scholarly journals Determination of digestible and available amino acids in meat meal using conventional and caecectomized cockerels or chick growth assays

1986 ◽  
Vol 56 (1) ◽  
pp. 227-240 ◽  
Author(s):  
Carl M. Parsons

1. The present study was designed to compare true digestible amino acid values for meat meal with available amino acid values. True digestible values were determined with a 48 h excreta collection assay using conventional (CONV) and caecectomized (CEC) cockerels. Available values for lysine, methionine and cystine were estimated by chick growth assays.2. True digestibilities of all sixteen measured amino acids (expressed as a proportion of the total) were lower for CEC than for CONV cockerels, with the average difference being approximately 0.10.3. Chick growth assays based on total weight gain indicated that the availabilities of amino acids expressed as a proportion of the total amino acids in meat meal were: 0.70 for lysine, 0.75 for methionine and 0.48 for cystine. Partitioning weight gains to reflect only growth attributable to supplemental crystalline amino acid or meat meal intake consistently yielded higher availability values than when total weight gains were used.4. True digestibility values determined with CEC cockerels were in better agreement with chick available values than were true digestibility values determined with CONV cockerels.5. The amounts of amino acids present in the caeca of meat meal-fed CONV cockerels at 48 h after feeding were small when compared with those levels voided in the excreta and those levels consumed in the feed.6. Multiple regression analyses of excreta and caecal amino acid profiles at 12 and 48 h after feeding suggested that significant amounts of non-digested dietary amino acids flowed into the caeca and were subsequently metabolized by the caecal microflora.

1974 ◽  
Vol 25 (1) ◽  
pp. 193 ◽  
Author(s):  
GR Skurray ◽  
RB Cumming

When a commercial meat meal was used to supplement wheat, corn and sorghum diets to growing chicks, there was a wide variation in performance. Feed conversion efficiencies were higher on diets based on wheat and corn than those based on sorghum. The nutritive value as determined by chick growth tests of a wheat-plus-meat meal diet was higher than a corn or sorghum-plus-meat meal diet. The nutritive value of a wheat–plus–meat meal diet, supplemented with lysine and methionine, was the same as that of a crystalline amino acid reference diet. The weight gains of chicks given these two diets were higher than those obtained with diets based on wheat, corn and sorghum, not supplemented with lysine and methionine. The results were explained in terms of the limiting and digestible essential amino acids in these diets. The limiting amino acids in the diets were determined from the plasma amino acid levels in chicks given these diets. ______________________ *Part VII, Aust. J. agric. Res., 23: 913-22 (1972).


1964 ◽  
Vol 44 (2) ◽  
pp. 228-234 ◽  
Author(s):  
J. D. Summers ◽  
S. J. Slinger ◽  
G. C. Ashton

When meat meal was used as the sole source of protein in a ration it did not support satisfactory weight gains in growing chickens. However, when the meat meal was supplemented with the amino acids in which it is limiting, satisfactory weight gains were achieved. One may conclude that the main problem with meat meal protein is one of amino acid imbalance rather than digestibility.It has been demonstrated in the present study that meat meal offered for sale in Ontario may be deficient in six amino acids as compared with soybean meal. These amino acids may be classified in order of their degree of deficiency. Methionine is easily the first limiting amino acid while tryptophane and isoleucine are second and about equally limiting. Cystine, threonine, and arginine are next in order of limitation. Part of the lack of response obtained when meat meal constitutes all of the protein in experimental diets can be explained on the basis of the excessive levels of calcium and phosphorus in the diet.


Molecules ◽  
2021 ◽  
Vol 26 (7) ◽  
pp. 2033
Author(s):  
Chuleeporn Bungthong ◽  
Sirithon Siriamornpun

Silk proteins have many advantageous components including proteins and pigments. The proteins—sericin and fibroin—have been widely studied for medical applications due to their good physiochemical properties and biological activities. Various strains of cocoon display different compositions such as amino-acid profiles and levels of antioxidant activity. Therefore, the objectives of this study were to find a suitable silk protein extraction method to obtain products with chemical and biological properties suitable as functional foods in two strains of Bombyx mori silk cocoon (Nangsew strains; yellow cocoon) and Samia ricini silk cocoon (Eri strains; white cocoon) extracted by water at 100 °C for 2, 4, 6 and 8 h. The results showed that Nangsew strains extracted for 6 h contained the highest amounts of protein, amino acids, total phenolics (TPC) and total flavonoids (TFC), plus DPPH radical-scavenging activity, ABTS radical scavenging capacity, and ferric reducing antioxidant power (FRAP), anti-glycation, α-amylase and α-glucosidase inhibition. The longer extraction time produced higher concentrations of amino acids, contributing to sweet and umami tastes in both silk strains. It seemed that the bitterness decreased as the extraction time increased, resulting in improvements in the sweetness and umami of silk-protein extracts.


2016 ◽  
Vol 101 (5) ◽  
pp. 2047-2055 ◽  
Author(s):  
Petri Wiklund ◽  
Xiaobo Zhang ◽  
Xiao Tan ◽  
Sirkka Keinänen-Kiukaanniemi ◽  
Markku Alen ◽  
...  

AbstractContext:Branched-chain and aromatic amino acids are associated with high risk of developing dyslipidemia and type II diabetes in adults.Objective:This study aimed to examine whether serum amino acid profiles associate with triglyceride concentrations during pubertal growth and predict hypertriglyceridemia in early adulthood.Design:This was a 7.5-year longitudinal study.Setting:The study was conducted at the Health Science Laboratory, University of Jyväskylä.Participants:A total of 396 nondiabetic Finnish girls aged 11.2 ± 0.8 years at the baseline participated in the study.Main Outcome Measures:Body composition was assessed by dual-energy x-ray absorptiometry; serum concentrations of glucose, insulin, and triglyceride by enzymatic photometric methods; and amino acids by nuclear magnetic resonance spectroscopy.Results:Serum leucine and isoleucine correlated significantly with future triglyceride, independent of baseline triglyceride level (P < .05 for all). In early adulthood (at the age of 18 years), these amino acids were significantly associated with hypertriglyceridemia, whereas fat mass and homeostasis model assessment of insulin resistance were not. Leucine was the strongest determinant discriminating subjects with hypertriglyceridemia from those with normal triglyceride level (area under the curve, 0.822; 95% confidence interval, 0.740–0.903; P = .000001).Conclusions:Serum leucine and isoleucine were associated with future serum triglyceride levels in girls during pubertal growth and predicted hypertriglyceridemia in early adulthood. Therefore, these amino acid indices may serve as biomarkers to identify individuals at high risk for developing hypertriglyceridemia and cardiovascular disease later in life. Further studies are needed to elucidate the role these amino acids play in the lipid metabolism.


2005 ◽  
Vol 17 (2) ◽  
pp. 216
Author(s):  
P. Booth ◽  
T. Watson ◽  
H. Leese

Pre-implantation embryos can produce and consume amino acids in a manner dependent upon stage of embryonic development (Partridge and Leese 1996 Reprod. Fert. Dev. 8, 945) that may also be predictive of subsequent viability (Houghton et al. 2002 Hum. Reprod. 17, 999). To examine these relationships in the pig, the appearance or depletion of 18 amino acids from a presumptive near-physiological mixture was determined by HPLC in porcine in vitro-produced embryos from the zygote to the blastocyst stage. Cumulus oocyte complexes derived from slaughterhouse prepubertal pig ovaries were matured for 40 h in modified TCM-199 before being fertilized (Day 0) with frozen thawed semen in tris-based medium. After 6 h, presumptive zygotes were denuded and cultured in groups of 20 in NCSU medium modified to contain a physiological mixture of 18 amino acids including 0.1 mM glutamine (NCSUaa). Groups of 2–10 embryos (dependent on stage) were removed on Day 0 (1 cell), Day 1 (2- and 4-cell), Day 4 (compact morula), and Day 6 (blastocyst) and placed in 4 μL NCSUaa for 24 h. After incubation, the embryos were removed and the medium analyzed by HPLC. Each stage was replicated 3–9 times. Since amino acid profiles of 2- and 4-cell embryos were not different, data were combined. Overall, arginine (1.19 ± 0.33), glutamine (0.78 ± 0.34) and threonine (0.05 ± 0.04) were significantly (P < 0.01) depleted from the medium whereas alanine (0.21 ± 0.1), glycine (0.20 ± 0.06), asparagine (0.13 ± 0.5), lysine (0.1 ± 0.03), isoleucine (0.08 ± 0.01), valine (0.05 ± 0.01), leucine (0.04 ± 0.02), phenylalanine (0.03 ± 0.01), and histidine (0.02 ± 0.04) significantly (P < 0.05) accumulated (mean of the 4 sampling timepoints; all values pmol/embryo/h ± SEM). The difference between amino acid accumulation and depletion (balance) was approximately equivalent between Day 0 and the morula stage although turnover (sum of depletion and accumulation) steadily decreased during this period from 3.1 on Day 0 to 1.35 pmol/embryo/h at the morula stage. However, at the blastocyst stage, turnover and balance increased to 6.32 and 2.42 pmol/embryo/h, respectively, i.e. net appearance occurred. Notable changes in amino acid profile during development included decreases in accumulation of asparagine, glutamate, and glycine in the medium and the depletion of glutamine over Days 0, 1, and 4, followed by reversal of these trends by Day 6. These data suggest that pig embryos can alter the accumulation and depletion rates of amino acids in a manner that is dependent on the specific amino acid and the stage of embryonic development. This work was supported by BBSRC.


1994 ◽  
Vol 266 (5) ◽  
pp. R1675-R1686 ◽  
Author(s):  
G. H. Anderson ◽  
E. T. Li ◽  
S. P. Anthony ◽  
L. T. Ng ◽  
R. Bialik

The relationship between plasma and brain amino acids and short-term food intake after administration of albumin, or its constituent amino acids, was examined. Rats given protein (0.85 g chicken egg albumin) or an amino acid mixture patterned after egg albumin reduced their food intake during 1 h of feeding beginning 30 min after gavage. Similarly, when given separately, the essential (EAA) and nonessential amino acid (NEAA) fractions of egg albumin caused comparable decreases in food intake. As the dose increased from 0.5 to 1.5 g the duration of anorexia prolonged to 12 h. Little change occurred in plasma amino acids at 30 and 60 min after albumin at 0.85 g, although many increased by 25-50% at 60 min after 1.5 g. Marked changes in plasma occurred after gavage with the total mixture of constituent free amino acids and after either EAA or NEAA fractions. Brain amino acid concentrations were little affected by albumin and did not show consistent changes after the amino acid treatments. Thus the reductions in food intake after ingestion of albumin or of its constituent amino acids were not predicted from the resulting changes in either plasma or brain concentrations of amino acids.


1983 ◽  
Vol 50 (2) ◽  
pp. 391-399 ◽  
Author(s):  
Kyu-Il Kim ◽  
James I. Elliott ◽  
Henry S. Bayley

1. The catabolism of [14C]phenylalanine was used to indicate the effects of varying the dietary level of lysine and threonine on the retention of dietary amino acids by 2-week-old pigs receiving diets containing skim milk and a mixture of free amino acids.2. Reducing the dietary level of lysine from 16 to 12 g/kg had no influence on phenylalanine oxidation, reducing the lysine level from 12 to 11 then to 10 g/kg caused an almost linear increase in phenylalanine oxidation whereas further reduction to 9 or 8 g/kg resulted in a less-marked increase in phenylalanine oxidation. This showed that 12 g lysine/kg was required to maximize amino acid retention and indicated that lysine was conserved more effectively at low dietary concentrations than at dietary concentrations approaching the requirement.3. Reducing the dietary level of threonine from 8 to 6 g/kg had no influence on phenylalanine oxidation, whereas further reduction to 4 g/kg caused a linear increase in phenylalanine catabolism showing that 6 g threonine/kg was required to maximize amino acid retention.4. Reduction of the levels of lysine, threonine and methionine from the generous levels characteristic of a diet containing 240 g protein from skim milk/kg, to the requirement levels determined separately in the presence of the generous levels of all the other amino acids, resulted in a twofold increase in phenylalanine catabolism. This shows that the pig seems able to conserve limiting intakes of a single amino acid, but not if the intakes of two or three amino acids are limiting.


1986 ◽  
Vol 55 (3) ◽  
pp. 659-668 ◽  
Author(s):  
Ronald O. Ball ◽  
James L. Atkinson ◽  
Henry S. Bayley

1. The catabolism of L-[ l-14C]phenylalanine was used to indicate the effects of single amino acid supplementation of an inadequate protein diet (200 g crude protein (nitrogen x 6.25)/kg) on the utilization of dietary amino acids in pigs of 2.5 kg body-weight reared on an adequate protein diet (240 g crude protein/kg) containing skim milk and a mixture of free amino acids.2. The oxidation of phenylalanine was decreased by the addition of proline or arginine to the inadequate protein diet but not by the addition of threonine, methionine, lysine or a mixture of essential amino acids, indicating that proline and arginine were limiting the utilization of dietary amino acids in the inadequate protein diet.3. Dietary proline concentrations of 13.9 and 14.2 g/kg minimized phenylalanine oxidation in diets containing 200 or 260 g protein/kg. This indicates a dietary proline requirement of 14 g/kg.4. Increasing the dietary arginine concentration in a diet containing 240 g protein/kg showed that an arginine concentration of 5.1 g/kg minimized phenylalanine oxidation. However, increasing the arginine concentration in a diet containing 200 g protein/kg increased phenylalanine oxidation, suggesting an amino acid imbalance involving arginine at this lower level of protein.


SpringerPlus ◽  
2014 ◽  
Vol 3 (1) ◽  
pp. 35 ◽  
Author(s):  
Takuya Matsumoto ◽  
Koichi Nakamura ◽  
Hideki Matsumoto ◽  
Ryosei Sakai ◽  
Tomomi Kuwahara ◽  
...  

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