Reactive extraction of amino acids mixture in hydrolysate from cottonseed meal with di(2-ethylhexyl) phosphoric acid

2014 ◽  
Vol 91 (2) ◽  
pp. 483-489 ◽  
Author(s):  
Jian Zhang ◽  
Shunxi Zhang ◽  
Xinni Yang ◽  
Ling Qiu ◽  
Bing Gao ◽  
...  



1980 ◽  
Vol 35 (6) ◽  
pp. 727-730
Author(s):  
Oemer Saygin ◽  
Peter Decker

Abstract Nonenzymatic catalysis by bivalent ions of Be, Mg, Ca, Zn, Mn, Ni and Co and bioorganic phosphates of the formation of hydroxamic acids from acetate or amino acids has been studied systematically. Increased yields of hydroxamate were observed at particular combinations of reactants. The most prominent increase (ca. 15-fold) was found with acetate and Ni++, and with a combination of ATP and Be++. Among others especially ribose-5-phosphate and glucose-5-phosphate enhanced yields in the presence of most metal ions. Since no release of inorganic phosphate was observed, this effect cannot be interpreted as an evidence for intermediate transhosphorylation reactions; it may also result from simple catalytic effects of metal sugar complexes.





2011 ◽  
Vol 10 (44) ◽  
pp. 8950-8955
Author(s):  
Z Kamran ◽  
Foroudi Farhad ◽  
V Vardanyan Albert ◽  
Molaei Mohamad


1962 ◽  
Vol 40 (5) ◽  
pp. 1018-1022 ◽  
Author(s):  
Florante A. Quiocho ◽  
Felix Friedberg

Treatment of ATP:creatine phosphotransferase with anhydrous sulphuric acid permits transposition of 24% of the threonine residues and 69% of the serine residues. Treatment with anhydrous phosphoric acid yields similar results: 41% of the threonine residues and 60% of the serine residues are rearranged. Anhydrous formic acid does not induce an N- to O-acyl migration in the protein.Non-specific hydrolysis of peptide bonds or destruction of certain amino acids that might have occurred simultaneously with rearrangement during the anhydrous sulphuric or anhydrous phosphoric acid appears to be very slight. When the protein is treated with anhydrous sulphuric acid, however, phenylalanine "disappears" almost completely from the chromatogram.



1994 ◽  
Vol 71 (4) ◽  
pp. 531-541 ◽  
Author(s):  
E. S. Batterham ◽  
L. M. Andersen

Two experiments were conducted to determine the utilization of ileal digestible isoleucine by growing pigs. In the first, the apparent ileal digestibility of amino acids in cottonseed meal, lupin-seed meal and soya-bean meal was determined in pigs fitted with‘T‘-shaped cannulas. In the second, three isoleucine-deficient diets were formulated to 0.23 g ileal digestible isoleucine/MJ digestible energy (DE) with the three protein concentrates contributing the only source of isoleucine in sucrose-based diets. An additional three diets were formulated with supplements of isoleucine to confirm that isoleucine was limiting in the first three diets. The growth performance and retention of isoleucine by pigs given the six diets over the 20–45 kg growth phase were then determined. The apparent ileal digestibility of isoleucine in the three protein concentrates (proportion of total) was: cottonseed meal 0.68, lupin-seed meal 0.86, soya-bean meal 0.86. There were no significant differences (P > 0.05) in growth rates (g/d) and crude protein deposition rates (g/d) of the pigs given the three diets formulated to 0.23 g ileal digestible isoleucine/MJ DE: cottonseed meal 590, 84; lupin-seed meal 613, 87; soya-bean meal 594, 91 (SEM 13.0, 2.9) respectively. The response of pigs to the addition of isoleucine confirmed that isoleucine was limiting in these diets. The proportion of ileal digestible isoleucine retained by pigs given the cottonseed meal (0.65) was slightly lower than that retained by pigs given soya-bean meal (0.73; P < 0.05). These results indicate that values for the ileal digestibility of isoleucine in protein concentrates more closely reflect the proportion of isoleucine that can be utilized by the pig than occurs for other amino acids such as lysine, threonine and methionine.



1952 ◽  
Vol 31 (1) ◽  
pp. 110-114 ◽  
Author(s):  
L.J. Machlin ◽  
C.A. Denton ◽  
H.R. Bird


1997 ◽  
Vol 346 (2) ◽  
pp. 191-197 ◽  
Author(s):  
Piotr Wieczorek ◽  
Jan Åke Jönsson ◽  
Lennart Mathiasson


1970 ◽  
Vol 21 (8) ◽  
pp. 437-438 ◽  
Author(s):  
Myna Panemangalore ◽  
M. N. Guttikar ◽  
M. Narayana Rao ◽  
M. Swaminathan


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