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1.
Crit Rev Food Sci Nutr ; 60(2): 276-297, 2020.
Artigo em Inglês | MEDLINE | ID: mdl-30596255

RESUMO

Resistant starch (RS) plays a key role in providing metabolic and colonic health benefits. In particular, RS type III (RS3) is of great interest because of its thermal stability and its preserved nutritional functionality. RS3 can be prepared by physical treatment, including high hydrostatic pressure, ultrasound, extrusion, autoclaving, microwave cooking, and heat-moisture treatment. The acid and enzymatic hydrolysis can also be applied to facilitate the generation of small molecules, which increases the inherent crystallinity of RS3 upon retrogradation. Depending on processing conditions, RS3 with diversified structural characteristics can be formed. These structures play a key role in determining the physiological behavior of RS3. Therefore, a deep understanding of the structural rearrangement pattern during different processing treatment is of great importance for regulating the molecular structure of RS3 and thereby its corresponding physiological properties. This review thus focuses on the past and current status of research into the in-depth study of RS3 formation mechanism and the changes to RS3 structural characteristics under different processing conditions. The objective was to provide a theoretical guidance for the rational selection of preparation methods for RS3 and for designing RS3 structures with specific physiological functionalities for relevant industrial applications.


Assuntos
Culinária , Amido , Hidrólise
2.
Int J Biol Macromol ; 120(Pt A): 650-656, 2018 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-30165145

RESUMO

Pea starch (S) was modified by autoclaving (A), α-amylolysis (E), and pullulanase debranching (P), the effect of pretreatments including autoclaving and α-amylolysis on the structural modifications to the pullulanase debranched starch was investigated. All processed pea starch was transformed from a C- to a B-type crystalline structure. The power law exponent (α) ranging from 1.85 to 2.64 suggested the existence of mass fractal structure. Compared with native starch, all treatments applied caused an enhanced short-range order which was reflected by the increased values of α, degree of double helix (DD), degree of order (DO), and double helix content based on SAXS, FTIR, and 13CNMR observations. The processed starch sample of AS, and APS exhibited the highest DO, and α values, as well as the stronger absorption peak between 3000 and 3695 cm-1on FT-IR spectrum. AEPS exhibited the significantly highest double helix content, indicating that the higher extent of degradation induced by the combined treatments of autoclaving, α-amylolysis, and pullulanase debranching would give the molecular chains a higher alignment opportunity for the evolution towards coil-to-helix transition. The results would be helpful for better understanding the structure-processing relationship and to provide theoretical foundation for the development of food ingredients with targeted functional properties.


Assuntos
Glicosídeo Hidrolases/química , Pisum sativum/química , Amido/química , alfa-Amilases/química , Pressão do Ar , Configuração de Carboidratos , Temperatura Alta , Hidrólise , Transição de Fase , Amido/isolamento & purificação
3.
Food Chem ; 263: 163-170, 2018 Oct 15.
Artigo em Inglês | MEDLINE | ID: mdl-29784302

RESUMO

This work focused on the structural characterization of resistant starch from untreated (UL-RS), germinated (GL-RS), fermented (FL-RS), microwaved (ML-RS), conventionally cooked (CL-RS), and autoclaved (AL-RS) lentil seeds. The size exclusion chromatography (SEC) results showed that UL-RS, RL-RS, and GL-RS (Group A samples) exhibited higher values of Mw and Rh¯ than FL-RS, ML-RS, AL-RS (Group C samples), and CL-RS (Group B sample). In parallel with the SEC result, other structural characteristics followed similar trends, where Group C samples exhibited the lowest values of double helix content and crystallinity by 13C NMR, and degree of order/double helix by FT-IR. Comparatively, Group A samples exhibited the opposite trends, and displayed large amorphous aggregates on their micrograph. The results are expected to provide information for better understanding the mechanism of resistant starch formation during different processing of lentil and to lay a theoretical foundation for the future study of their structure-function relationship.


Assuntos
Culinária/métodos , Lens (Planta)/química , Sementes/química , Amido/química , Cromatografia em Gel , Fermentação , Germinação , Espectroscopia de Ressonância Magnética , Micro-Ondas , Espectroscopia de Infravermelho com Transformada de Fourier
4.
Crit Rev Food Sci Nutr ; 58(7): 1059-1083, 2018 May 03.
Artigo em Inglês | MEDLINE | ID: mdl-27646607

RESUMO

Resistant starch (RS) is defined as the fraction of starch that escapes digestion in the small intestine due to either difficult enzyme/starch contact or to the strength of the crystalline regions formed both in native starch and in those retrograded starch. RS occurs naturally in some foods, and some may be generated in others as the results of several processing conditions. Varieties of techniques have been employed to obtain structural characteristics of RS such as their crystallinity, structural order, chain-length distribution and conformation, helicity, and double-helical structures. These structures play an important role in determining the physiological properties of RS such as their prebiotic and hypoglycaemic properties. However, such topic on structural characterization of RS and their structure-physiological function relationship have not been reviewed in previous literatures. Therefore, this review focuses on the past and current achievements of research on structural characterizations of a range of RS prepared from different sources of native starches as a result of a variety of processing conditions. The potential relationships between the structure and the physiological properties of RS, which is of paramount importance for the furtherance understanding and application of RS, are also reviewed in this study.


Assuntos
Digestão/fisiologia , Amido/química , Animais , Manipulação de Alimentos , Alimento Funcional , Amido/metabolismo
5.
Food Res Int ; 92: 64-78, 2017 02.
Artigo em Inglês | MEDLINE | ID: mdl-28290299

RESUMO

Saskatchewan grown yellow field pea was subjected to different processing conditions including dehulling, micronization, roasting, conventional/microwave cooking, germination, and combined germination and conventional cooking/roasting. Their nutritional and antinutritional compositions, functional properties, microstructure, thermal properties, in vitro protein and starch digestibility, and protein composition were studied. Processed field peas including conventional cooked yellow peas (CCYP), microwave cooked yellow peas (MCYP), germinated-conventional cooked yellow peas (GCCYP), and germinated-roasted yellow peas (GRYP) exhibited the significantly higher in vitro protein digestibility (IVPD), which was in accordance with their significantly lower trypsin inhibitor activity and tannin content. The SDS-PAGE and size exclusion HPLC profiles of untreated pea proteins and their hydrolysates also confirmed the IVPD result that these four treatments facilitated the hydrolysis of pea proteins to a greater extent. The CCYP, MCYP, GCCYP, and GRYP also exhibited significantly higher starch digestibility which was supported by their lower onset (To), peak (Tp), and conclusion (Tc) temperatures obtained from DSC thermogram, their lower pasting properties and starch damage results, as well as their distinguished amorphous flakes' configuration observed on the scanning electron microscopic image. LC/ESI-MS/MS analysis following in-gel digests of SDS-PAGE separated proteins allowed detailed compositional characterization of pea proteins. The present study would provide fundamental information to help to better understand the functionality of field peas as ingredients, and particularly in regards to agri-food industry to improve the process efficiency of field peas with enhanced nutritional and techno-functional qualities.


Assuntos
Manipulação de Alimentos , Proteínas de Ervilha/análise , Pisum sativum/química , Aminoácidos/análise , Cromatografia Líquida , Eletroforese em Gel de Poliacrilamida , Análise de Alimentos , Germinação , Temperatura Alta , Hidrólise , Microscopia Eletrônica de Varredura , Valor Nutritivo , Saskatchewan , Amido/química , Espectrometria de Massas em Tandem , Taninos/análise , Tripsina/análise
6.
J Sci Food Agric ; 96(3): 837-47, 2016 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-25727063

RESUMO

BACKGROUND: Salad dressings supplemented with pulse flours are novel products. A three-factor face-centered central composite design (CCD) was used to determine the effect of pulse flour concentration (3.5%, 7%, 10.5% w/w), egg yolk concentration (3%, 5%, 7% w/w) and oil concentration (20%, 35%, 50% w/w) on the rheological and color characteristics of salad dressings supplemented with pulse flours. RESULTS: The consistency coefficient m, plateau modulus G(N)(0), recoverable strain Q(t) and color values were all affected by the concentrations of pulse flours used. Scanning electron microscopy showed that dressings with lower oil and egg yolk contents had a less densely packed network compared with dressings with higher oil and egg yolk contents. Sensory results were most promising for salad dressings supplemented with the whole green lentil, yellow pea with low flour content, and chickpea with high oil content. CONCLUSION: This study should be useful for designing novel types of salad dressings to meet market requirements as well as helping to increase pulse consumption.


Assuntos
Cicer , Emulsões/química , Alimentos Fortificados/análise , Lens (Planta) , Pisum sativum , Adolescente , Adulto , Idoso , Fenômenos Químicos , Condimentos/análise , Comportamento do Consumidor , Gema de Ovo , Feminino , Humanos , Masculino , Microscopia Eletrônica de Varredura , Pessoa de Meia-Idade , Modelos Teóricos , Valor Nutritivo , Reologia , Sensação , Viscosidade
7.
Biotechnol Res Int ; 2014: 472723, 2014.
Artigo em Inglês | MEDLINE | ID: mdl-24744923

RESUMO

Soybeans and other pulses contain oligosaccharides which may cause intestinal disturbances such as flatulence. This study was undertaken to investigate α -galactosidase-producing probiotics added to frozen foods which can survive warming treatments used in thawing and consumption of the pulses. The maximum α -galactosidase activity (1.26 U/mg protein) was found in Bifidobacterium breve S46. Lactobacillus casei had the highest α -galactosidase thermostability among the various strains, with D values of 35, 29, and 9.3 minutes at 50°C, 55°C, and 60°C, respectively. The enzyme activity was less affected than viable cells by heating. However, the D values of two bacterial enzymes were lower than those of three commercial α -galactosidase-containing products. Freshly grown cells and their enzymes were more stable than the rehydrated cultures and their enzymes. Practical Application. Enzymes and cultures can be added to foods in order to enhance the digestibility of carbohydrates in the gastrointestinal tract. However since many foods are warmed, it is important that the thermostability of the enzymes be assessed. This paper provides data on the stability of α -galactosidase, which could potentially be added to food matrices containing stachyose or raffinose, such as beans.

8.
Food Agric Immunol ; 25(2): 200-208, 2014 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-24587593

RESUMO

Recovery of gluten in buckwheat flour was evaluated as part of an effort to produce wheat-contaminated buckwheat flours that could be used as reference materials (RMs) for testing the presence of gluten in buckwheat. RMs of buckwheat containing 0, 20, 100 and 1000 ppm gluten were created and tested by ELISA. The Gluten-Check kit detected gluten accurately at all levels; RIDASCREEN and Biokits tests were accurate at 20 and 100 ppm levels, but at 1000 ppm both suffered from extraction saturation effect; Veratox kit read 60% higher for the 20 ppm RM (i.e., 31.9 ppm), but close to the target at 100 ppm RM; Veratox R5 kit showed low accuracy with around 30% recovery at 20 and 100 ppm and some 60% at 1000 ppm level. Overall, the results showed variations in recovery among different test kits which could have important implications in the accurate detection of gluten in buckwheat.

9.
Plant Foods Hum Nutr ; 68(3): 306-12, 2013 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-23912803

RESUMO

Glabrous or hairless canaryseed is a nutritional grain that could be a good addition to the diet if approved as a novel food. To assess the impact of thermal treatment on its digestibility; raw, roasted or boiled flours prepared from three different varieties of glabrous canaryseed were subjected to in vitro gastrointestinal digestion conditions and the effect on protein electrophoretic profiles was examined using sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Roasting was done by dry-heat in an oven at 176 °C for 12 min whereas boiling was done in water at 98 °C for 12 min. SDS-PAGE showed approximately twenty-five protein bands in the undigested raw flour with molecular masses (MM) ranging from <14 kDa to >97 kDa. The dominant proteins had low MM, between the ranges of ~57 to 12 kDa. Roasting markedly altered the protein electrophoretic profile with the appearance of large molecular weight aggregates. Canaryseed proteins were more easily digested after thermal treatment and under sequential gastric-duodenal conditions than under gastric or duodenal conditions alone. Furthermore, roasting appeared to have a greater impact on in vitro protein digestibility than boiling.


Assuntos
Digestão , Trato Gastrointestinal/metabolismo , Phalaris/química , Proteínas de Plantas/análise , Proteínas de Plantas/metabolismo , Sementes/química , Animais , Quimotripsina/metabolismo , Duodeno/enzimologia , Eletroforese em Gel de Poliacrilamida , Mucosa Gástrica/enzimologia , Temperatura Alta , Técnicas In Vitro , Pepsina A/metabolismo , Proteínas de Plantas/química , Tripsina/metabolismo
10.
Mol Nutr Food Res ; 57(11): 2029-38, 2013 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-23780918

RESUMO

SCOPE: This study investigated the effects of supplementing different ratios of omega-6 and omega-3 fatty acids (O6H = 10:1, O3O6 = 4:1, and O3H = 1:4) to western-style diets on cow ß-lactoglobulin (BLG) induced allergic reactions in Balb/c mice. METHODS AND RESULTS: Three-week-old mice were randomly assigned to three diet groups (n = 20/group). At 9 wk of age, half of the mice from each dietary treatment (n = 10) were intraperitoneally (i.p.) sensitized with three weekly doses of BLG and alum while the remaining half from each group was sham sensitized (controls). One week after the final sensitization, all mice were orally challenged with BLG. Elevated BLG-specific serum Igs were observed in all sensitized and challenged mice. IFN-γ, MCP-1, and IL-12p40 concentrations from lymphocytes of mesenteric lymph nodes were highest in O3H mice, compared to O3O6 and O6H mice. O6H mice had the highest IL-4 concentrations from splenic lymphocytes and a significantly lower rectal temperature after the challenge in comparison to O3O6 and O3H mice. CONCLUSIONS: Our results suggest that the ω-3 PUFA rich diets alleviated the severity of allergic reactions, and may modulate immune response toward T helper cell (Th)1-favoured immune response while the ω-6 PUFA rich diet exhibited no allergy alleviation with a stronger Th2 polarized immune response.


Assuntos
Dieta , Suplementos Nutricionais , Ácidos Graxos Ômega-3/administração & dosagem , Ácidos Graxos Ômega-6/administração & dosagem , Lactoglobulinas/imunologia , Hipersensibilidade a Leite/prevenção & controle , Animais , Fatores de Transcrição Hélice-Alça-Hélice Básicos/imunologia , Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo , Quimiocina CCL2/sangue , Quimiocina CCL2/imunologia , Modelos Animais de Doenças , Ácidos Graxos Ômega-3/sangue , Ácidos Graxos Ômega-6/sangue , Feminino , Imunoglobulina A/sangue , Imunoglobulina A/imunologia , Imunoglobulina E/sangue , Imunoglobulina E/imunologia , Interferon gama/sangue , Interferon gama/imunologia , Interleucina-12/sangue , Interleucina-12/imunologia , Interleucina-4/imunologia , Interleucina-4/metabolismo , Camundongos , Camundongos Endogâmicos BALB C , Hipersensibilidade a Leite/imunologia , Baço/imunologia , Baço/metabolismo
11.
Foods ; 2(3): 338-349, 2013 Jul 25.
Artigo em Inglês | MEDLINE | ID: mdl-28239119

RESUMO

Although many consumers know that pulses are nutritious, long preparation times are frequently a barrier to consumption of lentils, dried peas and chickpeas. Therefore, a product has been developed which can be used as an ingredient in a wide variety of dishes without presoaking or precooking. Dried green peas, chickpeas or lentils were soaked, cooked, homogenized and spray-dried. Proximate analyses were conducted on the pulse powders and compared to an instant mashed potato product. Because the health benefits of pulses may be due in part to their carbohydrate content, a detailed carbohydrate analysis was carried out on the pulse powders. Pulse powders were higher in protein and total dietary fibre and lower in starch than potato flakes. After processing, the pulse powders maintained appreciable amounts of resistant starch (4.4%-5.2%). Total dietary fibre was higher in chickpeas and peas (26.2% and 27.1% respectively) than lentils (21.9%), whereas lentils had the highest protein content (22.7%). Pulse carbohydrates were rich in glucose, arabinose, galactose and uronic acids. Stachyose, a fermentable fibre, was the most abundant oligosaccharide, making up 1.5%-2.4% of the dried pulse powders. Spray-drying of cooked, homogenized pulses produces an easy to use ingredient with strong nutritional profile.

12.
J Nutr ; 143(2): 136-41, 2013 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-23236021

RESUMO

Probiotic supplementation and oral tolerance induction can reduce certain types of food allergy. The objectives of this study were to investigate the allergy-reducing effects of probiotics (VSL#3) and/or oral tolerance induction via low doses of an allergen supplementation in ß-lactoglobulin (BLG)-sensitized mice. Three-week-old, male BALB/c mice were divided into 6 groups (n = 8/group): sham-sensitized negative control (CTL-), BLG-sensitized positive control (CTL+), oral tolerance-induced and BLG-sensitized group (OT), probiotic-supplemented OT group (OTP), probiotic-supplemented CTL- (PRO), and probiotic-supplemented and BLG-sensitized (PROC) groups. Mice were i.p. sensitized with BLG and alum and then orally challenged with BLG. Immunological responses were assessed by monitoring hypersensitivity scores and measuring levels of BLG-specific serum Igs, total serum IgE and fecal IgA, and cytokines from serum and spleen lysates. Hypersensitivity scores were significantly lower in the PROC (2.00 ± 0.53), OT (0.75 ± 0.46), and OTP mice (1.00 ± 0.53) than in the CTL+ mice (2.63 ± 0.52) as were BLG-specific serum IgE concentrations (34.3 ± 10, 0.442 ± 0.36, 3.54 ± 3.5, and 78.5 ± 8.7 µg/L for PROC, OT, OTP, and CTL+, respectively). Our results suggest that supplementation of VSL#3 suppressed the allergic reaction mainly through increased intestinal secretary IgA (sIgA) in PROC mice, and oral tolerance offered allergen-specific protective effects to BLG-induced allergy, probably through CD4+CD25+ regulatory T cell-mediated active suppression. In OTP mice, probiotics did not induce a further reduction of hypersensitivity score compared with OT mice but may provide additional protection to unforeseen nonspecific challenges through increased intestinal sIgA.


Assuntos
Alérgenos/administração & dosagem , Tolerância Imunológica , Lactoglobulinas/administração & dosagem , Hipersensibilidade a Leite/prevenção & controle , Probióticos/uso terapêutico , Administração Oral , Alérgenos/uso terapêutico , Animais , Bovinos , Citocinas/sangue , Citocinas/metabolismo , Fezes/química , Imunoglobulina A Secretora/análise , Imunoglobulina E/análise , Mucosa Intestinal/imunologia , Mucosa Intestinal/metabolismo , Lactoglobulinas/efeitos adversos , Lactoglobulinas/uso terapêutico , Masculino , Camundongos , Camundongos Endogâmicos BALB C , Hipersensibilidade a Leite/sangue , Hipersensibilidade a Leite/imunologia , Hipersensibilidade a Leite/fisiopatologia , Índice de Gravidade de Doença , Baço/imunologia , Baço/metabolismo , Desmame
13.
J Allergy (Cairo) ; 2012: 746125, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-22187573

RESUMO

Although most consumers show no adverse symptoms to food allergens, health consequences for sensitized individuals can be very serious. As a result, the Codex General Standard for the Labelling of Prepackaged Foods has specified a series of allergenic ingredients/substances requiring mandatory declaration when present in processed prepackaged food products. Countries adhering to international standards are required to observe this minimum of eight substances, but additional priority allergens are included in the list in some countries. Enforcement agencies have traditionally focused their effort on surveillance of prepackaged goods, but there is a growing need to apply a bottom-up approach to allergen risk management in food manufacturing starting from primary food processing operations in order to minimize the possibility of allergen contamination in finished products. The present paper aims to review food production considerations that impact allergen risk management, and it is directed mainly to food manufacturers and policy makers. Furthermore, a series of food ingredients and the allergenic fractions identified from them, as well as the current methodology used for detection of these allergenic foods, is provided.

14.
Allergy Asthma Clin Immunol ; 7: 20, 2011 Dec 06.
Artigo em Inglês | MEDLINE | ID: mdl-22145744

RESUMO

BACKGROUND: Cow's milk allergy (CMA) is one of the most prevalent human food-borne allergies, particularly in infants and young children from developed countries. Our study aims to evaluate the effects of Lactobacillus rhamnosus GG (LGG) administration on CMA development using whole cow's milk proteins (CMP) sensitized Balb/C mice by two different sensitization methods. METHODS: LGG supplemented mice were either sensitized orally with CMP and cholera toxin B-subunit (CTB) as adjuvant, or intraperitoneally (IP) with CMP but without the adjuvant. Mice were then orally challenged with CMP and allergic responses were accessed by monitoring hypersensitivity scores, measuring the levels of CMP-specific immunoglobulins (IgG1, IgG2a and IgG) and total IgE from sera, and cytokines (IL-4 and IFN-γ) from spleen lysates. RESULTS: Sensitization to CMP was successful only in IP sensitized mice, but not in orally sensitized mice with CMP and CTB. Interestingly, LGG supplementation appeared to have reduced cow's milk allergy (CMA) in the IP group of mice, as indicated by lowered allergic responses. CONCLUSIONS: Adjuvant-free IP sensitization with CMP was successful in inducing CMA in the Balb/C mice model. LGG supplementation favourably modulated immune reactions by shifting Th2-dominated trends toward Th1-dominated responses in CMP sensitized mice. Our results also suggest that oral sensitization by the co-administration of CMP and CTB, as adjuvant, might not be appropriate to induce CMA in mice.

15.
J Agric Food Chem ; 55(14): 5819-26, 2007 Jul 11.
Artigo em Inglês | MEDLINE | ID: mdl-17567027

RESUMO

This study examined the immunogenic response of glycinin under varying conditions of pH and ionic strength using enzyme-linked immunosorbent assay. Differential scanning calorimetric (DSC) analysis and Fourier transform infrared spectroscopy (FTIR) were used to investigate the conformational changes induced as a result of these conditions, and the correlation with the changes observed in glycinin immunoreactivity were determined. A highly purified glycinin obtained by isoelectric precipitation followed by native preparative continuous flow electrophoresis was used for these studies. Purity was confirmed by two-dimensional-polyacrylamide gel electrophoresis and mass spectroscopy. DSC and FTIR results suggest that glycinin immunoreactivity is affected by changes in the tertiary and secondary packing of the protein, when flexibility, stability, and accessibility of certain substructures are modified. Aggregation and/or increased compactness of glycinin subcomponents could have potentially prevented epitopes from reacting with the IgG antibodies.


Assuntos
Globulinas/química , Globulinas/imunologia , Glycine max/química , Proteínas de Soja/química , Proteínas de Soja/imunologia , Ensaio de Imunoadsorção Enzimática , Globulinas/isolamento & purificação , Concentração de Íons de Hidrogênio , Concentração Osmolar , Conformação Proteica , Proteínas de Soja/isolamento & purificação , Espectroscopia de Infravermelho com Transformada de Fourier
16.
Crit Rev Food Sci Nutr ; 47(2): 127-43, 2007.
Artigo em Inglês | MEDLINE | ID: mdl-17364698

RESUMO

Soybean is considered one of the "big eight" foods that are believed to be responsible for 90% of all allergenic reactions. Soy allergy is of particular importance, because soybeans are widely used in processed foods and, therefore, represent a particularly insidious source of hidden allergens. Although significant advances have been made in the identification and characterization of soybean allergens, scientists are not completely certain about which proteins in soy cause allergic reactions. At least 16 allergens have been identified. Most of them, as with other plant food allergens, have a metabolic, storage, or protective function. These allergens belong to protein families which have conserved structural features in relation with their biological activity, which explains the wide immunochemical cross-recognition observed among members of the legume family. Detailed analysis of the structure-allergenicity relationships has been hampered by the complexity and heterogeneity of soybean proteins. A variety of technological approaches have been attempted to decrease soybean allergenicity. This paper provides a comprehensive review of the current body of knowledge on the identification and characterization of soybean allergens, as well as an update on current hypoallergenization techniques.


Assuntos
Alérgenos/efeitos adversos , Hipersensibilidade Alimentar/diagnóstico , Hipersensibilidade Alimentar/terapia , Proteínas de Soja/efeitos adversos , Reações Cruzadas , Hipersensibilidade Alimentar/etiologia , Hipersensibilidade Alimentar/prevenção & controle , Humanos , Fosfatidilcolinas/efeitos adversos , Proteínas de Vegetais Comestíveis/efeitos adversos
17.
J Agric Food Chem ; 52(23): 6991-6, 2004 Nov 17.
Artigo em Inglês | MEDLINE | ID: mdl-15537308

RESUMO

Soy protein concentrates produced by combining electroacidification and dead-end ultrafiltration with a membrane of 100 kDa (pH 7 and 6) were compared with concentrates produced by ultrafiltration (pH 9) and a traditional acid precipitation procedure at pH 4.5. Mineral removal during ultrafiltration (mainly potassium, phosphorus, and calcium) was enhanced for the pH 6 electroacidified extract, compared to the extract at pH 9. This yielded a concentrate with improved solubility characteristics. The solubility for the concentrate prepared at pH 6 was enhanced by as high as 45% when compared to the concentrate at pH 9. The concentrate produced according to the traditional acid precipitation process showed mineral contents and solubility profile similar to those of the pH 6 concentrate, but required twice as much water during the process. The effect of electroacidification treatments on ultrafiltration permeate flux was quantified through the measurement of the different hydraulic resistances. Cake resistance was the main resistance to the permeate flux, and it was minimum at pH 9, maximum at pH 7, and intermediate at pH 6.


Assuntos
Proteínas de Soja/isolamento & purificação , Eletroquímica , Concentração de Íons de Hidrogênio , Minerais/análise , Solubilidade , Ultrafiltração
18.
J Dairy Res ; 71(2): 207-15, 2004 May.
Artigo em Inglês | MEDLINE | ID: mdl-15190950

RESUMO

Fourier transform infrared spectroscopy (FTIR) and differential scanning calorimetry (DSC) were used to monitor changes in the secondary structure and thermal stability of beta-lactoglobulin A and B in the presence of sodium dodecyl sulphate (SDS), N-ethylmaleimide (NEM), urea and cysteine. An increase in the thermal stabilities of both proteins was noted in the presence of 10 mM-SDS. In the presence of 50 mM-SDS, there was extensive denaturation of both variants. In general, the beta-strand/beta-sheet regions in the secondary structure of both variants were very susceptible to denaturation by SDS and cysteine, suggesting that these regions may be held by hydrophobic and disulphide bonds. At ambient temperature and physiological pH, a notable difference was observed in the 1636 and 1627 cm(-1) regions of the FTIR spectra of the two beta-lg variants. The results suggest possible differences in the nature of the beta-sheet/beta-strand distribution/ content of the two proteins. Urea and NEM at a concentration of 50 mM, had little effect on the secondary structure and denaturation of both variants. New findings are presented which further indicate that although the beta-lg B variant showed greater thermal stability than the A variant in all the cases studied, its denaturation temperature and secondary structure were affected to a greater extent by the protein perturbants than beta-lg A.


Assuntos
Cisteína/farmacologia , Etilmaleimida/farmacologia , Temperatura Alta , Lactoglobulinas/química , Dodecilsulfato de Sódio/farmacologia , Ureia/farmacologia , Varredura Diferencial de Calorimetria , Estabilidade de Medicamentos , Concentração de Íons de Hidrogênio , Desnaturação Proteica/efeitos dos fármacos , Estrutura Secundária de Proteína , Espectroscopia de Infravermelho com Transformada de Fourier
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