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1.
Ultrason Sonochem ; 105: 106870, 2024 May.
Artigo em Inglês | MEDLINE | ID: mdl-38579570

RESUMO

The obtained seeds from fruit processing are considered by-products containing proteins that could be utilized as ingredients in food manufacturing. However, in the specific case of soursop seeds, their usage for the preparation of protein isolates is limited. In this investigation a protein isolate from soursop seeds (SSPI) was obtained by alkaline extraction and isoelectric precipitation methods. The SSPI was sonicated at 200, 400 and 600 W during 15 and 30 min and its effect on the physicochemical, functional, biochemical, and structural properties was evaluated. Ultrasound increased (p < 0.05) up to 5 % protein content, 261 % protein solubility, 60.7 % foaming capacity, 30.2 % foaming stability, 86 % emulsifying activity index, 4.1 % emulsifying stability index, 85.4 % in vitro protein digestibility, 423.4 % albumin content, 83 % total sulfhydryl content, 316 % free sulfhydryl content, 236 % α-helix, 46 % ß-sheet, and 43 % ß-turn of SSPI, in comparison with the control treatment without ultrasound. Furthermore, ultrasound decreased (p < 0.05) up to 50 % particle size, 37 % molecular flexibility, 68 % surface hydrophobicity, 41 % intrinsic florescence spectrum, and 60 % random coil content. Scanning electron microscopy analysis revealed smooth structures of the SSPI with molecular weights ranging from 12 kDa to 65 kDa. The increase of albumins content in the SSPI by ultrasound was highly correlated (r = 0.962; p < 0.01) with the protein solubility. Improving the physicochemical, functional, biochemical and structural properties of SSPI by ultrasound could contribute to its utilization as ingredient in food industry.


Assuntos
Annona , Proteínas de Plantas , Sementes , Solubilidade , Sementes/química , Proteínas de Plantas/química , Proteínas de Plantas/isolamento & purificação , Annona/química , Ondas Ultrassônicas , Fenômenos Químicos , Sonicação
2.
Trop Anim Health Prod ; 55(5): 288, 2023 Aug 14.
Artigo em Inglês | MEDLINE | ID: mdl-37578575

RESUMO

During the dry and rainy seasons of the Northeastern Zone of Peru, a chemical characterization of five species of bamboo prevalent in the area (Guadua lynnclarkiae, G. takahashiae, Bambusa vulgaris, G. weberbaueri, and Dendrocalamus asper) was conducted. Then, the effect of supplementing bamboo leaves (0, 20, and 40% inclusion of D. asper) on the intake and live weight gain of 18 Gyr × Holstein heifers was evaluated for 28 days. Among the species evaluated, D. asper has the greatest crude protein (CP) concentration (158-166 g/kg Dry matter- DM), post-ruminal CP supply (127 g/kg DM), and in vitro organic matter digestibility (444-456 g/kg DM) but similar concentrations of crude ash (124 g/kg DM), calcium (2.4-2.8 mg/g), phosphorus (0.7-2.1 mg/g), protein fractions A, B1, B2, B3, C (45, 5, 35, 56, and 17g/kg DM, respectively), rumen-undegraded CP (31% CP), neutral detergent fiber (NDF, 685g/kg DM), and acid detergent fiber (ADF, 357 g/kg DM) than the other species evaluated. Dry matter intake was higher in the control treatment and in the 20% bamboo leaf inclusion treatment than in the 40% bamboo inclusion treatment. Intake of CP and NDF decreased with the increase in bamboo inclusion. Despite the differences in DM, CP, and NDF intake, the live weight gain remained similar across treatments. However, there was a greater feed conversion in the 20% bamboo leaf inclusion treatment. During the dry season, bamboo leaves can be used as an alternative supplement at a maximum inclusion of 20% without affecting the live weight gain.


Assuntos
Fibras na Dieta , Digestão , Bovinos , Animais , Feminino , Peru , Fibras na Dieta/metabolismo , Ração Animal/análise , Detergentes/metabolismo , Aumento de Peso , Dieta/veterinária , Rúmen/metabolismo , Fermentação
3.
Front Vet Sci ; 10: 1043656, 2023.
Artigo em Inglês | MEDLINE | ID: mdl-36816195

RESUMO

Introduction: Horses submitted to carbohydrate overload can develop laminitis due to changes in cecal pH and microbiota, followed by an increase in transmural absorption of luminal content, including bacterial toxins. In response to acute injury there is hepatic overproduction of several proteins known as acute phase proteins (APP). Few studies have evaluated protein fractionation to characterize the inflammatory response in acute laminitis. The aim of this study was to test the viability of an experimental model to induce acute laminitis, using a single carbohydrate overload, and the influence of a buffering solution on the development of the disease; also, study the kinetics of APP during acute laminitis, as well as the correlation between these proteins and clinical signs associated to this syndrome. Methods: Ten healthy horses were divided in a factorial and randomized way into four groups (n = 5): control group (CG), starch group (SG), buffer group (BG), and starch C buffer group (SBG). They were evaluated at seven times (T0h, T4h, T8h, T12h, T24h, T48h, and T72h), which included clinical evaluation and blood sample collection. Total serum protein and albumin concentrations were determined by colorimetry and the other APP by polyacrylamide gel electrophoresis containing sodium dodecyl sulfate and commercial ELISA kits. Data were analyzed by two-way ANOVA, followed by Tukey's test (p < 0.05). The correlation between clinical signs and APP were verified using the Pearson's correlation coefficient. Results and discussion: 40% of the animals from SG and 60% from SBG developed clinical laminitis. A single administration of buffer solution was not able to prevent clinical signs of laminitis. There was no difference between groups on total serum protein, albumin, serum amyloid A and C-reactive protein concentrations (p > 0.05). Transferrin, considered a negative APP, showed a positive response pattern in SG and SBG. Ceruloplasmin had a positive correlation with Obel grade, heart rate on animals from SGB and number of steps on horses submitted to starch overload (SG and SBG). Ceruloplasmin, α-1-antitrypsin and haptoglobin concentrations increased in SBG, suggesting an inflammatory response in animals of this group. Changes in clinical parameters were also more evident in the SBG, corroborating the protein fractionation findings.

4.
J Sep Sci ; 45(10): 1784-1796, 2022 May.
Artigo em Inglês | MEDLINE | ID: mdl-35306742

RESUMO

Sample preparation and protein fractionation are important issues for proteomic studies. Protein extraction procedures strongly affect the performance of fractionation methods by provoking protein dispersion in several fractions. The most notable exception is the gel-based electrophoretic protein fractionation due to its resolution and effectiveness of sodium dodecyl sulfate as a solubilizing agent, while its main limitation lies in the poor recovery of the gel-trapped proteins. We created a fractionator device to separate complex mixture of proteins and peptides that is based on the continuous gel electrophoresis/electroelution sorting of these molecules. In an unsupervised process, complex mixtures of proteins or peptides are fractionated into the gel while separated fractions are simultaneously and sequentially electroeluted to the solution containing wells. The performance of the device was studied for protein fractionation in terms of reproducibility, protein recovery, and loading capacity. In a setup free of sodium dodecyl sulfate, complex peptide mixtures can also be fractionated. More than 11,700 proteins were identified in the whole-cell lysate of the CaSki cell line by using the fractionator combined with the filter-aided sample preparation method and mass spectrometry analysis. Fractionator-based proteome characterization increased 1.7-fold the number of identified proteins compared to the unfractionated sample analysis.


Assuntos
Peptídeos , Proteômica , Eletroforese em Gel de Poliacrilamida , Peptídeos/química , Proteoma/análise , Proteômica/métodos , Reprodutibilidade dos Testes , Dodecilsulfato de Sódio/química
5.
Int J Mol Sci ; 22(6)2021 Mar 16.
Artigo em Inglês | MEDLINE | ID: mdl-33809562

RESUMO

Adzuki seed ß-vignin, a vicilin-like globulin, has proven to exert various health-promoting biological activities, notably in cardiovascular health. A simple scalable enrichment procedure of this protein for further nutritional and functional studies is crucial. In this study, a simplified chromatography-independent protein fractionation procedure has been optimized and described. The electrophoretic analysis showed a high degree of homogeneity of ß-vignin isolate. Furthermore, the molecular features of the purified protein were investigated. The adzuki bean ß-vignin was found to have a native size of 146 kDa, and the molecular weight determined was consistent with a trimeric structure. These were identified in two main polypeptide chains (masses of 56-54 kDa) that are glycosylated polypeptides with metal binding capacity, and one minor polypeptide chain with a mass 37 kDa, wherein these features are absent. The in vitro analysis showed a high degree of digestibility of the protein (92%) and potential anti-inflammatory capacity. The results lay the basis not only for further investigation of the health-promoting properties of the adzuki bean ß-vignin protein, but also for a possible application as nutraceutical molecule.


Assuntos
Cromatografia/métodos , Proteínas de Plantas/genética , Vigna/química , Sequência de Aminoácidos , Células CACO-2 , Fracionamento Químico , Farinha , Globulinas/química , Humanos , Concentração de Íons de Hidrogênio , Inflamação/patologia , Proteínas de Plantas/química , Proteínas de Plantas/isolamento & purificação , Sementes/química , Solubilidade
6.
R. bras. Ci. avíc. ; 21(3): eRBCA-2018-0941, 2019. tab, ilus, graf
Artigo em Inglês | VETINDEX | ID: vti-25832

RESUMO

The objective of this study was to compare characteristics and properties of breast meat from spent Lohmann Brown layers (SP, 90 weeks old, n = 24) and those of commercial broilers (BR, 6 weeks old, n = 24). The breasts of both SP and BR were collected from a local processing plant, vacuum-packed in a plastic bag, and stored at -18ºC until further analyses. The SP showed a greater water-holding capacity, tougher and chewier texture (p 0.05). Both raw and cooked SP breasts comprised the greater total collagen but lower soluble collagen than those of BR (p 0.05). Muscle fibers of the SP, observed under scanning electron microscope, were small, with average fiber diameter of 37.85±1.40 m, densely packed and surrounded by complex networks of connective tissue. The lower myofibril fragmentation index and alkaline-soluble protein fractions of the SP (p 0.05) suggested lesser degree of postmortem fragmentation and protein denaturation in SP compared to BR. Based on differential scanning calorimetry, multiple endothermic transitions were observed in both raw BR and SP breast samples. While BR thermograms comprise five transitions at 57.7ºC, 64.2ºC, 67.6ºC, 72.3ºC and 77.6ºC with total H of 15.31 J/g dry meat, the SP samples exhibited four transitions at 55.1ºC, 62.1ºC, 70.5ºC and 77.7ºC and total H of 17.62 J/g dry meat. Overall, the findings indicated that cooked meat toughness of SP was attributed by the high total and heat-stable collagen content, densely packing of small muscle fibers, and the superior myofibril integrity.(AU)


Assuntos
Animais , Galinhas/anatomia & histologia , Galinhas/crescimento & desenvolvimento , Carne/classificação
7.
Rev. bras. ciênc. avic ; 21(3): eRBCA, 2019. tab, ilus, graf
Artigo em Inglês | VETINDEX | ID: biblio-1490668

RESUMO

The objective of this study was to compare characteristics and properties of breast meat from spent Lohmann Brown layers (SP, 90 weeks old, n = 24) and those of commercial broilers (BR, 6 weeks old, n = 24). The breasts of both SP and BR were collected from a local processing plant, vacuum-packed in a plastic bag, and stored at -18ºC until further analyses. The SP showed a greater water-holding capacity, tougher and chewier texture (p 0.05). Both raw and cooked SP breasts comprised the greater total collagen but lower soluble collagen than those of BR (p 0.05). Muscle fibers of the SP, observed under scanning electron microscope, were small, with average fiber diameter of 37.85±1.40 m, densely packed and surrounded by complex networks of connective tissue. The lower myofibril fragmentation index and alkaline-soluble protein fractions of the SP (p 0.05) suggested lesser degree of postmortem fragmentation and protein denaturation in SP compared to BR. Based on differential scanning calorimetry, multiple endothermic transitions were observed in both raw BR and SP breast samples. While BR thermograms comprise five transitions at 57.7ºC, 64.2ºC, 67.6ºC, 72.3ºC and 77.6ºC with total H of 15.31 J/g dry meat, the SP samples exhibited four transitions at 55.1ºC, 62.1ºC, 70.5ºC and 77.7ºC and total H of 17.62 J/g dry meat. Overall, the findings indicated that cooked meat toughness of SP was attributed by the high total and heat-stable collagen content, densely packing of small muscle fibers, and the superior myofibril integrity.


Assuntos
Animais , Carne/classificação , Galinhas/anatomia & histologia , Galinhas/crescimento & desenvolvimento
8.
Methods Mol Biol ; 1416: 509-19, 2016.
Artigo em Inglês | MEDLINE | ID: mdl-27236693

RESUMO

Mesenchymal stem or stromal cells (MSCs) are of great interest in biomedical sciences and disease treatment because of their multipotency and wide range of applications for tissue repair and suppression of the immune system. Proteomic analysis of these unique cells has contributed to the identification of important pathways utilized by MSCs to differentiate into distinct tissues as well as important proteins responsible for their special function in vivo and in vitro. However, comparison of proteomic studies in MSCs still suffers from the heterogeneity of MSC preparations. In addition, as proteomics technology advances, several studies can be revisited in order to increase the depth of analysis and, therefore, elucidate more refined mechanisms involved in MSC functionalities. Here, we present detailed protocols to obtain MSCs, as well as protocols to perform in-depth profiling and quantification of alterations in MSC proteomes.


Assuntos
Células-Tronco Mesenquimais/metabolismo , Proteômica/métodos , Veias Umbilicais/citologia , Diferenciação Celular , Proliferação de Células , Feminino , Humanos , Imunofenotipagem , Células-Tronco Mesenquimais/citologia , Gravidez
9.
R. bras. Saúde Prod. Anim. ; 13(3): 604-618, July-Sept. 2012. tab
Artigo em Português | VETINDEX | ID: vti-26995

RESUMO

Objetivou-se com este trabalho avaliar o potencial forrageiro e o valor nutricional do feno de diferentes frações da parte aérea de quatro variedades de mandioca. Utilizou-se um delineamento em blocos casualizados, esquema fatorial 4 x 3, com quatro repetições, composto de quatro variedades de mandioca (Amarelinha, Olho Roxo, Periquita e Sabará) e três formas de aproveitamento da parte aérea (Planta Inteira, Terço Superior e Sobras de Plantio). A variedade Periquita, quando considerada a fração planta inteira, apresentou maior potencial produtivo de feno e forragem. Os maiores valores de relação folha/haste foram encontrados na fração do terço superior. A variedade Amarelinha apresentou menor teor de lignina e fração C dos carboidratos e, juntamente, com a variedade Olho Roxo teve maior valor de nutrientes digestíveis totais. A fração do terço superior apresentou maior teor de proteína bruta e menores teores fibra e lignina, o que foi confirmado pelo fracionamento dos carboidratos. Quanto ao fracionamento proteico, não houve diferença entre as variedades de mandioca, todavia, a fração planta inteira teve menor valor na fração C. Para as frações proteicas B1 e B2 houve efeito de interação das variedades com as frações da parte aérea. A parte aérea das variedades de mandioca avaliadas nas diferentes frações apresenta bom potencial produtivo e os fenos produzidos da parte aérea e do terço superior das variedades Amarelinha e Olho Roxo apresentam melhor valor nutricional.(AU)


The objective to this was work evaluate the forage potential and nutritional value the hay, of different fractions of the aerial parts of four cassava varieties. We used a randomized complete block design, factorial design 4 x 3 with four replications being four varieties of cassava (Amarelinha, Olho Roxo, Periquita and Sabará) and three forms of exploitation of cassava foliage (Entire Plant, Superior Third, Surpluses of Planting). Variety Periquita used when the whole plant fraction showed better results on the productive potential of hay and forage. The highest values of leaf / foliage were found in the fraction of the upper third. The variety Amarelinha had lower lignin content and carbohydrate fraction C and together with the variety Olho Roxo had a higher value of TDN. The fraction of the upper third had the highest crude protein content and lower fiber and lignin, which was confirmed by fractionation of carbohydrates. As to the division protein did not differ between the cassava varieties, however, the fraction of the whole plant was lowest in fraction C. For protein fractions B1 and B2 was no interaction effect of varieties with the fractions of the shoot. We can conclude that the varieties of this study in the different fractions of the aerial have good productive potential and who also the hay produced the shoot and Olho Roxo Amarelinha varieties have better nutritional value, as well as the upper third of the hay.(AU)


Assuntos
Manihot , Valor Nutritivo
10.
Rev. bras. saúde prod. anim ; 13(3): 604-618, July-Sept. 2012. tab
Artigo em Português | VETINDEX | ID: biblio-1493165

RESUMO

Objetivou-se com este trabalho avaliar o potencial forrageiro e o valor nutricional do feno de diferentes frações da parte aérea de quatro variedades de mandioca. Utilizou-se um delineamento em blocos casualizados, esquema fatorial 4 x 3, com quatro repetições, composto de quatro variedades de mandioca (Amarelinha, Olho Roxo, Periquita e Sabará) e três formas de aproveitamento da parte aérea (Planta Inteira, Terço Superior e Sobras de Plantio). A variedade Periquita, quando considerada a fração planta inteira, apresentou maior potencial produtivo de feno e forragem. Os maiores valores de relação folha/haste foram encontrados na fração do terço superior. A variedade Amarelinha apresentou menor teor de lignina e fração C dos carboidratos e, juntamente, com a variedade Olho Roxo teve maior valor de nutrientes digestíveis totais. A fração do terço superior apresentou maior teor de proteína bruta e menores teores fibra e lignina, o que foi confirmado pelo fracionamento dos carboidratos. Quanto ao fracionamento proteico, não houve diferença entre as variedades de mandioca, todavia, a fração planta inteira teve menor valor na fração C. Para as frações proteicas B1 e B2 houve efeito de interação das variedades com as frações da parte aérea. A parte aérea das variedades de mandioca avaliadas nas diferentes frações apresenta bom potencial produtivo e os fenos produzidos da parte aérea e do terço superior das variedades Amarelinha e Olho Roxo apresentam melhor valor nutricional.


The objective to this was work evaluate the forage potential and nutritional value the hay, of different fractions of the aerial parts of four cassava varieties. We used a randomized complete block design, factorial design 4 x 3 with four replications being four varieties of cassava (Amarelinha, Olho Roxo, Periquita and Sabará) and three forms of exploitation of cassava foliage (Entire Plant, Superior Third, Surpluses of Planting). Variety Periquita used when the whole plant fraction showed better results on the productive potential of hay and forage. The highest values of leaf / foliage were found in the fraction of the upper third. The variety Amarelinha had lower lignin content and carbohydrate fraction C and together with the variety Olho Roxo had a higher value of TDN. The fraction of the upper third had the highest crude protein content and lower fiber and lignin, which was confirmed by fractionation of carbohydrates. As to the division protein did not differ between the cassava varieties, however, the fraction of the whole plant was lowest in fraction C. For protein fractions B1 and B2 was no interaction effect of varieties with the fractions of the shoot. We can conclude that the varieties of this study in the different fractions of the aerial have good productive potential and who also the hay produced the shoot and Olho Roxo Amarelinha varieties have better nutritional value, as well as the upper third of the hay.


Assuntos
Manihot , Valor Nutritivo
11.
Rev. Inst. Nac. Hig ; 41(1): 38-42, jun. 2010. graf, tab
Artigo em Espanhol | LILACS, LIVECS | ID: lil-631772

RESUMO

La harina de nuez de Barinas (Caryodendron orinocense K.) de acuerdo a estudios realizados presenta un contenido de pro teínas en el rango de 15-18%, que permite se pueda considerar como fuente de proteína. Sin embargo no se conoce la composición de estas proteínas. En este estudio se realizó un proceso de fraccionamiento de acuerdo a la solubilidad en diferentes solventes (agua, cloruro de sodio al 5%, hidróxido de sodio 0,02N, etanol al 70%), y el establecimiento de la composición proteica según el peso molecular de la harina de nuez de Barinas obtenida a partir de las nueces secas, molidas y des grasadas, determinando el rango de pesos moleculares por SDS-PAGE y su comparación con el rango de pesos moleculares de las proteínas de la harina de soya (Glycine max). Asi mismo, se determinó la digestibilidad in vitro por hidrólisis enzimática. Los resultados indican un rango de PM de 20.000- 97.000 daltons para la soya y de 6.500-45.000 daltons para la nuez de Barinas. El peso molecular más bajo sugiere una más fácil digestión de las proteínas, que corrobora el valor de la di - ges tibilidad obtenido de 75%. Las proteínas presentes están cons tituidas por albúminas 50,72%, globulinas 15,56%, prolaminas 23,10% y glutelinas 2,52% que representan el 92,15% del total de proteínas presentes. Estas fracciones presentaron una pureza de 81,57%, 94,01%, 70,86% y 92,53%, respectivamente. Estos resultados sugieren la posibilidad de uso de la harina de Caryodendron orinocense K en el desarrollo de productos alimenticios para niños y ancianos.


Nuez de Barinas (Caryodendron orinocense K.) flour has been reported to have a content of proteins in the range of 15-18% that allows considering it as a source of proteins. However, there is no evidence on the composition of these proteins. The objective of this study was the extraction and separation of the different fractions of proteins based on their solubility in different solvents (water, 5% sodium chloride, sodium hydroxide 0.02N, and 70% ethanol), and the protein composition assessment of the nuez de Barinas flour from dried, milled, and defatted nuts; by analysis of the range of mo lecular weight by SDS-PAGE. Molecular weights of proteins from soybean (Glycine max) flour, were used for comparison. In vitro protein digestibility was determined by enzymatic hydrolysis. Results presented soy proteins in the range of 20.000-97.000 daltons while the nuez de Barinas flour proteins were in the range of 6.500-45.000 daltons. Low molecular weight proteins should suggest a much easier digestibility of these proteins, which is related to the digestibility index of 75% found. Protein composition was found to be 50,72% albumins, 15,56% globulins, 23,10% prolamins, and 2,52% glutelins which represent 92,15% of total proteins present. These fractions showed a percent purity of 81.57, 94.01, 70.86 and 92.53, respectively. These results suggest the possibility to use this flour Caryodendron orinocense K. in developing food products for children and elderly persons.


Assuntos
Humanos , Masculino , Feminino , Pré-Escolar , Criança , Idoso , Idoso de 80 Anos ou mais , Plantas/classificação , Proteínas/uso terapêutico , Albuminas , Prolaminas , Saúde Pública , Globulinas , Nozes/classificação
12.
Rev. Inst. Med. Trop. Säo Paulo ; Rev. Inst. Med. Trop. Säo Paulo;49(6): 385-388, Nov.-Dec. 2007. ilus
Artigo em Inglês | LILACS | ID: lil-470522

RESUMO

This report describes a preliminary characterization of proteolytic activity of proteins isolated from lysate of Giardia trophozoites of an axenic Brazilian strain. Fractions obtained by high-performance liquid chromatography (FPLC) were tested in SDS-polyacrylamide gel for the protein profiles, and the proteases activity was analyzed using gelatin impregnated SDS-PAGE. The proteases characterization was based on inhibition assays employing synthetic inhibitors for cysteine (E-64, IAA), serine (PMSF, TPCK, TLCK, and elastatinal), metalo (EDTA) and aspartic (pepstatin) proteases. Among thirty eluted fractions, polypeptide bands were observed in eight of them, however, proteolytic activity was detected in four ones (F23, F24, F25 and F26). Protein profiles of these fractions showed a banding pattern composed by few bands distributed in the migration region of 45 to < 18 kDa. The zymograms revealed proteolytic activity in all the four fractions assayed, mainly distributed in the migration region of 62 to 35 kDa. Among the profiles, the main pronounced zones of proteolysis were distinguished at 62, 55, 53, 50, 46 and 40 kDa. In inhibition assays, the protease activities were significantly inhibited by cysteine (E-64) and serine proteases (TPCK, TLCK and elastatinal) inhibitors. Gels incubated with other cysteine and serine protease inhibitors, IAA and PMSF, respectively, showed a decrease in the intensity of hydrolysis zones. Indeed, in the assays with the inhibitors EDTA for metalloproteases and pepstatin for aspartic proteases, none inhibition was detected against the substrate. These observations are relevants, especially if we consider that to define the real role of the proteases in host-parasite interaction, the purification of these enzymes for detailed studies may be warranted.


O presente estudo consiste em uma caracterização preliminar da atividade proteolítica de frações de proteínas purificadas a partir de lisados de trofozoítos de cepa isolada e axenizada no Brasil. Frações obtidas por cromatografia líquida (FPLC) foram analisadas quanto ao perfil eletroforético em géis de poliacrilamida (SDS-PAGE) e a atividade proteolítica foi avaliada em géis contendo gelatina como substrato. A caracterização das enzimas foi realizada a partir da análise do efeito de inibidores sintéticos de cisteína-proteases (E-64, IAA), serina-proteases (PMSF), serina e cisteína-proteases (TPCK, TLCK, elastatinal), metalo-proteases (EDTA) e aspartil proteases (pepstatina) sobre a degradação do substrato. Entre 30 frações eluídas, bandas de proteínas foram observadas em oito delas, entretanto, atividade proteolítica foi detectada apenas nas frações 23, 24, 25 e 26. O perfil eletroforético das proteínas revelou poucas bandas distribuídas na faixa de 45 a 18 kDa. Os zimogramas revelaram zonas de proteólise na faixa de aproximadamente 62 a 35 kDa, entretanto destacaram-se as bandas de hidrólise de 62, 55, 53, 50, 46 e 40 kDa. Nos ensaios de inibição, a proteólise foi marcantemente inibida por E-64, TPCK, TLCK e elastatinal. Redução discreta da proteólise foi observada com IAA e PMSF, enquanto que EDTA e pepstatina não promoveram alteração dos perfis de hidrólise. Estas observações são relevantes, especialmente se considerarmos que para elucidar o envolvimento das proteases na relação parasita-hospedeiro, a purificação dessas moléculas é um requisito importante.


Assuntos
Animais , Humanos , Giardia/enzimologia , Peptídeo Hidrolases/metabolismo , Proteínas de Protozoários/metabolismo , Cromatografia Líquida , Eletroforese em Gel de Poliacrilamida , Peptídeo Hidrolases/isolamento & purificação , Proteínas de Protozoários/isolamento & purificação
13.
Sci. agric. ; 61(6)2004.
Artigo em Inglês | VETINDEX | ID: vti-439925

RESUMO

Even though hulless barley is widely known due to its nutritional potential, in Brazil it is only grown at a few agricultural experimental stations. There is no published data about the chemical composition of Brazilian hulless barley varieties; however, research laboratories have studied their agronomical characteristics. The objectives of this study were to present the chemical characterization and effect of flour fractionation on protein concentration of six Brazilian hulless barley varieties, namely IAC IBON 214/82, IAC 8612/421, IAC 8501/31, IAC 8501/12, IAPAR 39-Acumaí, and IAC 8501/22. The analyses included: ash, ether extract, total protein, starch, total insoluble and soluble dietary fiber, and beta-glucans. Flour fractionation was carried out by sieving. The flour fractions were evaluated for crude protein, protein, and protein and non-protein nitrogen. Chemical composition varied (P 0.05) among all the varieties. IAC 8501/22, IAC 8501/31, and IAC 8501/12 showed the highest protein content (15.69, 15.25, and 14.94% respectively). Differences (P 0.05) among the protein of the fractionated flours were detected, and might be attributed primarily to genetic background since all varieties were grown under the same environmental conditions. Fractionating the flour increased the total protein content, in some fractions, by up to 2%. These results may be useful in the food industry for the selection of hulless barley varieties for human consumption and to produce substantially protein-enriched flour fractions.


Apesar de a cevada nua ser amplamente conhecida por seu potencial nutricional, no Brasil é apenas cultivada em poucas estações experimentais agronômicas. Em relação as variedades brasileiras de cevada nua, não se têm dados sobre a composição química, entretanto instituições de pesquisa têm estudado suas características agronômicas. Os objetivos deste estudo foram apresentar a caracterização química e o efeito no fracionamento da farinha obtida visando à concentração de proteína de seis variedades brasileiras de cevada nua: IAC IBON 214/82, IAC 8612/421, IAC 8501/31, IAC 8501/12, IAPAR 39-Acumaí, e IAC 8501/22. Foram realizadas análises de: cinzas, extrato etéreo, proteína total, amido, fibra alimentar total, solúvel e insolúvel e beta-glucanas. As frações das farinhas foram obtidas por peneiramento e avaliadas quanto aos teores de proteína bruta, proteína, nitrogênio protéico e não protéico. Houve variação entre as variedades testadas (P 0,05). As variedades IAC 8501/22, IAC 8501/31 e IAC 8501/12 apresentaram o maior teor de proteína (15,69; 15,25 e 14,94% respectivamente). Foi observada diferença (P 0,05) quanto ao teor de proteína nas frações de farinha de cada variedade, a qual pode ser atribuída principalmente às características genéticas, uma vez que todas as variedades foram cultivadas sob as mesmas condições ambientais. Após o fracionamento, foi observada concentração, em algumas frações, de no máximo 2% em relação a farinha integral. As variedades brasileiras de cevada nua apresentam potencial para consumo humano bem como para a produção de farinhas enriquecidas com alta proteína.

14.
Sci. agric ; 61(6)2004.
Artigo em Inglês | LILACS-Express | VETINDEX | ID: biblio-1496489

RESUMO

Even though hulless barley is widely known due to its nutritional potential, in Brazil it is only grown at a few agricultural experimental stations. There is no published data about the chemical composition of Brazilian hulless barley varieties; however, research laboratories have studied their agronomical characteristics. The objectives of this study were to present the chemical characterization and effect of flour fractionation on protein concentration of six Brazilian hulless barley varieties, namely IAC IBON 214/82, IAC 8612/421, IAC 8501/31, IAC 8501/12, IAPAR 39-Acumaí, and IAC 8501/22. The analyses included: ash, ether extract, total protein, starch, total insoluble and soluble dietary fiber, and beta-glucans. Flour fractionation was carried out by sieving. The flour fractions were evaluated for crude protein, protein, and protein and non-protein nitrogen. Chemical composition varied (P 0.05) among all the varieties. IAC 8501/22, IAC 8501/31, and IAC 8501/12 showed the highest protein content (15.69, 15.25, and 14.94% respectively). Differences (P 0.05) among the protein of the fractionated flours were detected, and might be attributed primarily to genetic background since all varieties were grown under the same environmental conditions. Fractionating the flour increased the total protein content, in some fractions, by up to 2%. These results may be useful in the food industry for the selection of hulless barley varieties for human consumption and to produce substantially protein-enriched flour fractions.


Apesar de a cevada nua ser amplamente conhecida por seu potencial nutricional, no Brasil é apenas cultivada em poucas estações experimentais agronômicas. Em relação as variedades brasileiras de cevada nua, não se têm dados sobre a composição química, entretanto instituições de pesquisa têm estudado suas características agronômicas. Os objetivos deste estudo foram apresentar a caracterização química e o efeito no fracionamento da farinha obtida visando à concentração de proteína de seis variedades brasileiras de cevada nua: IAC IBON 214/82, IAC 8612/421, IAC 8501/31, IAC 8501/12, IAPAR 39-Acumaí, e IAC 8501/22. Foram realizadas análises de: cinzas, extrato etéreo, proteína total, amido, fibra alimentar total, solúvel e insolúvel e beta-glucanas. As frações das farinhas foram obtidas por peneiramento e avaliadas quanto aos teores de proteína bruta, proteína, nitrogênio protéico e não protéico. Houve variação entre as variedades testadas (P 0,05). As variedades IAC 8501/22, IAC 8501/31 e IAC 8501/12 apresentaram o maior teor de proteína (15,69; 15,25 e 14,94% respectivamente). Foi observada diferença (P 0,05) quanto ao teor de proteína nas frações de farinha de cada variedade, a qual pode ser atribuída principalmente às características genéticas, uma vez que todas as variedades foram cultivadas sob as mesmas condições ambientais. Após o fracionamento, foi observada concentração, em algumas frações, de no máximo 2% em relação a farinha integral. As variedades brasileiras de cevada nua apresentam potencial para consumo humano bem como para a produção de farinhas enriquecidas com alta proteína.

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