Study of the amino acid composition of macaroni products under the influence of different storage temperatures

2021 ◽  
pp. 147-152
Author(s):  
I.A. Tarasova ◽  
E.A. Tarasova
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Comparative Method ◽  
Exchange Chromatography ◽  
Photometric Detection ◽  
Three Samples ◽  
C 30 ◽  
Limiting Amino Acids

The article presents the studies of the amino acid composition in the samples of macaroni products by the method of chromatographic analysis. Amino acids were separated by ion exchange chromatography, reacted with ninhydrin, and their content was determined by photometric detection at a wavelength of 570 nm. Amino acid compositions of three samples of macaroni products stored at temperatures 20±2°C, 30±2°C and 40±2°C were investigated. The biological value of macaroni products proteins was determined by a comparative method for analyzing the quantitative content of amino acids with the ideal protein scale proposed by the FAO/WHO Committee. The limiting amino acids for macaroni products after 12 months of storage are valine, threonine and lysine, with the lysine content being the lowest.

Grain amino acid composition of barley (Hordeum vulgare L.) cultivars subjected to selenium doses

2017 ◽  
Vol 43 (3) ◽  
pp. 268-276 ◽  
Author(s):  
Semih Yilmaz ◽  
Ali İrfan İlbaş ◽  
Mikail Akbulut ◽  
Aysun Çetin
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Acid Content ◽  
Amino Acid Content ◽  
Sulfur Amino Acids ◽  
Hordeum Vulgare L ◽  
Barley Cultivars ◽  
Limiting Amino Acids

Abstract Background: Selenium (Se34) is an essential micronutrient for humans and animals and has growth promoting and antioxidative effects at low concentrations. Methods: Effects of various sodium selenite (Na2SeO3) doses on grain amino acid content of barley cultivars (Bülbül 89 and Çetin 2000) was investigated using ion exchange liquid chromatography. Results: Majority of the amino acids could be altered with Selenium (Se) fertilization. Grain Se content of Bülbül 89 (0.175 mg kg−1) and Çetin 2000 (0.171 mg kg−1) were similar and both displayed an increase in proteinogenic, essential, and sulfur amino acids. The response of cultivars was more pronounced for Se accumulation and amino acid content at mid dose (12.5 mg ha−1). The quantities of proteinogenic, essential and sulfur amino acids increased considerably at that dose. Se induced increase in nitrogen content might cause an increase in some of the proteins of grain and consequently can alter amino acid composition. An obvious increase in the limiting amino acids (lysine and threonine) were prominent in response to Se fertilization. Conclusion: Se treatment influence amino acid composition of barley grains; especially improve the quantity of limiting amino acids and consequently nutritional value of the grain.

AMINO ACID COMPOSITION OF THE PROTEINS OF THE MUSCLES AND ORGANS OF THE NORMAL, CASTRATED AND TESTOSTERONE TREATED GUINEA PIG

1964 ◽  
Vol 45 (4) ◽  
pp. 613-622 ◽  
Author(s):  
Charles D. Kochakian ◽  
John Hill ◽  
Giovanni Costa
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Seminal Fluid ◽  
Normal Growth ◽  
Exchange Chromatography ◽  
Seminal Vesicles ◽  
Androgen Treatment ◽  
The Individual

ABSTRACT The protein of several muscles, liver, kidney, prostate, seminal vesicles and seminal vesicle fluid of normal, castrated and testosterone propionate or testosterone treated guinea pigs was prepared by either trichloracetic or perchloric acid treatment. The extracted and defatted proteins were hydrolysed with acid and the amino acid composition determined by ion exchange chromatography. Each tissue contained all of the commonly occurring amino acids. The seminal fluid also contained several other unidentified ninhydrin reacting compounds. The quantity of each acid changed in direct proportion with the changes in weight of the tissues produced by castration or androgen treatment. The nine different muscles analysed ranged in no dependency to very great dependency on androgen for normal growth but the amino acid composition of their proteins was practically identical. The quantity of the individual amino acids of the fluid of the seminal vesicles was very different from that of the organ.

scholarly journals STUDY OF THE PEGANUM HARMALA AMINO ACID COMPOSITION GROWING IN AZERBAIJAN

2021 ◽  
pp. 121-128
Author(s):  
Tohfa Nasibova ◽  
Eldar Garaev
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Exchange Chromatography ◽  
Peganum Harmala ◽  
Plant Parts ◽  
Depth Study ◽  
The Individual ◽  
Qualitative And Quantitative Study

The aim of the research is a qualitative and quantitative study of the amino acid composition of Syrian rue (Peganum harmala, Nitrariaceae), growing in the natural conditions of the Azerbaijan Republic. After preliminary confirmation of the presence of amino acids, the plant parts were subjected to in-depth study by ion-exchange chromatography using post-column derivatization on a L-8800 amino acid analyzer (Hitachi, Ltd.). Amino acid analysis of the roots of P. harmala, conducted in the course of this study, was carried out by us for the first time. According to the results of the analysis, 18 amino acids were identified in the studied parts of P.harmala, 8 of which nonessential, 9 are essential and 3 are conditionally essential. The total amount of amino acids for the roots was 7.162%, seeds - 6.096%, and stems - 14.676%. From the individual amino acids in the underground organs of P. harmala, proline predominates (2.149%), and aspartic acid predominates in the stems and seeds (2.698% and 2.394%, respectively). The least detected amino acids are ornithine in the roots and stems (0.007% and 0.020%, respectively) and cysteine in the seeds (0.024%). Hydroxyproline was not found in the stems. At the same time, with the exception of proline, hydroxyproline, hydroxylysine and ornithine in the stems, the remaining amino acids were found to be higher than in other organs.

Amino acid composition of degradation-resistant peptides in extracellular rumen fluid of sheep

1993 ◽  
Vol 120 (1) ◽  
pp. 129-133 ◽  
Author(s):  
R. J. Wallace ◽  
C. J. Newbold ◽  
N. D. Watt ◽  
V. Buchan ◽  
D. S. Brown
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Rumen Fluid ◽  
Particulate Material ◽  
Exchange Chromatography ◽  
Supernatant Fluid ◽  
Isoleucine Leucine ◽  
Rotary Evaporation

SUMMARYRumen fluid was removed from four sheep 6 h after feeding, and the fluid was centrifuged to remove the micro-organisms. Perchloric acid (PCA) was added to the supernatant fluid to precipitate soluble proteins, which were again removed by centrifugation. The PCA extract was neutralized with KOH and the precipitate was removed by centrifugation. The supernatant fluid was hydrolysed with 6 MHC1 at 110 °C for 24 h, then dried by rotary evaporation, and the amino acid composition of each extract was analysed by ion-exchange chromatography. The recovery of amino acids was 98%, except for methionine, cysteine and tryptophan, which were destroyed. The recovery of amino acids from added Trypticase was 92% of the peptide mixture as amino acids. The free amino acid composition of extracellular rumen fluid was low and variable in both amount and composition (0·36, S.D. 0·49, μmol/ml). The concentration of amino acids released by acid hydrolysis of the PCA extract, presumed to be derived from peptides, was larger and its composition was less variable (1 ·02, S.D. 0·30, μmol/ml). Aspartic acid and histidine were enriched in peptides in comparison with the amino acids present in the feed or in rumen particulate material. Glycine and proline contents were higher in peptides that in particulate material. In contrast, the contents of isoleucine, leucine, tyrosine and phenylalanine tended to be lower in peptides than in the other materials. It was concluded that extracellular degradation-resistant peptides had a composition that was different to microbial protein and to the feed. The peptides appeared to be enriched for amino acids which previous studies with pure peptides had shown tend to make peptides more resistant to degradation.

scholarly journals The Amino Acid Composition of Keratins

1955 ◽  
Vol 8 (4) ◽  
pp. 537 ◽  
Author(s):  
DH Simmonds
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Merino Wool

The amino acid composition of 16-hr 6N HCI hydrolysates of three qualities of commercially classified wools has now been determined using the technique of Moore and Stein (1951). In this paper the results obtained on samples of Merino 70's and Corriedale 56's wool are compared with those previously reported for Merino wool of 64's quality. The overall pattern of the amino acid composition of the three wools is similar although small variations between the wools are observed with some of the amino acids.

scholarly journals Amino acid production in isolated rat liver mitochondria

1973 ◽  
Vol 134 (2) ◽  
pp. 431-436 ◽  
Author(s):  
W. Ferdinand ◽  
W. Bartley ◽  
V. Broomhead
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Lipid Hydroperoxide ◽  
Liver Mitochondria ◽  
Cysteic Acid ◽  
Rat Liver Mitochondria ◽  
Isolated Mitochondria ◽  
Selective Retention

Amino acid analyses of mitochondrial membranes are compared with the amino acid composition of whole mitochondria (Alberti, 1964) and found to be very similar except in the cystine content. The composition of the endogenous amino acids found in freshly prepared mitochondria has been established and shown to differ considerably from the amino acid composition of membranes or whole mitochondria. The amino acids produced during anaerobic incubation of mitochondria at pH7.4, on the other hand, resemble the membrane in composition, supporting the view that neutral proteinase activity is responsible for their appearance. Aerobic incubation produces a similar pattern of amino acids except that amino acids such as proline, serine, asparagine, glutamic acid and glutamine, which can be metabolically utilized under aerobic conditions, are present to a smaller extent. The presence of large relative concentrations of endogenous taurine, cysteic acid and oxidized glutathione and the accumulation of taurine during incubation is found. The selective retention of taurine and cysteic acid within the mitochondria is established. It is proposed that the first step in the degeneration of isolated mitochondria results from lipid hydroperoxide accumulation caused by the lack of glutathione reductase in isolated mitochondria.

scholarly journals AMINO ACID COMPOSITION AND ELECTROPHORETIC PROPERTIES OF HYPERTENSIN I

1955 ◽  
Vol 102 (4) ◽  
pp. 435-440 ◽  
Author(s):  
Leonard T. Skeggs ◽  
Walton H. Marsh ◽  
Joseph R. Kahn ◽  
Norman P. Shumway
Keyword(s):  
Amino Acids ◽  
Quantitative Analysis ◽  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Isoelectric Point ◽  
Column Chromatography ◽  
Isoleucine Leucine ◽  
Ion Exchange Column

A preparation of hypertensin I was purified by countercurrent distribution and was shown to migrate as a single component in starch blocks at pH 9.3 and 4.2. It had an isoelectric point of 7.7. Quantitative analysis by ion exchange column chromatography showed eight amino acids in approximately unimolar proportion: aspartic, proline, valine, isoleucine, leucine, tyrosine, phenylalanine, and arginine. There were in addition two moles of histidine.

scholarly journals WRAP-based nanoparticles for siRNA delivery: a SAR study and a comparison with lipid-based transfection reagents

2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Karidia Konate ◽  
Emilie Josse ◽  
Milana Tasic ◽  
Karima Redjatti ◽  
Gudrun Aldrian ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Gene Silencing ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Sirna Delivery ◽  
Cell Penetrating Peptides ◽  
Sirna Transfection ◽  
Arginine Residues ◽  
Sar Study

AbstractRecently, we designed novel amphipathic cell-penetrating peptides, called WRAP, able to transfer efficiently siRNA molecules into cells. In order to gain more information about the relationship between amino acid composition, nanoparticle formation and cellular internalization of these peptides composed of only three amino acids (leucine, arginine and tryptophan), we performed a structure–activity relationship (SAR) study. First, we compared our WRAP1 and WRAP5 peptides with the C6M1 peptide also composed of the same three amino acids and showing similar behaviors in siRNA transfection. Afterwards, to further define the main determinants in the WRAP activity, we synthesized 13 new WRAP analogues harboring different modifications like the number and location of leucine and arginine residues, the relative location of tryptophan residues, as well as the role of the α-helix formation upon proline insertions within the native WRAP sequence. After having compared the ability of these peptides to form peptide-based nanoparticles (PBNs) using different biophysical methods and to induce a targeted gene silencing in cells, we established the main sequential requirements of the amino acid composition of the WRAP peptide. In addition, upon measuring the WRAP-based siRNA transfection ability into cells compared to several non-peptide transfection agents available on the markets, we confirmed that WRAP peptides induced an equivalent level of targeted gene silencing but in most of the cases with lower cell toxicity as clearly shown in clonogenic assays.

Sign in / Sign up

Export Citation Format

Share Document