Composition and Nutritive Characteristics of Atlantic Canadian White Fish Meals

1974 ◽  
Vol 31 (2) ◽  
pp. 201-204 ◽  
Author(s):  
L. W. Regier ◽  
P. M. Jangaard ◽  
H. E. Power ◽  
B. E. March ◽  
J. Biely
Keyword(s):  
Amino Acids ◽  
Chemical Composition ◽  
Growth Response ◽  
Protein Quality ◽  
Eastern Canada ◽  
Available Lysine ◽  
Feeding Trials ◽  
Macro And Micronutrients ◽  
Composite Samples

Three composite samples of whitefish meals, each representing samples over 4 mo from plants in eastern Canada were analyzed for proximate composition, minerals, vitamins, amino acids, available lysine, and pepsin digestibility. Protein quality was evaluated biologically in feeding trials with chicks. The composite samples were similar in chemical composition with respect to both macro- and micronutrients. In vitro pepsin digestibility was 95–96% and chemically estimated available lysine 6.5–6.9 g/16 g N, or 87–96% of the total lysine present. The growth response to the meals, when they were fed to supply either 4 or 8% of supplementary protein in diets containing a total of 14.5 or 18.5% of protein, respectively, indicated that the supplementary protein value was high.

Influence of growing conditions on rumen escape protein and chemical composition in grass

2000 ◽  
Vol 2000 ◽  
pp. 56-56
Author(s):  
J.W. Cone ◽  
A.H. van Gelder ◽  
A.A. Kamman ◽  
V.A. Hindle
Keyword(s):  
Chemical Composition ◽  
Protein Quality ◽  
Streptomyces Griseus ◽  
Grass Silage ◽  
Growing Conditions

The amount of rumen escape protein is commonly determined with the nylon bag technique. However, there is also an in vitro technique described using a protease of Streptomyces griseus (Aufrère et al., 1991; Cone et al., 1996), allowing systematical analysis of protein quality in a large number of samples. The aim of this study was to identify the influences of growing conditions on content of rumen escape protein in grass and grass silage and to investigate the relationships between rumen escape protein determined in vitro and in situ and chemical composition.

scholarly journals Protein quality of feeding-stuffs

1967 ◽  
Vol 21 (1) ◽  
pp. 181-206 ◽  
Author(s):  
A. W. Boyne ◽  
S. A. Price ◽  
G. D. Rosen ◽  
J. A. Stott
Keyword(s):  
Optical Density ◽  
Bacterial Growth ◽  
Growth Response ◽  
Protein Quality ◽  
Skim Milk ◽  
Titratable Acidity ◽  
Tetrahymena Pyriformis ◽  
Collaborative Studies ◽  
Dry Grinding ◽  
Available Lysine

1. Samples of whale, meat, fish, groundnut and soya-bean meals and skim-milk powders were assayed microbiologically with Tetrahymena pyriformis W and Streptococcus zymogenes for available methionine and available lysine.2. Detailed collaborative studies on the assay of available methionine with Strep. zymogenes were conducted on the effects of dry- or wet-grinding the test meals, the use of crude or purified papain for predigesting the ground meals and the use of optical density or titratable acidity as criteria of bacterial growth response.3. Wide differences were observed in the available methionine and available lysine contents of a variety of meals in the preliminary studies, with a promising measure of interlaboratory agreement in the assay of available methionine with Strep. zymogenes.4. As a result of detailed collaborative studies a provisional method is proposed for the assay of available methione with Strep. zymogenes, adopting dry-grinding and predigestion with an agreed level of papain in the preparation of the meals. No general recommendation could be offered on the comparative merits of optical density and titratable acidity as criteria of bacterial growth response.

scholarly journals Available lysine and digestible amino acid contents of proteinaceous foods of India

2012 ◽  
Vol 108 (S2) ◽  
pp. S59-S68 ◽  
Author(s):  
Shane M. Rutherfurd ◽  
Kiran Bains ◽  
Paul J. Moughan
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Quality ◽  
Amino Acid Content ◽  
Essential Amino Acids ◽  
Food Ingredients ◽  
Available Lysine ◽  
Amino Acid Contents ◽  
Sulphur Amino Acids ◽  
Prepared Food

Cereals and legumes are staple foods in India and are limiting in lysine and sulphur amino acids, respectively. Available lysine loss, due to Maillard-type reactions that may occur during food preparation, exacerbates the problem of lysine deficiency particularly in cereals. Consequently, determining the contents of digestible essential amino acids, particularly lysine, is important. True ileal digestibilities of most amino acids (including total and reactive lysine) were determined for ten food ingredients and eleven foods commonly consumed in India. Semi-synthetic diets each containing either an ingredient or the prepared food as the sole protein source were formulated to contain 100 g kg− 1protein (75 g kg− 1for rice-based diets) and fed to growing rats. Titanium dioxide was included as an indigestible marker. Digesta were collected and the amino acid content (including reactive lysine) of diets and ileal digesta determined. Available (digestible reactive) lysine content ranged from 1·9–15·4 g kg− 1and 1·8–12·7 g kg− 1across the ingredients and prepared foods respectively. True ileal amino acid digestibility varied widely both across ingredients and prepared foods for each amino acid (on average 60–92 %) and across amino acids within each ingredient and prepared food (overall digestibility 31–96 %). Amino acid digestibility was low for many of the ingredients and prepared foods and consequently digestibility must be considered when assessing the protein quality of poorer quality foods. Given commonly encountered daily energy intakes for members of the Indian population, it is estimated that lysine is limiting for adults in many Indian diets.

scholarly journals Availability to pigs of amino acids in cereal grains

1981 ◽  
Vol 46 (1) ◽  
pp. 181-192 ◽  
Author(s):  
M. R. Taverner ◽  
D. J. Farrell
Keyword(s):  
Amino Acids ◽  
Bulk Density ◽  
Protein Digestibility ◽  
Cereal Grains ◽  
In Vitro Digestibility ◽  
Lysine Content ◽  
Ileal Digestibility ◽  
Acid Detergent Fibre ◽  
Available Lysine

1. Protein digestibility and lysine availability were determined in a range of grain samples using an in vitro digestibility assay calibrated with ileal digestibility values.2. Mean(± SE) values predicted for nitrogen digestibility were 0·92±0·011 in wheat and 0·88±0·021 in barley, and the predicted lysine availability in wheat was 0·86±0·021.3. Chemical and physical characteristics of the grains were determined and those most closely associated with protein digestibility for wheat were the contents of hemicellulose, neutral-detergent fibre, the bulk density, and to a lesser extent, N and acid-detergent fibre contents. These relationships were used to determine prediction equations for the available lysine content of wheat.

scholarly journals Availability to pigs of amino acids in cereal grains

1981 ◽  
Vol 46 (1) ◽  
pp. 173-180 ◽  
Author(s):  
M. R. Taverner ◽  
D. J. Farrell
Keyword(s):  
Amino Acids ◽  
Canonical Correlation ◽  
In Vitro Assay ◽  
Cereal Grains ◽  
In Vitro Digestibility ◽  
Vitro Assay ◽  
Indispensable Amino Acids ◽  
Available Lysine ◽  
The Difference

1. Availability values for amino acids in nine cereal grains determined by faecal analyses with pigs and by the Silcock available lysine test (Roach et al. 1967) and an in vitro digestibility assay were compared with ileal availability values for the same grains determined with pigs by Taverner et al. (1981b).2. There was a significant canonical correlation of ileal and faecal availability values. On average, apparent faecal availability of the indispensable amino acids was 4·2% greater than apparent ileal availability, but the difference was up to 12·6% for threonine. Furthermore, the difference appeared to increase as the digestibility of the grain decreased.3. Silcock available-lysine values for the cereal grains were unrelated to the lysine truly absorbed by the pig.4. There were close relationships of ileal protein and lysine availability values on nitrogen digestibility determined by an in vitro assay using pronase enzyme.

scholarly journals Identification of a sialoglycopeptide released by self-digestion from human erythrocyte membranes

1976 ◽  
Vol 158 (2) ◽  
pp. 497-500 ◽  
Author(s):  
A Brovelli ◽  
G Pallavicini ◽  
F Sinigaglia ◽  
C L Balduini ◽  
C Balduini
Keyword(s):  
Amino Acids ◽  
Chemical Composition ◽  
Human Erythrocyte ◽  
Molecular Size ◽  
Erythrocyte Membranes ◽  
Erythrocyte Ghosts ◽  
Human Erythrocyte Membranes

Membranes from human O Rhesus-positive erythrocyte ‘ghosts’ were tested in vitro for their ability to digest their own glycoproteins. ‘Ghost’ membranes incubated in Tris/HCl buffer, pH 7.4, release a sialoglycopeptide, which contains glucosamine, galactosamine, galactose and mainly polar amino acids. Chemical composition, molecular size and aggregation properties suggest that this glycopeptide may be a fragment of glycophorin.

scholarly journals In vitro Determination of the Release Kinetics of Peptides and Free Amino Acids During the Digestion of Food Proteins

2005 ◽  
Vol 88 (3) ◽  
pp. 935-948 ◽  
Author(s):  
Laurent Savoie ◽  
Rafael A Agudelo ◽  
Sylvie F Gauthier ◽  
Johanne Marin ◽  
Yves Pouliot
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Protein Quality ◽  
Release Kinetics ◽  
In Vitro Digestion ◽  
Exchange Chromatography ◽  
Protein Sources ◽  
Kinetics Of ◽  
Peptide Fractions

Abstract The kinetics of peptide release during in vitro digestion of 4 protein sources (casein, cod protein, soy protein, and gluten) were investigated. Samples were sequentially hydrolyzed with pepsin (30 min) and pancreatin (2, 4, or 6 h) in a dialysis cell with continuous removal of digestion products. Nondialyzed digests were fractionated by ion-exchange chromatography and ultrafiltration. Animal proteins were digested at a greater rate than plant proteins. Target amino acids of specific enzymes appeared more rapidly in the dialyzed fractions when compared to other amino acids. Throughout the hydrolysis, nondialyzed digests contained a higher proportion of peptide mixtures with basic-neutral properties. Except for gluten, peptide fractions with molecular weights that exceeded 10 kDa (basic-neutral, BN > 10) were rapidly hydrolyzed during the first 2 h of pancreatin digestion. The kinetics of release and the composition of peptide fractions were different when the protein sources were compared. The analysis of amino acids revealed that threonine and proline proportions were relatively high in BN > 10 and in peptide fractions with molecular weight between 10-1 kDa (BN 10-1), while tyrosine, phenylalanine, lysine, and arginine predominated in the low molecular weight (<1 kDa) fractions. More resistant peptides were generally rich in proline and glutamic acid. The role of in vitro digestion assays in dietary protein quality evaluation is discussed.

CHEMICAL COMPOSITION AND PROTEIN CHARACTERISTICS OF LENTILS

1976 ◽  
Vol 56 (4) ◽  
pp. 787-794 ◽  
Author(s):  
R. S. BHATTY ◽  
A. E. SLINKARD ◽  
F. W. SOSULSKI
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Quality ◽  
Protein Solubility ◽  
Nonprotein Nitrogen ◽  
Total Carbohydrate ◽  
Amino Acid Compositions ◽  
Chemical Score ◽  
Gross Energy

Chemical and amino acid compositions, protein solubility (Osborn classification), and in vitro protein quality of six genotypes of lentils (Lens culinaris Medik.) were determined. Lentils contained an average of 28.6% protein, 3.1% ash, 4.4% fiber, 0.7% ether extract, 63.1% total carbohydrate (nitrogen-free extract), 44.3% starch and 4,186 kcal/kg of gross energy. Lentil starch contained 36.1% amylose. About one-half (47.1%) of the lentil proteins were soluble in 1.0 M sodium chloride, 3.8% soluble in water, 3.1% soluble in 70% ethanol, and 14.9% soluble in dilute hydrochloric acid. Only 24.0% of the lentil proteins were not solubilized by these solvents. The lentils contained 6.8% of the meal nitrogen as nonprotein nitrogen. The amino acid compositions of the six lentil genotypes were similar. The major amino acids were glutamic acid, aspartic acid, arginine, leucine and lysine; the minor amino acids were methionine, cystine and tryptophan. Because of the lower concentrations of the latter amino acids, lentil proteins gave a chemical score of 35, a protein score of 46, and an essential amino acid index of 63, relative to egg protein.

scholarly journals The in vitro determination of the protein quality of rumen microorganisms of cows on urea-rich feed

1979 ◽  
Vol 51 (1) ◽  
pp. 68-78
Author(s):  
Eeva-Liisa Syväoja ◽  
Matti Kreula
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Protein Quality ◽  
Diaminopimelic Acid ◽  
In Vitro Digestibility ◽  
Amino Acid Compositions

The amino acid composition, essential amino acid index (EAA-I), pepsin-pancreatin in vitro digestibility and pepsin-pancreatin-digest-residue-index (PPDR-I) of the rumen bacterial and protozoal protein of cows fed urea and ammonium salts as their sole source of nitrogen (0-cows) or as a partial source (ULP-cows), and of cows on normal protein-rich feed (NorP-cows), were determined. The amino acid compositions of the rumen bacteria showed very slight changes even though the diets were very different. The amino acid compositions of the pure bacterial strains isolated from the rumina differed slightly. The amino acid compositions of the rumen protozoa of the ULP- and NorP-cows differed only with respect to isoleucine and tyrosine. Protozoa could be found only occasionally in the rumen of the 0-cow, there being only two species. Their nutritional significance was obviously very small. When the nutritional quality of the microbial protein was studied on the basis of its amino acid composition it was found that the EAA-I of bacteria did not differ significantly. Neither did the EAA-I of protozoa differ. The pepsin-pancreatin in vitro digestibility of protozoa was higher on all the feeds than that of bacteria. The rumen bacterial in vitro digestibility with 0-cows differed from that of the ULP-samples but not from that of the NorP-samples. The digestibility of single amino acids, With the exception of diaminopimelic acid, glycine and alanine, did not differ from the digestibility of the total amino acids. The much larger number of bacteria in the rumen of 0-cows compared with those of ULP- and NorP-cows compensates in this way for the lower digestibility of bacterial protein in 0-cows. The PPDR-I of both bacteria and protozoa were well correlated with the in vitro digestibility.

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