Amino acid profiles of chemical and anatomical fractions of oat grains

Draper, S. R.

doi:10.1002/jsfa.2740241013

Cited by 37 publications

(18 citation statements)

References 9 publications

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“…This further confirms that AA composition of leaf proteins is generally conserved regardless of species. Note that the AA composition of oat grains reported in the present study generally agreed with that of whole oat meal reported by Draper (1973) (Table 3). Note.…”

Section: Amino Acid Composition Of Growing Oat Forages and Matured Grsupporting

confidence: 90%

“…This makes comparisons among studies possible. In Table 3, the AA compositions of forage and grain from two oat varieties for the present study are shown, along with those of alfalfa leaves, orchard grass, and whole oat meal adapted from previous reports (Fiorentini & Galoppini, 1983;Kammes et al, 2011;Draper, 1973), all expressed as % of total AA recovered for easy comparison. Results indicate that AA composition of oat forage changed with growing stages and differed from that of grain.…”

Section: Amino Acid Composition Of Growing Oat Forages and Matured Grmentioning

confidence: 99%

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Nutrient Composition and Protein Extractability of Oat Forage Harvested at Different Maturity Stages as Compared to Grain

Liu¹,

Mahmood

2015

JAS

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Two oat varieties (CDC Dancer and Lamont) were grown in fields. Plants were harvested at three key stages: seedling (Forage 1), mid-season (Forage 2), and full grain maturity. The mature plants were separated into stover (Forage 3) and Grain. There were differential changes among measured attributes during growth. From seeds to Forage 1, crude protein (CP) and ash contents increased several fold, beta-glucan decreased, starch disappeared, and oil content remained unchanged for both oat varieties examined. As plants grew, CP, ash, oil and beta-glucan decreased, but other carbohydrates increased significantly. The CP content in Forage 1 was 5-fold higher than Forage 3 and 2-fold higher than Grain. Most macro and micro-minerals in forage followed the same changing pattern as ash. Amino acid composition of forage differed significantly from that of Grain. When subjected to aqueous media with a wide range of pH, forage harvested at each stage as well as grain all had their unique protein extractability curves. For forage, the peak value (the maximum extraction) decreased with maturity. Yet, as observed for both varieties, Forage 1 had a peak value half of that from Grain. In conclusion, based on the results from this study, nutrient composition in oat forages harvested at an early stage can be comparable or even superior to oat grains but low protein extractability limits oat forage use as an alternative protein source for non-ruminants.

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Section: Amino Acid Composition Of Growing Oat Forages and Matured Grsupporting

confidence: 90%

Section: Amino Acid Composition Of Growing Oat Forages and Matured Grmentioning

confidence: 99%

Nutrient Composition and Protein Extractability of Oat Forage Harvested at Different Maturity Stages as Compared to Grain

Liu¹,

Mahmood

2015

JAS

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“…Danielsson (3), in early work with the ultracentrifuge, reported sedimentation constants of 2.6 and 8.1 for oat globulin. The amino acid composition of the oat globulin fraction has been reported (5,19). Cell-free synthesis of oat globulin was achieved by Luthe and Peterson (10).…”

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confidence: 99%

Subunit Structure and Composition of Oat Seed Globulin

Peterson¹

1978

Plant Physiol.

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Oat (Avena sadva L.) seed globuln was extracted from pound caryopses with 1 M NaCI, 0.05 M Tris(hydroxymethyl)antnoethane (pH 8.5) at room temperature. The globulin had a sedimentation constant of 12.1, and a molecular weight of 322,000, as determined by analytical ultracentrifugation. The globulin could be separated into two major subunits by sodiumdodecyl sulfate polyacrylamide gel electropboresis. Molecular weights of the subunits were 21,700 (a) and 31,700 (p8), and they were present in equimolar amounts. A subunit model of 6a and 6p8 per molecule of globulin is proposed. Amino acid analysis ilndicated that the a subunit contained more basic amino acids and aspartic acid/asparagine but less glutamic acid/glutamine and glycine than the p subunit.In oat (Avena sativa L.) kernels, the primary storage protein is classified as a globulin because of its solubility in dilute salt solution but insolubility in water (1). The globulin fraction accounts for the majority of total seed protein (1,13,14). The alcohol-soluble prolamin fraction, which is the major seed storage protein in most cereals, is very low in oats (1,6,11,13,14).In To determine the solubility of oat globulin under various conditions, the defatted flour was extracted with 1 M NaCl, 0.05 M Tris (pH 8.5) at a ratio of 100 ml/g, using magnetic stirring at room temperature for 1 to 2 hr. The extract was centrifuged for 20 min at 23 C and 27,000g, and the supernatant was dialyzed against two changes of distilled H20 at 4 C, precipitating the globulin. Ten-ml aliquots of the dialysate were centrifuged as above, but at 1 C to collect the suspended globulin precipitate. The various test solutions (1.5 ml) were added, and a Vortex mixer and ultrasonic bath were used at 23 C to achieve maximum dissolution. The solutions were centrifuged at 23 C and 27,000g for 20 min to pellet the undissolved protein, and the supernatants were assayed for protein (9) using BSA (Sigma, fraction V) as the standard.The globulin was normally prepared by extraction and dialysis as described above, and the dialysate was freeze-dried to recover the globulin from suspension. The dried globulin was stored indefinitely at -20 C.Analytical Ultracentrifugation. The oat globulin was dissolved in 0.5 M NaCl, 0.05 M Tris (pH 8.5) at a concentration of 3.2 mg/ml for sedimentation velocity analysis at 40,000 rpm and 20C on a Spinco model E ultracentrifuge. S20, was determined as described by Svedberg and Pedersen (18). For mol wt estimation, a sedimentation equilibrium analysis was done at 10,589 rpm, 20 C, for 10 hr. Partial specific volume was estimated by summation of the products of partial specific volume and weight per cent of each amino acid (16). Mol Wt Estimation by Polyacrylamide Gel Electropboresis. Oat globulin was solubilized in Triton X-100 and electrophoresed on polyacrylamide gels containing 4 to 10% acrylamide. The procedures of Hearing et al. (7)

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“…1 oats from 2 crop years were substituted for corn and soybean meal at levels of tj, S00, 600 and 782 or 808 g kg-' in isoenergetic and isolysinic diets. Egg yield (46.4 (Draper 1973) is better …”

mentioning

confidence: 99%

EVALUATION OF NAKED OATS (Avena nuda) AS A FEEDINGSTUFF FOR LAYING HENS

Cave¹,

Hamilton²,

Burrows³

1989

Can. J. Anim. Sci.

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C,c,vB, N. A', HerraLroN, R. M. G' eNp BURROWS, V' D. 1989. Evaluation of naked oats lAyetn nuda) as a feedingstuff for laying hens. Can. J. Anim. Sci. 69: '189-799 ' Two experiments were conducted with 640 and 480 White Leghorn strain-cross hens to determine the optimum level of inclusion of naked oats (Avena nuda L. 'Tibor') in diets fed for 51 wk. In exp. 1 oats from 2 crop years were substituted for corn and soybean meal at levels of tj, S00, 600 and 782 or 808 g kg-' in isoenergetic and isolysinic diets. Egg yield (46.4 (Draper 1973) is better

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Amino acid profiles of chemical and anatomical fractions of oat grains

Cited by 37 publications

References 9 publications

Nutrient Composition and Protein Extractability of Oat Forage Harvested at Different Maturity Stages as Compared to Grain

Nutrient Composition and Protein Extractability of Oat Forage Harvested at Different Maturity Stages as Compared to Grain

Subunit Structure and Composition of Oat Seed Globulin

EVALUATION OF NAKED OATS (Avena nuda) AS A FEEDINGSTUFF FOR LAYING HENS

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