG presented the highest chewiness and cohesiveness values, similar to those of the control treatment. Springiness was similar for all treatments, but hardness was higher in cheeses prepared with the peanut protein isolate added with TG. From these results it can be concluded that panela cheeses can be elaborated following a traditional procedure, but with the addition of soybean or peanut protein to the dairy ingredients. Cheeses containing these protein isolates showed higher protein than the milk control cheese and similar textural characteristics.


Asunto(s)
Arachis/química , Queso/análisis , Manipulación de Alimentos/métodos , Glycine max/química , Leche/química , Proteínas de Vegetales Comestibles/química , Transglutaminasas , Animales , Suplementos Dietéticos , Humanos , Proteínas de Vegetales Comestibles/aislamiento & purificación
13.
J Agric Food Chem ; 62(32): 8204-13, 2014 Aug 13.
Artículo en Inglés | MEDLINE | ID: mdl-25058384

RESUMEN

Previously developed radical-scavenging pea protein hydrolysates (PPHs) prepared with Flavourzyme (Fla-PPH) and Protamex (Pro-PPH) were used as cosurfactants with Tween 20 to produce soybean oil-in-water (O/W) emulsions, and the suppression of lipid oxidation was investigated. Both PPHs significantly retarded oxidation (P < 0.05) of the emulsions when stored at 37 °C for 14 days. Electron microscopy revealed an interfacial peptidyl membrane around oil droplets, which afforded steric restrictions to oxidation initiators. When licorice extract (LE) was also used in emulsion preparation, a remarkable synergistic oxidation inhibition was observed with both PPHs. LE adsorbed onto oil droplets either directly or through associating with PPH to produce a thick and compact interfacial membrane enabling the defense against oxygen species. Liquiritin apioside, neolicuroside, glabrene, and 18ß-glycyrrhetic acid were the predominant phenolic derivatives partitioning at the interface and most likely the major contributors to the notable synergistic antioxidant activity when coupled with PPHs.


Asunto(s)
Antioxidantes/química , Glycyrrhiza/química , Pisum sativum/química , Extractos Vegetales/química , Proteínas de Vegetales Comestibles/química , Hidrolisados de Proteína/química , Aceite de Soja/química , Emulsionantes/agonistas , Emulsionantes/química , Emulsionantes/metabolismo , Emulsiones , Endopeptidasas/metabolismo , Flavonoides/agonistas , Flavonoides/química , Conservantes de Alimentos/química , Conservantes de Alimentos/metabolismo , Almacenamiento de Alimentos , Glucósidos/agonistas , Glucósidos/química , Oxidación-Reducción , Extractos Vegetales/agonistas , Proteínas de Vegetales Comestibles/agonistas , Proteínas de Vegetales Comestibles/metabolismo , Raíces de Plantas/química , Hidrolisados de Proteína/agonistas , Estabilidad Proteica , Proteínas de Almacenamiento de Semillas/agonistas , Proteínas de Almacenamiento de Semillas/química , Proteínas de Almacenamiento de Semillas/metabolismo , Semillas/química , Propiedades de Superficie
14.
Nutrition ; 28(11-12): 1180-5, 2012.
Artículo en Inglés | MEDLINE | ID: mdl-22858204

RESUMEN

OBJECTIVE: The present study identified the effects of heat oxidation on protein carbonyl content and α,α-diphenyl-ß-picrylhydrazyl (DPPH) free radical-scavenging activity in soy protein. The changes on antioxidant status in male mice fed a heat-oxidized diet were also investigated. METHODS: Soy protein heated at 100°C for 30, 60, and 90 min was used to determine the protein carbonyl content and DPPH free radical-scavenging activity in vitro. Male KM mice (3 wk old) were fed a normal diet, an oxidized diet (HD) containing 12% heat-oxidized soy protein, or an HD supplemented with 0.1% lipoic acid. After 4 wk of feeding, apparent digestibility, reactive oxygen species, malondialdehyde, and total antioxidant capacity levels were measured. The antioxidant enzyme activities in serum and tissues were also assayed. RESULTS: Heat-oxidized soy protein showed a significant increase in protein carbonyl formation and a decrease in DPPH free radical-scavenging activity. The HD induced a significant decrease in food intake and apparent digestibility of dry matter and crude protein in mice. Increased levels of reactive oxygen species and malondialdehyde in serum and tissues accompanied by decreased total antioxidant capacity and antioxidant enzyme activities were also observed in HD-fed mice. These changes were partly restored in the lipoic acid-treated group. CONCLUSION: Heat-oxidized soy protein showed a relatively higher protein carbonyl content and a loss of its free radical-scavenging activity in vitro. The heat oxidation also led the soy protein to generate reactive oxygen species, decrease the antioxidant status, and induce redox imbalance in vivo. The heat oxidation of food protein could be a potential health risk in humans.


Asunto(s)
Antioxidantes/química , Manipulación de Alimentos , Estrés Oxidativo , Proteínas de Vegetales Comestibles/efectos adversos , Proteínas de Vegetales Comestibles/química , Proteínas de Soja/efectos adversos , Proteínas de Soja/química , Animales , Antioxidantes/metabolismo , Digestión , Calor/efectos adversos , Peroxidación de Lípido , Masculino , Ratones , Ratones Endogámicos , Oxidación-Reducción , Proteínas de Vegetales Comestibles/metabolismo , Carbonilación Proteica , Conformación Proteica , Desnaturalización Proteica , Distribución Aleatoria , Especies Reactivas de Oxígeno/sangre , Especies Reactivas de Oxígeno/metabolismo , Proteínas de Soja/metabolismo , Ácido Tióctico/química , Ácido Tióctico/metabolismo , Factores de Tiempo
15.
J Food Sci ; 76(1): E158-64, 2011.
Artículo en Inglés | MEDLINE | ID: mdl-21535668

RESUMEN

Microfiltration (MF) membranes with pore sizes of 200 and 450 nm and ultrafiltration (UF) membranes with molecular weight cut off of 50, 100, and 500 kDa were assessed for their ability to eliminate nonprotein substances from okara protein extract in a laboratory cross-flow membrane system. Both MF and UF improved the protein content of okara extract to a similar extent from approximately 68% to approximately 81% owing to the presence of protein in the feed leading to the formation of dynamic layer controlling the performance rather than the actual pore size of membranes. Although normalized flux in MF-450 (117 LMH/MPa) was close to UF-500 (118 LMH/MPa), the latter was selected based on higher average flux (47 LMH) offering the advantage of reduced processing time. Membrane processing of soy extract improved the protein content from 62% to 85% much closer to the target value. However, the final protein content in okara (approximately 80%) did not reach the target value (90%) owing to the greater presence of soluble fibers that were retained by the membrane. Solubility curve of membrane okara protein concentrate (MOPC) showed lower solubility than soy protein concentrate and a commercial isolate in the entire pH range. However, water absorption and fat-binding capacities of MOPC were either superior or comparable while emulsifying properties were in accordance with its solubility. The results of this study showed that okara protein concentrate (80%) could be produced using membrane technology without loss of any true proteins, thus offering value addition to okara, hitherto underutilized. Practical Application: Okara, a byproduct obtained during processing soybean for soymilk, is either underutilized or unutilized in spite of the fact that its protein quality is as good as that of soy milk and tofu. Membrane-processed protein products have been shown to possess superior functional properties compared to conventionally produced protein products. However, the potential of membrane technology has not been exploited for the recovery of okara protein. Our study showed that protein content of okara extract could be improved from approximately 68% to approximately 81% without losing any true proteins in the process.


Asunto(s)
Tecnología de Alimentos , Proteínas de Vegetales Comestibles/química , Proteínas de Vegetales Comestibles/aislamiento & purificación , Proteínas de Soja/química , Proteínas de Soja/aislamiento & purificación , Algoritmos , Emulsionantes/análisis , Emulsionantes/química , Emulsionantes/economía , Emulsionantes/aislamiento & purificación , Emulsiones , Filtración , Industria de Procesamiento de Alimentos/economía , Concentración de Iones de Hidrógeno , Residuos Industriales/análisis , Residuos Industriales/economía , Peso Molecular , Aceites de Plantas/análisis , Proteínas de Vegetales Comestibles/economía , Proteínas de Vegetales Comestibles/metabolismo , Semillas/química , Solubilidad , Proteínas de Soja/economía , Proteínas de Soja/metabolismo , Glycine max/química , Factores de Tiempo , Inhibidores de Tripsina/metabolismo , Ultrafiltración , Agua/análisis
16.
J Sci Food Agric ; 91(6): 1022-31, 2011 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-21328351

RESUMEN

BACKGROUND: Chickpea (Cicer arietinum L.) seeds are a good source of protein that has potential applications in new product formulation and fortification. The main objectives of this study were to analyse the physicochemical, thermal and functional properties of chickpea protein isolates (CPIs) and compare them with those of soy (SPI) and pea (PPI) protein isolates. RESULTS: Extracted CPIs had mean protein contents of 728-853 g kg(-1) (dry weight basis). Analysis of their deconvoluted Fourier transform infrared spectra gave secondary structure estimates of 25.6-32.7% α-helices, 32.5-40.4% ß-sheets, 13.8-18.9% turns and 16.3-19.2% disordered structures. CPIs from CDC Xena, among Kabuli varieties, and Myles, among Desi varieties, as well as SPI had the highest water-holding and oil absorption capacities. The emulsifying properties of Kabuli CPIs were superior to those of PPI and Desi CPIs and as good as those of SPI. The heat-induced gelation properties of CPIs showed a minimum protein concentration required to form a gel structure ranging from 100 to 140 g L(-1) . Denaturation temperatures and enthalpies of CPIs ranged from 89.0 to 92.0 °C and from 2.4 to 4.0 J g(-1) respectively. CONCLUSION: The results suggest that most physicochemical, thermal and functional properties of CPIs compare favourably with those of SPI and are better than those of PPI. Hence CPI may be suitable as a high-quality substitute for SPI in food applications.


Asunto(s)
Cicer/metabolismo , Emulsionantes/química , Glycine max/metabolismo , Pisum sativum/metabolismo , Proteínas de Vegetales Comestibles/química , Semillas/metabolismo , Canadá , Fenómenos Químicos , Elasticidad , Emulsionantes/aislamiento & purificación , Emulsionantes/metabolismo , Tecnología de Alimentos , Geles , Calor/efectos adversos , Pigmentación , Aceites de Plantas/análisis , Proteínas de Vegetales Comestibles/aislamiento & purificación , Proteínas de Vegetales Comestibles/metabolismo , Desnaturalización Proteica , Estabilidad Proteica , Estructura Secundaria de Proteína , Especificidad de la Especie , Espectroscopía Infrarroja por Transformada de Fourier , Agua/análisis
17.
J Oleo Sci ; 59(3): 115-20, 2010.
Artículo en Inglés | MEDLINE | ID: mdl-20124752

RESUMEN

It has been reported that oil heated with vegetable protein under reduced pressure, followed by filtration (soy oil), decreased body, liver and retroperitoneal fat tissue weights and serum triacylglycerol levels in Wistar rats. In order to clarify the mechanism of these weight-loss promoting effects, gastrointestinal tract content transfer was traced. Fasted 10-week-old rats were fed a slurry containing AIN93G without fat, Cr(2)O(3) (marker), and 7 wt% soy oil or fresh oil (control) and sacrificed at 20, 60, 120, or 360 min; then, blood, stomach, small intestine, cecum, colon and feces were collected. The results indicated that the content transferred faster from stomach to small intestine in the soy oil group than in the control group. At 60 min after the ingestion of diet, an increased serum triacylglycerol level was found in the soy oil group. In addition, fecal excretion in the soy oil group was significantly higher 120 min after the administration than in the control group, suggesting that soy oil stimulated peristalsis of the colon and that colon contents (food ingested before administration) were actively excreted.


Asunto(s)
Tracto Gastrointestinal/efectos de los fármacos , Tracto Gastrointestinal/metabolismo , Peristaltismo/efectos de los fármacos , Aceites de Plantas/farmacología , Proteínas de Vegetales Comestibles/química , Temperatura , Tejido Adiposo/efectos de los fármacos , Tejido Adiposo/metabolismo , Animales , Transporte Biológico/efectos de los fármacos , Peso Corporal/efectos de los fármacos , Colon/efectos de los fármacos , Colon/metabolismo , Dieta , Heces/química , Tamaño de los Órganos/efectos de los fármacos , Especificidad de Órganos/efectos de los fármacos , Aceites de Plantas/administración & dosificación , Aceites de Plantas/análisis , Ratas , Ratas Wistar , Triglicéridos/sangre
18.
Anal Bioanal Chem ; 396(1): 443-56, 2010 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-19841911

RESUMEN

This review gives an overview of current knowledge about 3-monochloropropane-1,2-diol (3-MCPD) formation and detection. Although 3-MCPD is often mentioned with regard to soy sauce and acid-hydrolysed vegetable protein (HVP), and much research has been done in that area, the emphasis here is placed on other foods. This contaminant can be found in a great variety of foodstuffs and is difficult to avoid in our daily nutrition. Despite its low concentration in most foods, its carcinogenic properties are of general concern. Its formation is a multivariate problem influenced by factors such as heat, moisture and sugar/lipid content, depending on the type of food and respective processing employed. Understanding the formation of this contaminant in food is fundamental to not only preventing or reducing it, but also developing efficient analytical methods of detecting it. Considering the differences between 3-MCPD-containing foods, and the need to test for the contaminant at different levels of food processing, one would expect a variety of analytical approaches. In this review, an attempt is made to provide an up-to-date list of available analytical methods and to highlight the differences among these techniques. Finally, the emergence of 3-MCPD esters and analytical techniques for them are also discussed here, although they are not the main focus of this review.


Asunto(s)
Compuestos Alílicos/análisis , Pan , Grano Comestible/química , Glicerol/análogos & derivados , Proteínas de Vegetales Comestibles/química , Alimentos de Soja , Compuestos Alílicos/química , Queso , Café/química , Glicerol/análisis , Glicerol/química , Hidrocarburos Clorados , Estructura Molecular , Alimentos de Soja/análisis , alfa-Clorhidrina
19.
Indian J Exp Biol ; 47(3): 169-75, 2009 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-19405381

RESUMEN

Rats fed with alcohol (18%) at 3.76 g/day for 45 days showed significant reduction in body weight, glutathione (GSH) content and activities of superoxide dismutase (SOD) and catalase in liver. Lecithin cholesterol acyltransferase (LCAT) in plasma, levels of HDL cholesterol in serum, hepatic bile acid production and fecal excretion of neutral sterols also showed significant reduction. Simultaneous feeding of garlic protein (GP) or soy protein (SP) (500 mg/kg body weight/day for 45 days) to alcohol fed groups increased each of above parameters significantly towards normal values. Increase in GSH content and catalase activity in liver, was significantly higher for SP treated group than for GP treated group. However, increase in plasma LCAT was significantly higher for GP treated group than for SP treated group. Alcohol fed rats showed significant increase in liver weight, serum and tissue cholesterol, serum triacylglycerol (TAG), phospholipids (PL) and free fatty acid (FFA) levels and activity of HMGCoA reductase in liver and intestine. Lipid peroxidation, glucose-6 phosphate dehydrogenase (G6PD), glutathione peroxidase (GPx) and glutathione reductase (GR) in liver and incorporation of labeled acetate into liver cholesterol also showed significant increase. GP and SP treated rats showed decrease in these values towards normal. GP feeding showed a better effect than SP in lowering serum and heart total cholesterol, and in maintaining GPx at near normal level, while SP feeding showed a better effect in lowering serum FFA level and maintaining GR activity at near normal level. In suppressing incorporation of labeled acetate into serum cholesterol, GP feeding showed a better effect than SP. Antiatherogenic and antiperoxidative effects of these proteins may be due to lower lysine/arginine ratio.


Asunto(s)
Consumo de Bebidas Alcohólicas/metabolismo , Aterosclerosis/prevención & control , Ajo/química , Peroxidación de Lípido/efectos de los fármacos , Hígado/efectos de los fármacos , Proteínas de Vegetales Comestibles/farmacología , Proteínas de Soja/farmacología , Aminoácidos/análisis , Animales , Aterosclerosis/sangre , Lípidos/sangre , Hígado/enzimología , Hígado/metabolismo , Pruebas de Función Hepática , Masculino , Proteínas de Vegetales Comestibles/administración & dosificación , Proteínas de Vegetales Comestibles/química , Ratas , Ratas Sprague-Dawley , Proteínas de Soja/administración & dosificación , Proteínas de Soja/química
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