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1.
Food Res Int ; 99(Pt 3): 971-978, 2017 09.
Artigo em Inglês | MEDLINE | ID: mdl-28865623

RESUMO

A protein extract from the brown seaweed Himanthalia elongata (Linnaeus) S. F. Gray was prepared and its functional properties, colour and amino acid composition were assessed for its potential future use by the food industry. The total content of amino acids was determined as 54.02±0.46gaminoacids/kg dry weight, with high levels of the essential amino acids lysine and methionine. SDS-PAGE showed 5 protein bands with molecular weights of 71.6, 53.7, 43.3, 36.4 and 27.1kDa. The water holding capacity and oil holding capacity were determined as 10.27±0.09gH2O/g and 8.1±0.07goil/g respectively. Foaming activity and stability were higher at alkaline pH values. The emulsifying capacity and stability of the extract varied depending on the pH and oil used. These results demonstrate the potential use of Himanthalia elongata protein extract in the food industry.


Assuntos
Emulsificantes/farmacologia , Aditivos Alimentares/farmacologia , Phaeophyceae/química , Proteínas de Plantas/farmacologia , Alga Marinha/química , Sequência de Aminoácidos , Cor , Emulsificantes/isolamento & purificação , Aditivos Alimentares/isolamento & purificação , Indústria Alimentícia/métodos , Proteínas de Plantas/isolamento & purificação , Solubilidade
2.
J Food Sci ; 77(4): C333-9, 2012 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-22429318

RESUMO

Effect of acylation with saturated fatty acids on surface functional properties of tofu whey-derived peptides was investigated. Tofu whey (TW) and soy proteins (7S, 11S, and acid-precipitated soy protein [APP]) were hydrolyzed by Protease M 'Amano' G, and resulting peptide mixtures were acylated with esterified fatty acids of different chain length (6C to 18C) to form a covalent linkage between the carboxyl group of fatty acid and the free amino groups of peptide. Acylation significantly (P < 0.05) increased emulsifying properties of 7S, 11S, and APP peptides independent of fatty acid chain length. Acylation decreased water binding capacity although oil binding capacity of acylated tofu whey ultra filtered fraction (UFTW < 3 kDa), 7S- and 11S-peptides were improved compared to native peptides. 7S peptides acylated with long chain fatty acids had shown significant higher surface hydrophobicity as in contrast with acylated UFTW < 3 kDa and APP peptides. Fluorescence spectra studies revealed structural conformation of acylated soy peptides as compared to native peptides. This study shows that chemical modification with fatty acids can further affect functional properties of soy proteins.


Assuntos
Emulsificantes/química , Ácidos Graxos/química , Aditivos Alimentares/química , Lipopeptídeos/química , Fragmentos de Peptídeos/química , Proteínas de Vegetais Comestíveis/química , Proteínas de Soja/química , Acilação , Antígenos de Plantas/química , Antígenos de Plantas/metabolismo , Fenômenos Químicos , Emulsificantes/economia , Emulsificantes/isolamento & purificação , Emulsificantes/metabolismo , Endopeptidases/metabolismo , Aditivos Alimentares/economia , Aditivos Alimentares/isolamento & purificação , Aditivos Alimentares/metabolismo , Indústria de Processamento de Alimentos/economia , Globulinas/química , Globulinas/metabolismo , Interações Hidrofóbicas e Hidrofílicas , Resíduos Industriais/análise , Resíduos Industriais/economia , Lipopeptídeos/isolamento & purificação , Lipopeptídeos/metabolismo , Peso Molecular , Fragmentos de Peptídeos/isolamento & purificação , Fragmentos de Peptídeos/metabolismo , Proteínas de Vegetais Comestíveis/isolamento & purificação , Proteínas de Vegetais Comestíveis/metabolismo , Conformação Proteica , Proteínas de Armazenamento de Sementes/química , Proteínas de Armazenamento de Sementes/metabolismo , Proteínas de Soja/isolamento & purificação , Proteínas de Soja/metabolismo , Propriedades de Superfície , Ultrafiltração , Água/análise
3.
J Food Sci ; 76(3): E266-73, 2011 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-21535826

RESUMO

UNLABELLED: Canola meal protein isolates were prepared from defatted canola meal flour using alkaline solubilization and acid precipitation. A central composite design was used to model 2nd-order response surfaces for the protein yield and the functional properties of protein isolates. The solubilization pH and precipitation pH were used as design factors. The models showed that the protein yield and functional properties of isolates, such as water absorption and fat absorption, were sensitive to both solubilization pH and precipitation pH, whereas the emulsification was sensitive to only solubilization pH. Gel electrophoresis analysis of protein fractions gave evidence to the compositional changes between proteins isolated under different conditions. Differences in glass transition temperatures suggest that proteins tend to be more denatured when solubilized at highly alkaline conditions. These conformational and compositional changes due to different protein separation conditions have contributed to the changes in functional properties of protein isolates. PRACTICAL APPLICATION: Protein isolation conditions may be determined primarily through optimization of total protein yield. Improvements in protein functional properties may be achieved with a relatively small sacrifice in yield by altering isolation conditions.


Assuntos
Brassica rapa/química , Proteínas Alimentares/análise , Proteínas Alimentares/isolamento & purificação , Proteínas de Plantas/química , Proteínas de Plantas/isolamento & purificação , Sementes/química , Precipitação Química , Proteínas Alimentares/economia , Emulsificantes/química , Emulsificantes/economia , Emulsificantes/isolamento & purificação , Ácidos Graxos Monoinsaturados/análise , Indústria de Processamento de Alimentos/economia , Concentração de Íons de Hidrogênio , Interações Hidrofóbicas e Hidrofílicas , Resíduos Industriais/análise , Resíduos Industriais/economia , Cinética , Modelos Químicos , Peso Molecular , Proteínas de Plantas/economia , Desnaturação Proteica , Óleo de Brassica napus , Solubilidade , Propriedades de Superfície , Temperatura , Água/análise
4.
J Food Sci ; 76(1): E158-64, 2011.
Artigo em Inglês | MEDLINE | ID: mdl-21535668

RESUMO

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.


Assuntos
Tecnologia de Alimentos , Proteínas de Vegetais Comestíveis/química , Proteínas de Vegetais Comestíveis/isolamento & purificação , Proteínas de Soja/química , Proteínas de Soja/isolamento & purificação , Algoritmos , Emulsificantes/análise , Emulsificantes/química , Emulsificantes/economia , Emulsificantes/isolamento & purificação , Emulsões , Filtração , Indústria de Processamento de Alimentos/economia , Concentração de Íons de Hidrogênio , Resíduos Industriais/análise , Resíduos Industriais/economia , Peso Molecular , Óleos de Plantas/análise , Proteínas de Vegetais Comestíveis/economia , Proteínas de Vegetais Comestíveis/metabolismo , Sementes/química , Solubilidade , Proteínas de Soja/economia , Proteínas de Soja/metabolismo , Glycine max/química , Fatores de Tempo , Inibidores da Tripsina/metabolismo , Ultrafiltração , Água/análise
5.
J Agric Food Chem ; 58(18): 10162-8, 2010 Sep 22.
Artigo em Inglês | MEDLINE | ID: mdl-20735032

RESUMO

The results of the present study show that Lactobacillus pentosus can produce extracellular bioemulsifiers by utilizing hemicellulosic sugars from grape marc as a source of carbon. The effectiveness of these bioemulsifiers (LPEM) was studied by preparing kerosene/water (K/W) emulsions in the presence and absence of these emulsifiers. Various parameters such as relative emulsion volume (EV), stabilizing capacity (ES), viscosity, and droplet size of K/W emulsions were measured. The EV values for K/W emulsions stabilized by concentrated LPEM were approximately 74.5% after 72 h of emulsion formation, with ES values of 97%. These values were higher than those obtained with dodecyl sodium sulfate as emulsifier (EV=62.3% and ES=87.7%). Additionally, K/W emulsions stabilized by LPEM produced polydisperse emulsions containing droplets of radius between 10 and 40 µm, which were smaller than those obtained for K/W emulsions without LPEM (droplet radius=60-100 µm). Moreover, the viscosity values of the K/W emulsions without and with LPEM were approximately 236 and 495 cP, respectively.


Assuntos
Emulsificantes/química , Fermentação , Querosene , Lactobacillus/metabolismo , Polissacarídeos/química , Água , Fenômenos Químicos , Emulsificantes/isolamento & purificação , Emulsificantes/metabolismo , Emulsões , Indústria de Processamento de Alimentos/economia , Frutas/química , Resíduos Industriais/análise , Resíduos Industriais/economia , Polissacarídeos/isolamento & purificação , Polissacarídeos/metabolismo , Vitis/química
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