Agronomic characteristics, isoflavone content and Kunitz trypsin inhibitor of vegetable soybean genotypes

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Structure of tick anticoagulant peptide at 1.6 Å resolution complexed with bovine pancreatic trypsin inhibitor

The structure of tick anticoagulant peptide (TAP) has been determined by X-ray crystallography at t.6 Å resolution complexed with bovine pancreatic trypsin inhibitor (BPTI). The TAP-BPTI crystals are tetragonal, a = b = 46.87, c = 50.35 Å, space group P41, four complexes per unit cell. The TAP molecules are highly dipolar and form an intermolecular helical array along the c-axis with a diameter of about 45 Å. Individual TAP units interact in a head-to-tail fashion, the positive end of one molecule associating with the distal negative end of another, and vice versa. The BPTI molecules have a uniformly distributed positively charged surface that interacts extensively through 14 hydrogen bonds and two hydrogen bonded salt bridges with the helical groove around the helical TAP chains. Comparing the structure of TAP in TAP-BPTI with TAP bound to factor Xa(Xa) suggests a massive reorganization in the N-terminal tetrapeptide and the first disulfide loop of TAP (CyS5(T)- Cys 15(T)) upon binding to Xa. The Tyr1(T)OH atom of TAP moves 14.2 Å to interact with Asp189 of the S1 specificity site, Arg3(T)CZ moves 5.0 Å with the guanidinium group forming a cation-π-electron complex in the S4 subsite of Xa, while Lys7(T)NZ differs in position by 10.6 Å in TAP-BPTI and TAP-Xa, all of which indicates a different pre-Xa-bound conformation for the N- terminal of TAP in its native state. In contrast to TAP, the BPTI structure of TAP-BPTI is practically the same as all those of previously determined structures of BPTI, only arginine and lysine side-chain conformations showing significant differences.

Changes in protein fractions, trypsin inhibitor and proteolytic activity in the cotyledons of germinating chickpea

The chickpea seed germination was carried out in 6 days. During the period it was observed a little variation on total nitrogen contents, however the non protein nitrogen was double. A decrease of 19.1 and 20.6% in relation to total nitrogen was observed to the total globulin and albumin fractions, respectively. The gel filtration chromatography on Sepharose CL-6B and SDS-PAGE demonstrated alterations on the distribution patterns of the albumin and total globulin fractions between the initial and the sixth day of germination suggesting the occurrence of protein degradation in the germination process.The assay for acid protease only appeared in the albumin fraction with casein and chickpea total globulin as substrates, whereas the former was more degradated than the latter, however the transformations detected in the protein fractions apppear indicated that others enzymes could be acting during the process. The trypsin inhibitor activity had a little drop after six day of germination indicating a possible increase on the digestibility of the proteins.

Effectiveness inactivation of trypsin inhibitor fron brazilian cultivarof beans (Phaseolus vulgaris L.)

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Effectveness inactivation of trypsin inhibitor from brazilian cultivars of beans (Phaseolus vulgaris L.)

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Heat treatment and inactivation of trypsin-chymotrypsin inhibitors and lectins from beans (Phaseolus vulgaris L.)

This work investigates some factors affecting the inactivation of common bean trypsin inhibitor and phytohemagglutin. Trypsin inhibitor activity was totally stable to heat treatment (30 min, 97C) in the total protein extract, albumin or globulin fraction. Heat treatment of the whole beans easily inactivated the inhibitor. Heat resistance of trypsin inhibitor was intermediate in the bean flour which received the same heat treatment. Independent of sample, the inhibitor was very stable to heat treatment at neutral and acidic pH and labile under strong alkaline conditions. Heating for 30 min in boiling water at pH 12 resulted in complete inactivation of the trypsin inhibitor. Autoclaving (121C) soaked whole beans and flour for 5 min inactivated 55% of the trypsin inhibitor activity in the soaked flour and 75% in the whole beans. After autoclaving 20 min, inactivation of trypsin inhibitor was about 65% in the flour and 80% in the whole beans. The phytohemagglutinin (lectin) activity was totally destroyed in the autoclaved beans after 5 min and in the flour after 15 min.

The Kallikrein Inhibitor from Bauhinia bauhinioides (BbKI) shows antithrombotic properties in venous and arterial thrombosis models

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Avaliação da atividade dos inibidores de tripsina após digestão enzimática em grãos de soja tratados termicamente

Este trabalho avalia a reativação dos inibidores de tripsina, após proteólise in vitro, de grãos de soja tratados termicamente. Para a inativação térmica dos inibidores, os grãos foram embebidos em água destilada (1:5 p/v) durante 12 horas e aquecidos em placas sob refluxo por 30 minutos. A reativação dos inibidores foi avaliada em comparação com a atividade das amostras cruas e aquecidas. A digestibilidade in vitro das proteínas variou de 47% ('OC-13') a 59% (Paraná), apresentando uma melhora, em média, de 32,6% com o aquecimento. A atividade dos inibidores de tripsina para os grãos crus variou de 122 a 206 UTI/mg de amostra, e os valores correlacionaram-se negativamente com a porcentagem de digestibilidade (r = -0,9177). Os inibidores tiveram suas atividades totalmente inativadas com o aquecimento dos grãos, os quais apresentaram porcentagem de recuperação, em média, de 40%. Com o aquecimento, a inativação dos inibidores provavelmente ocorre por complexação com os componentes do grão, o que leva à recuperação da atividade com o processo de digestão enzimática.

Alterações bromatológicas em soja e milho processados por extrusão

Avaliaram-se os efeitos da temperatura do processo de extrusão sobre as características das frações nitrogenadas e dos carboidratos, do extrato etéreo, da digestibilidade in vitro da proteína e do fator antitríptico da soja e do milho. O experimento foi conduzido em delineamento experimental inteiramente casualizado, com três repetições, em esquema fatorial 5 × 4, composto de cinco combinações de soja e milho (100% soja; 75% soja e 25% milho; 50% soja e 50% milho; 25% soja e 75% milho; 100% milho, com base na matéria seca) e quatro temperaturas de extrusão (sem extrusão; e extrusão a 80, 100 ou 120ºC). O processo de extrusão promoveu aumento na fração lipídica e redução nos teores de fibra em detergente neutro (FDN) e fibra em detergente ácido (FDA), que variaram de acordo com a proporção de milho e soja e com a temperatura de processamento, conseqüentemente, os teores de proteína insolúvel em detergente neutro (PIDN) e proteína insolúvel em detergente ácido (PIDA) sofreram redução. A mesma tendência foi observada nos teores de lignina, que foram menores nas misturas com até 50% de soja, processadas a 120ºC. A extrusão, independentemente da temperatura, promoveu aumento da fração A dos carboidratos, tanto no milho como na soja. Nas frações B2 e C diminuíram com a maior participação de soja na mistura. A extrusão reduziu as frações nitrogenadas A, B1 e C, fato observado nas misturas contendo soja. O processamento promoveu aumento da fração B2, exceto no milho a 100%. Alterações menos significativas foram observadas na fração B3. O processamento por extrusão não altera a digestibilidade in vitro da proteína de milho e soja, no entanto, reduz a quantidade de inibidor de tripsina quando as misturas desses grãos são processadas a 120ºC.

Nutritional Responses of Rats to Diets Based on Chickpea (Cicer arietinum L.) Seed Meal or Its Protein Fractions

The aim of this study was to isolate the protein fractions from chickpea, var. IAC-Marrocos, as well as to evaluate its in vivo nutritional protein quality. Among the proteins, albumins showed better nutritional value in the in vivo assays and amino acid contents, despite their higher trypsin inhibitor contents. Trypsin inhibitors were found to be heat labile in all samples, but the digestibility results for unheated and heated flour and albumins suggest that their contents are not very decisive. The PER values for casein (not supplemented) were very similar to those of heated flour and unheated or heated albumin and total globulins. The albumin and glutelin fractions showed the best results for PDCAAS, however, lower than those of casein. Despite the high digestibility of the globulin the very low essential amino acid content lowered its PDCAAS, and it had the lowest values.

Effects of Compounds from Passiflora edulis Sims f. flavicarpa Juice on Blood Coagulation and on Proteolytic Enzymes

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Venom peptide analysis of Vipera ammodytes meridionalis (Viperinae) and Bothrops jararacussu (Crotalinae) demonstrates subfamily-specificity of the peptidome in the family Viperidae

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Fatores antinutricionais e coeficientes de digestibilidade aparente da proteína de produtos de soja para o pacu (Piaractus mesopotamicus)

This study aimed to determine the activities of trypsin inhibitors, hemagglutinant and tannin levels in soybean meal and in raw and processed soy, as well evaluate the protein apparent digestibility coefficient for pacu juveniles. The apparent coefficients of raw, extruded, toasted and milled soy were determined using chromium oxide (0.5%) as marker. A reference diet was created with 26% crude protein and 4,352 kcal kg-1, with each feed containing 30% of the test diet. Feces were collected by abdominal pressure. All analyzed products presented anti-nutritional factors, but the lowest trypsin inhibitor activity was observed in soybean meal. Soy that received thermal treatment presented better digestibility coefficients and lower hemagglutinating activity values than raw soy. No effects of trypsin and tannin inhibitor were observed on the protein digestibility coefficient, but a negative relationship was observed between hemagglutinin levels and protein digestibility coefficient. The use of soybean meal and extruded or toasted soy is recommended for pacu feeding.

Nutritional evaluation of soy yoghurt in comparison to soymilk and commercial milk yoghurt. Effect of fermentation on soy protein

Soymilk was fermented using Lactobacillus delbrueckii ssp. bulgaricus and Streptococcus thermophilus. The soy yoghurt produced was evaluated in comparison to soymilk and commercial milk yoghurt by biological evaluation, rat growth, nitrogen balance assays and microbiological methods. Trypsin inhibitor activity and chemical composition were also determined for all samples. For the soy yoghurt, the growth and nitrogen balance values were not different from the control diet, but the nitrogen balance values were higher than for the soymilk, without significant difference in terms of growth assays. Compared to the commercial yoghurt, Net Protein Ratio and Nitrogen Utilization values were lower, but the Protein Efficiency Ratio, Biological Value and Net Protein Utilization values were equivalent, and for digestibility assays the best results were obtained with the soy yoghurt. The results indicated that soy yoghurt represents a good protein alternative to milk yoghurt and casein. The protein quality of soymilk evidently increased during the fermentation process using Lactobacillus delbrueckii ssp. bulgaricus and Streptococcus thermophilus, including a reduction in trypsin inhibitor levels of about 30%.

Inibidor de tripsina da soja na transferência de imunidade passiva de bezerras da raça holandesa

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)