MIXED FEED FORMULA FOR VALUABLE FISH SPECIES WITH REPLACE THE EXPENSIVE PROTEIN COMPONENTS BY GREEN PROTEIN CONCENTRATES

10.12737/7731 ◽  
2014 ◽  
Vol 9 (4) ◽  
pp. 83-87
Author(s):  
Рудой ◽  
Dmitriy Rudoy

This article presents the results of a study of the amino acid composition of green protein concentrates. The technique of recalculation of formulations for the replacement of expensive protein components by the protein concentrates from green plants. The authors drafted recommendations for replacement such feed ingredients like soy, meat and bone and fish meal by cheaper green protein concentrates. According to the protein content, the soybean is proposed to replace by green protein concentrates of canola, alfalfa, fodder beet; the meat and bone meal by green protein concentrates of canola and alfalfa, fish meal by green protein concentrates of rape.

2020 ◽  
Vol 36 (4) ◽  
pp. 49-58
Author(s):  
V.V. Kolpakova ◽  
R.V. Ulanova ◽  
L.V. Chumikina ◽  
V.V. Bessonov

The goal of the study was to develop a biotechnological process for the production of protein concentrates via bioconversion of pea flour and whey, a secondary product of starch manufacture. Standard and special methods were used to analyze the chemical and biochemical composition of protein concentrates (amino acid, carbohydrate, and fractional) of flour, whey and protein concentrates. It was established that pea flour contains 52.28-57.05% water-soluble nitrogenous substances, 23.04-25.50% salt-soluble, 2.94-4.69% alcohol-soluble compounds, 0-0.61% of soluble glutenine, 6.67-10.40% alkali-soluble glutenine and 5.96-10.86% insoluble sclerotic substances. A mathematical model and optimal parameters of the enzymatic extraction of pea protein with a yield of 65-70% were developed. Ultrasonic exposure increased the yield of nitrogenous substances by 23.16 ± 0.69%, compared with the control without ultrasound. The protein concentrate had a mass fraction of nitrogenous substances of 72.48 ± 0.41% (Nx6.25) and a complete amino acid composition. The microbial conversion by the Saccharomyces cerevisiae 121 and Geotrichum candidum 977 cultures of starch whey which remained after protein precipitation allowed us to obtain feed concentrates from biomass and culture liquid with a protein mass fraction of 61.68-70.48% (Nx6.25). Protein concentrates positively affected the vital signs of rats and their excretory products. A technological scheme was developed to test the complex pea grain and starch whey processing under pilot conditions. pea, protein concentrate, extracts, whey, bioconversion, Geotrichum candidum, Saccharomyces cerevisiae, chemical composition, amino acid composition


1975 ◽  
Vol 29 (2) ◽  
pp. 250-254
Author(s):  
C. Christias ◽  
C. Couvaraki ◽  
S. G. Georgopoulos ◽  
B. Macris ◽  
V. Vomvoyanni

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Ping Feng ◽  
Ming Gao ◽  
Timothy Holley ◽  
TianHui Zhou ◽  
Anita Burgher ◽  
...  

2021 ◽  
pp. 38-40
Author(s):  
Денис Сергеевич Куликов ◽  
Валентина Андреевна Гулакова ◽  
Валентина Васильевна Колпакова ◽  
Рузалия Владимировна Уланова

Из зерна нута получены белковые концентраты пищевого и кормового назначения с массовой долей белка на сухое вещество 83,22±0,35 % и 54,22±0,46 % соответственно и сбалансированным аминокислотным составом. Protein concentrates for food and feed purposes were obtained from chickpea grains with a mass fraction of protein per dry matter of 83.22±0.35 % and 54.22±0.46 %, respectively, and a balanced amino acid composition.


1988 ◽  
Vol 51 (10) ◽  
pp. 807-810 ◽  
Author(s):  
DILEK HEPERKAN ◽  
ÍHSAN ALPERDEN

Level of mold contamination and mycoflora were determined for 144 mixed feed and feed ingredients, including corn, sunflower cake, soja cake, meat and bone meal, and fish meal. Four samples were found to be free of mold. Among the feed samples examined, the mold count has been found to be low (102 to 103 colonies/g) for fish meal, high (104 to 105 colonies/g) for meat-bone meal and sunflower cake, and extremely high (more than 105 colonies/g) for soja cake, corn and mixed feed. The predominant flora in the feed samples consisted of Penicillium, Aspergillus, Fusarium, Mucor and Eurotium, respectively. The most frequently encountered species was found to be Penicillium aurantiogriseum, followed by Aspergillus flavus.


Blood ◽  
1974 ◽  
Vol 44 (2) ◽  
pp. 235-246 ◽  
Author(s):  
I. Olsson ◽  
P. Venge

Abstract The highly cationic proteins of human granulocytes, whose electrophoretic mobilities toward the cathode are faster than that for lysozyme, were isolated from the cytoplasmic granules of leukocytes, obtained from patients with chronic myeloid leukemia. The granule extract was subjected to chromatography on Sephadex G-75 and E-aminocaproic acid-Sepharose ion adsorbant followed by preparative electrophoresis on agarose. Seven cationic protein components were identified, and five of these were obtained in a pure form. One group of cationic proteins, including components 1-4, exhibited molecular weights in the range 25,500-28,500, almost identical amino acid composition, and complete immunologic identity. Another group of proteins, including components 5-7, exhibited molecular weights in the range 21,000-29,000 and also showed complete immunologic identity; amino acid analysis performed on component 5 indicated a different amino acid composition from that of components 1-4. Cationic proteins with similar electrophoretic mobilities and immunochemical identities were also detected in granule extracts of granulocytes from healthy individuals. The proteins isolated from human granulocytes have a higher molecular weight and a lower content of basic amino acids than the cationic proteins with antibacterial and permeability-increasing properties previously demonstrated in rabbit polymorphonuclear granulocytes.


1987 ◽  
Vol 66 (12) ◽  
pp. 1721-1726 ◽  
Author(s):  
T. Aoba ◽  
T. Tanabe ◽  
E.C. Moreno

The fluid was separated from the immature soft enamel of porcine permanent teeth in the secretory stage according to procedures reported previously (Aoba and Moreno, 1987). The protein content of the fluid was about 2.8% w/v; its amino-acid composition was characterized by high contents of Pro, Glx, Leu, and His, showing composition similar to that of the 20 kilo-dalton (kd) amelogenin or its C-terminal segments. The two major protein species in the fluid had apparent molecular weights of 13 kd and 11 kd, as determined by SDS electrophoresis; the N-terminal residue of the former was Leu, while that of the latter was Ala. The C-terminal sequence of both of them was -Met-Phe-Ser. By comparison with the published sequence of 20-kd porcine amelogenin, it is concluded that the main fluid constituents were derived by cleavages of N-terminal segments from the 20-kd amelogenin.


Sign in / Sign up

Export Citation Format

Share Document