scholarly journals Morphological composition of the body and chemical composition of trout meat depending on amino acid levels in feed

2021 ◽  
pp. 188-195
Author(s):  
V.M. Kondratiuk ◽  
A.O. Ivaniuta
10.5219/1601 ◽  
2021 ◽  
Vol 15 ◽  
pp. 497-505
Author(s):  
Vadym Kondratiuk ◽  
Volodymyr Otchenashko

The article studies the effect of using complete compound feeds with different energy levels on the morphological composition of the body and the amino acid composition of trout meat proteins. The experiment aimed to establish the influence of different levels of energy nutrition of commercial rainbow trout on the morphological composition of their body and the amino acid composition of meat proteins. For this purpose, five experimental groups were formed using the analog method. The study lasted 210 days and was divided into two periods: comparative (10 days) and main (200 days). During the comparative period, the study fish consumed compound feed of the control group. During the main period, the energy level in experimental compound feeds for different experimental trout groups ranged from 16 to 20 mJ per 1 kg. It was found that with an increase in the mass of two-year-old trout, the mass of muscle tissue and the yield of edible parts probably increases. Feeding fish with an increased amount of metabolic energy (20 mJ.kg-1) resulted in a significant change in the weight of internal organs, including the heart, liver, and kidneys. Increasing the metabolic energy in the compound feeds of fish from 18 mJ.kg-1 to 19 – 20 mJ.kg-1 leads to a significant increase in bowel mass by 13.3 – 5.0%. An increase in the level of metabolic energy in rainbow trout diets from 18 mJ.kg-1 to 19 – 20 mJ.kg-1 contributed to a likely increase in the methionine content in meat. A similar pattern was observed for the tryptophan content. It was found that the content of most essential amino acids in the protein of rainbow trout meat exceeds the corresponding values in the "ideal" protein, except for the content of isoleucine and leucine, which refers them to limiting amino acids.


2012 ◽  
Vol 14 (2) ◽  
pp. 97-107 ◽  
Author(s):  
EP da Silva ◽  
CBV Rabello ◽  
MB de Lima ◽  
EMF de Arruda ◽  
JV Ludke ◽  
...  

2021 ◽  
Vol 9 ◽  
Author(s):  
Aaron Ciechanover

Proteins are the engines of all forms of life, for humans and for all the plant and animal kingdoms. Proteins are used both to build organs (such as bones, muscles, and skin) and to perform bodily functions. These functions range from digestion (processing food and converting it into energy), to enabling movement and sensation (sight and hearing), to protecting the body from foreign invaders with our antibodies, which are also proteins. What are proteins? They can be compared to words in a language that contains letters. In the Hebrew alphabet, there are 26 letters out of which countless words can be composed. But when we write, we use just a fraction of these infinite options, with the average number of letters in a word ranging between 3 and 8. The biological “protein alphabet” is comprised of 20 “letters” called amino acids, which are the building blocks of the proteins that make up the body. Proteins are chains of amino acid, linked together in a specific order governed by the DNA. Unlike the words of a spoken language, the average protein consists of hundreds of amino acids. The extensive length of proteins and the chemical composition of the amino acids make proteins sensitive to many factors, such as high temperatures, radiation, and chemicals. All these factors damage proteins and alter their fragile structures, negatively affecting how they function. When proteins are damaged or when they finish performing their functions and are no longer needed, the body breaks them down. With my doctoral adviser, Prof. Avram Hershko, and our research collaborator, Prof. Irwin Rose from the Fox Chase Cancer Center in Philadelphia, we discovered the mechanism responsible for targeted degradation of proteins in cells. This degradation can recognize damaged proteins or proteins that are not needed anymore, while leaving intact the “healthy,” functional ones. This mechanism is called the ubiquitin system after its principal protein, ubiquitin, which was the first protein we discovered in the system. Ubiquitin’s role is to tag undesirable proteins so that the cell’s “grinder” can recognize them and break them down, enabling the cell to function normally. In this article, we will explain the story of proteins and the ubiquitin system that we discovered in a study that earned us, among other prizes, the Nobel Prize in Chemistry in 2004.


1962 ◽  
Vol 156 (964) ◽  
pp. 299-306

The centenary of Hopkins’s birth is also the sixtieth anniversary of the isolation of tryptophan by Hopkins & Cole (1901), and if in their paper they were in error over its constitution their work was, according to Harris (1949), one of the first to employ bacterial degradation as an aid to establishing chemical composition. The correct structure was established by Ellinger & Flamand in 1907. By 1906 Wilcock & Hopkins had shown that a particular protein zein failed as a protein source to support life and that the presence of a group in a protein molecule, viz. tryptophan, was a dietary essential and £served some purpose in the body other than forming tissue or supplying energy’. The concept and importance in nutrition of the essential amino acid thus emerges in the same year that we have Hopkins’s prophecy that ‘the factors whose deficiency were responsible for diseases such as scurvy and rickets were certainly of the kind which comprises the minimal qualitative factors which must be added to artificially refined diets to enable them to support mammalian survival and growth’: the tryptophan story was later to lead into this other realm of his activity.


2021 ◽  
Vol 22 (12) ◽  
pp. 6198
Author(s):  
Aleksandra A. Ageeva ◽  
Ilya M. Magin ◽  
Alexander B. Doktorov ◽  
Victor F. Plyusnin ◽  
Polina S. Kuznetsova ◽  
...  

The study of the L- and D-amino acid properties in proteins and peptides has attracted considerable attention in recent years, as the replacement of even one L-amino acid by its D-analogue due to aging of the body is resulted in a number of pathological conditions, including Alzheimer’s and Parkinson’s diseases. A recent trend is using short model systems to study the peculiarities of proteins with D-amino acids. In this report, the comparison of the excited states quenching of L- and D-tryptophan (Trp) in a model donor–acceptor dyad with (R)- and (S)-ketoprofen (KP-Trp) was carried out by photochemically induced dynamic nuclear polarization (CIDNP) and fluorescence spectroscopy. Quenching of the Trp excited states, which occurs via two mechanisms: prevailing resonance energy transfer (RET) and electron transfer (ET), indeed demonstrates some peculiarities for all three studied configurations of the dyad: (R,S)-, (S,R)-, and (S,S)-. Thus, the ET efficiency is identical for (S,R)- and (R,S)-enantiomers, while RET differs by 1.6 times. For (S,S)-, the CIDNP coefficient is almost an order of magnitude greater than for (R,S)- and (S,R)-. To understand the source of this difference, hyperpolarization of (S,S)-and (R,S)- has been calculated using theory involving the electron dipole–dipole interaction in the secular equation.


2021 ◽  
pp. 101327
Author(s):  
Maria Camila Alfaro-Wisaquillo ◽  
Edgar O. Oviedo-Rondón ◽  
Hernan A. Cordova-Noboa ◽  
Justina V. Caldas ◽  
Gustavo A. Quintana-Ospina ◽  
...  

2020 ◽  
Vol 98 (Supplement_3) ◽  
pp. 76-76
Author(s):  
Ron Ball ◽  
Crystal L Levesque ◽  
D J Cadogan

Abstract Most sows are fed a constant energy and amino acid supply throughout gestation, in line with the recommendations of most authorities and swine genetic companies. These recommendations for sow feeding have seen little change in decades, despite the many ways that sows have changed dramatically in reproductive performance. Beginning in about the year 2000, sow litter size has steadily increased as a result of genetic selection. With this increase in litter number has been a steady decline in birth weight, and the resulting negative effects of lower birthweight on subsequent piglet performance. Many experiments using so-called ‘bump’ feeding, or increased energy intake in late gestation, have been conducted in attempts to arrest this decline in birthweight and piglet performance. Generally, these experiments have shown little to no improvement in birthweight and often have negative effects on sow feed intake during gestation. These experiments have ignored the fact that the energy:amino acid ratios (lysine, threonine, isoleucine, tryptophan) in late gestation are different than during early and mid-gestation. In recent research in Australia we hypothesised that rapidly increasing essential amino acid levels in late gestation would increase birth weight and potentially improve subsequent reproductive performance. Three hundred and thirty-four multiparous PIC sows (average parity 3.6, average LW 261 kg) were housed in a dynamic gestation pen after mating and randomly assigned to one of two diet regimes. Two 13.5 MJ/kg DE gestation diets were formulated and created by blending in an ESF. The Control diet contained 0.48 g SID lysine per MJ DE and SID threonine, methionine+ cysteine, isoleucine and tryptophan at 68%, 65%, 58% and18% of SID lysine and offered at 2.2kg/day from d 28 to d 110. Sow were then moved to the farrowing house and placed on a lactation diet at 3.5kg/d. The Treatment diet contained 0.55 g SID lysine/MJ DE and SID threonine, methionine+cysteine, isoleucine and tryptophan at 78%, 65%, 60% and 20% of SID lysine and offered at 2.1kg/d from d 28 to d 85 and then increased to 2.4 kg/d to d 110 d. Increasing essential amino acid levels in late gestation increased gestational weight gain (5.6 kg, P=0.004), increased total litter birth weight (1.25 kg, P=0.003), and increased the birthweight of liveborn pigs from 1.286 to 1.329 kg, (P=0.04). There was no significant effect on the total number born or born alive. Piglet performance is not available because this commercial farm practices cross-fostering. Effects of continuation of this feeding regime in the same sows during subsequent parities is currently being evaluated.


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