Prediction of crude protein digestibility of animal by-product meals for dogs by the protein solubility in pepsin method

Animal by-product meals have large variability in crude protein (CP) content and digestibility. In vivo digestibility procedures are precise but laborious, and in vitro methods could be an alternative to evaluate and classify these ingredients. The present study reports prediction equations to estimate the CP digestibility of meat and bone meal (MBM) and poultry by-product meal (PM) using the protein solubility in pepsin method (PSP). Total tract CP digestibility of eight MBM and eight PM samples was determined in dogs by the substitution method. A basal diet was formulated for dog maintenance, and sixteen diets were produced by mixing 70 % of the basal diet and 30 % of each tested meal. Six dogs per diet were used to determine ingredient digestibility. In addition, PSP of the MBM and PM samples was determined using three pepsin concentrations: 0·02, 0·002 and 0·0002 %. The CP content of MBM and PM ranged from 39 to 46 % and 57 to 69 %, respectively, and their mean CP digestibility by dogs was 76 (2·4) and 85 (2·6) %, respectively. The pepsin concentration with higher Pearson correlation coefficients with the in vivo results were 0·0002 % for MBM (r 0·380; P = 0·008) and 0·02 % for PM (r 0·482; P = 0·005). The relationship between the in vivo and in vitro results was better explained by the following equations: CP digestibility of MBM = 61·7 + 0·2644 × PSP at 0·0002 % (P = 0·008; R (2) 0·126); and CP digestibility of PM = 54·1 + 0·3833 × PSP at 0·02 % (P = 0·005; R (2) 0·216). Although significant, the coefficients of determination were low, indicating that the models were weak and need to be used with caution.

Study of the proteins in the defatted flour and protein concentrate of baru nuts (Dipteryx alata Vog)

O baru (Dipteryx alata Vog.) é uma leguminosa abundante no Cerrado brasileiro, cuja castanha pode ser explorada através do uso sustentável para o aproveitamento das frações proteicas e lipídicas. Este trabalho teve como objetivo estudar as proteínas desta castanha, presentes na farinha desengordurada e no concentrado proteico, quanto as suas propriedades funcionais, ao perfil das frações proteicas e à digestibilidade in vitro. A farinha desengordurada com hexano foi submetida à extração no pH de maior solubilidade das proteínas, obtendo-se o concentrado proteico. O perfil eletroforético das frações proteicas foi avaliado em gel de SDS-PAGE. As propriedades funcionais indicaram a possibilidade de emprego em diversos alimentos, assim como a soja, conferindo capacidade de absorção de água, capacidade de absorção de óleo, propriedades emulsificantes e espumabilidade. As globulinas, seguidas das albuminas, são as frações majoritárias da farinha e do concentrado proteico, respectivamente. A digestibilidade foi superior no concentrado em relação à farinha desengordurada.

Porcentagens de saponinas e taninos em vinte e oito cultivares de alfafa (Medicago sativa L.) em duas épocas de corte - Botucatu - SP

O objetivo do estudo foi determinar os conteúdos de saponinas, taninos e a solubilidade da proteína (SP) de 28 cultivares de alfafa: Crioula, Monarca, BR 4, Alto Great, MH 4, SW 9210 A, 5929, BR 1, EL Grande, 5715, MH 15, Valley Plus, BR 2, Rio, SW 8210, Maricopa, ICI 990, 5888, P 30, Alfa-200, WL 516, SW 8112 A, BR 3, Florida 77, Araucana, Falcon, Semit 921 e Sutter. O material analisado foi obtido do 10º e 14º corte, respectivamente; em 08/12/97 e 16/04/98, de um experimento desenvolvido na Faculdade de Medicina Veterinária e Zootecnia, UNESP, Botucatu. Amostras de cada cultivar foram colhidas, pesadas e secas em estufa a 52ºC. As saponinas foram extraídas com solvente hidrofílico e lipofílico e o conteúdo foi calculado pela equação y=0,8121x-1,4759, R² = 1,00. A extração dos taninos totais e condensados foi efetuada por meio de ultra-som (12 min), sendo os taninos totais determinados pela equação: y=44,978 + 0,5644 com R²=0,9977 e os condensados, multiplicando-se a absorbância por 78,26 dividido pelo teor de matéria seca. A SP foi determinada pelo método de KOH, de acordo com a seguinte fórmula: SP (%) = proteína solúvel x 100/proteína bruta da amostra. Os teores de saponinas, taninos totais e condensados e a solubilidade da proteína não diferiram (P>0,05) entre as cultivares. Houve efeito (P<0,05) da época de corte apenas sobre o teor de taninos totais. Os teores médios de saponinas de 1,00% aliados à baixa solubilidade média da proteína bruta (34,11%) não se constituem em fatores limitantes para uso dos cultivares de alfafa estudadas.

Physicochemical characterization of collagen fibers and collagen powder for self-composite film production

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

Estudo do valor nutritivo do farelo de guandu [Cajanus cajan (L.) Miilps] var. fava larga na alimentação de frangos de corte. 1. Avaliação do tratamento térmico

The experiment was conducted to evaluate pigeon pea (Cajanus cajan) protein in broiler chicks (up to 28 days of age) feeding, as compared to soybean (Glycine mar) protein, In the experiment the effects of temperature and autoclaving on antinutritional factors on pigeon pea meal were studied. Temperatures of 100, 110 e 120 degrees C and times of autoclaving of 10, 20 and 30 minutes were applied using a two-way factorial design, replicated in four times. Underheating and overheating during the process of inactivation of proteases inhibiting were evaluated by ureatic activity and protein solubility analysis, after the grains were dried and ground. After 28 days, the best time of autoclaving was 20 minutes (p<,05) irrespectively of temperature, which lead to a lower feed consuption. There were no histopathological alterations in kidney, liver, pancreas, heart and intestines of the broilers.

Isolamento, fracionamento e caracterização parcial das proteínas de amêndoa de Baru (Dipteryx alata Vog.)

Pós-graduação em Alimentos e Nutrição - FCFAR

Valor nutricional e parâmetros de qualidade de subprodutos de origem animal para cães

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Isolation, solubility and in vitro hydrolysis of chickpea vicilin-like protein

The chickpea vicilin-like globulin was isolated and chromatographed on Sepharose CL-6B and Sephacryl S-300. The native globulin with a molecular weight of 140 kDa was resolved in Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in seven polypeptide bands in the range of 12.4-67 kDa. The solubility profile of the protein in water and NaCl solutions was typical of a legume globulin. The purified vicilin-like globulin, native and heated, was hydrolyzed by pepsin, trypsin and chymotrypsin. The hydrolysis patterns indicated that the native vicilin-like protein was only partially degraded by the enzymes in comparison with casein. Heating increased its susceptibility to hydrolysis relative to the native form, for all the enzymes. However, the results obtained by the pH-drop method revealed that the in vitro digestibility of the vicilin-like protein was not altered by heating, while 11 S-like and total globulins suffered a small increase, indicating that the structural characteristics of storage globulins may be important factors limiting the protein digestion. (c) 2007 Swiss Society of Food Science and Technology. Published by Elsevier Ltd. All rights reserved.

Thermal study and physico-chemical characterization of some functional properties of guava seeds protein isolate (Psidium guajava)

The guava seed protein isolate ( PI) was obtained from the protein precipitation belonging to the class of the gluteline (Ip 4.5). The conditions for the preparation of the PI were determined by both the solubility curve and simultaneous thermogravimetry-differential thermal analysis (TG-DTA): pH 11.5, absence of NaCl and whiteners and T=( 25 +/- 3) degrees C. Under these conditions a yield of 77.0 +/- 0.4%, protein content of 94.2 +/- 0.3, ashes 0.50 +/- 0.05% and thermal stability, T= 200 degrees C, were obtained. The TG-DTA curves and the PI emulsification capacity study showed the presence of hydrophobic microdomains at pH 11.5 and 3.0 suggesting a random coil protein conformation and, to pH 10.0, an open protein conformation. The capacity of emulsification (CE), in the absence of NaCl, was verified for: 1 - pH 3.0 and 8.5, using the IP extracted at pH 10.0 and 11.5, CE >= 343 +/- 5 g of emulsified oil/g of protein; 2 - pH 6.60 just for the PI obtained at pH 11.5, CE >= 140 +/- 8 g of emulsified oil/g of protein.

Systematic analysis of protein-detergent complexes applying dynamic light scattering to optimize solutions for crystallization trials

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)