scholarly journals Swim Bladder of Farmed Totoaba macdonaldi: A Source of Value-Added Collagen

2021 ◽  
Author(s):  
Honorio Cruz-López ◽  
Sergio Rodríguez-Morales ◽  
Luis M Enríquez ◽  
Luis Jesús Villarreal-Gómez ◽  
Conal True ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Type I Collagen ◽  
Type I ◽  
Swim Bladder ◽  
High Quality ◽  
Totoaba Macdonaldi ◽  
Quality Type

Abstract PurposeFinding strategies to use swim bladder of farmed totoaba (Totoaba macdonaldi) is of utmost need to reduce waste. Fish swim bladders are rich in collagen; hence, extracting collagen is a promising alternative with benefits for aquaculture of totoaba and the environment.MethodsThe elemental biochemical composition of totoaba swim bladders, including proximate composition and amino acid composition were determined. Acid-enzyme solubilisation (PSC) was used to extract collagen from swim bladders and its characteristics were analyzed. The alcalase and papain were used for the preparation of collagen hydrolysates.ResultsSwim bladders contained 95% protein, 2.4% fat, and 0.8% ash (dry basis). The essential amino acids content was low, but the functional amino acids content was high. The PSC yield was high, 68% (dry weight). The amino acid composition profile, electrophoretic pattern, and structural integrity analyses of the isolated collagen suggested it is typical type-I collagen with high purity. The denaturalization temperature was 34.5 °C, probably attributable to the imino acid content (205 residues/1000 residues). Papain-hydrolysates (<3 kDa) of this collagen exhibited higher radical scavenging activity than Alcalase-hydrolysates.ConclusionsSwim bladder from farmed totoaba is an ideal raw material for producing high-quality type-I collagen and a viable alternative to conventional collagen sources.Statement of NoveltyTo our knowledge, this paper is the first to examine the composition and characteristics of collagen of swim bladder from Totoaba macdonaldi. Although the processing currently wastes bladders, this study showed that they could be a potential source for producing high-quality type-I collagen.

scholarly journals Study of amino acid composition of filling for extruded grain crops

2021 ◽  
pp. 90-94
Author(s):  
U. Ch. Сhomanov ◽  
G. E. Zhumalieva ◽  
M. Ch Tultabayev ◽  
G. S. Aktokalova ◽  
R. K. Kassimbek ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Shelf Life ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Essential Amino Acids ◽  
The Body ◽  
High Quality ◽  
Grain Crops ◽  
Grain Products

In this paper, the amino acid composition of protein filling for extruded grain products is studied. According to research, essential amino acids make up more than 1/3 of all amino acids, which means that the protein filling is of high quality. The article considers covering the daily requirement of amino acids of the body with protein filling. It was found that the protein filling contains a rich amino acid composition, and allows you to get extruded grain products with a long shelf life.

scholarly journals The Macroheterogeneity of Type I Tyrosine-rich Proteins of Merino Wool

1974 ◽  
Vol 27 (6) ◽  
pp. 617 ◽  
Author(s):  
J M Gillespie ◽  
MJ Frenkel
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Quaternary Ammonium ◽  
Deae Cellulose ◽  
Type I ◽  
Merino Wool ◽  
Poor Family ◽  
Tyrosine Content

The cystine-poor family of tyrosine-rich proteins of wool as their S-carboxymethyl derivatives has been shown by chromatography on quaternary ammonium ethylcellulose (QAE-cellulose) at pH 10� 5 to consist of 10 groups of proteins which span a threefold range of tyrosine content and vary in many other amino acids, particularly S-carboxymethylcysteine. Electrophoresis at pH 8�9 revealed that most fractions contain two or more components and by further chromatography of five of these groups at pH 8�3 on DEAE-cellulose 10 components have been isolated. The amino acid composition suggests that the components within each QAE-cellulose group are very closely related.

scholarly journals Differences in the amino acid composition of the breast muscle of wild and farmed pheasants

2012 ◽  
Vol 30 (No. 4) ◽  
pp. 309-313 ◽  
Author(s):  
A. Brudnicki ◽  
A. Kułakowska ◽  
D. Pietruszyńska ◽  
M. Łożyca-Kapłon ◽  
J. Wach
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Nutritional Value ◽  
Amino Acid Profile ◽  
Breast Muscle ◽  
High Quality ◽  
Nutritional Values ◽  
Biological Value

Numerous studies show the slaughter yield and also basic chemical composition of pheasant meat. The results reveal a higher biological value of the meat of pheasants which were fed naturally, in comparison to the meat of pheasants fed with commercial mixtures. In many countries, the pheasant is selected with the aim of producing high quality meat with very desirable nutritional values. There are only few publications on amino acid composition of pheasant meat. The knowledge of amino acid composition of pheasant meat can be used to determine its potential nutritional value. The amino acid compositions were compared of the meats of wild and farm pheasants. In the study, the following amino acids were determined: Asp, Thr, Ser, Glu, Pro, Gly, Ala, Val, Ile, Leu, Tyr, Phe, His, Lys, Arg. An improved amino acid profile was found in the breast muscle of pheasants kept at the farm in comparison with that of wild pheasants. &nbsp;

scholarly journals Economical Evolution: Microbes Reduce the Synthetic Cost of Extracellular Proteins

mBio ◽  
2010 ◽  
Vol 1 (3) ◽  
Author(s):  
Daniel R. Smith ◽  
Matthew R. Chapman
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Pseudomonas Syringae ◽  
Extracellular Proteins ◽  
Compositional Bias ◽  
Type I ◽  
Content Type ◽  
Wide Range

ABSTRACT Protein evolution is not simply a race toward improved function. Because organisms compete for limited resources, fitness is also affected by the relative economy of an organism’s proteome. Indeed, many abundant proteins contain relatively high percentages of amino acids that are metabolically less taxing for the cell to make, thus reducing cellular cost. However, not all abundant proteins are economical, and many economical proteins are not particularly abundant. Here we examined protein composition and found that the relative synthetic cost of amino acids constrains the composition of microbial extracellular proteins. In Escherichia coli, extracellular proteins contain, on average, fewer energetically expensive amino acids independent of their abundance, length, function, or structure. Economic pressures have strategically shaped the amino acid composition of multicomponent surface appendages, such as flagella, curli, and type I pili, and extracellular enzymes, including type III effector proteins and secreted serine proteases. Furthermore, in silico analysis of Pseudomonas syringae, Mycobacterium tuberculosis, Saccharomyces cerevisiae, and over 25 other microbes spanning a wide range of GC content revealed a broad bias toward more economical amino acids in extracellular proteins. The synthesis of any protein, especially those rich in expensive aromatic amino acids, represents a significant investment. Because extracellular proteins are lost to the environment and not recycled like other cellular proteins, they present a greater burden on the cell, as their amino acids cannot be reutilized during translation. We hypothesize that evolution has optimized extracellular proteins to reduce their synthetic burden on the cell. IMPORTANCE Microbes secrete proteins to perform essential interactions with their environment, such as motility, pathogenesis, biofilm formation, and resource acquisition. However, because microbes generally lack protein import systems, secretion is often a one-way street. Consequently, secreted proteins are less likely to be recycled by the cell due to environmental loss. We demonstrate that evolution has in turn selected these extracellular proteins for increased economy at the level of their amino acid composition. Compared to their cellular counterparts, extracellular proteins have fewer synthetically expensive amino acids and more inexpensive amino acids. The resulting bias lessens the loss of cellular resources due to secretion. Furthermore, this economical bias was observed regardless of the abundance, length, structure, or function of extracellular proteins. Thus, it appears that economy may address the compositional bias seen in many extracellular proteins and deliver further insight into the forces driving their evolution.

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.

scholarly journals Features of сalibration еequations for IR scanners in determining the amino acid composition of soy proteins

2020 ◽  
Author(s):  
С.Е. НИЗКИЙ ◽  
Г.А. КОДИРОВА ◽  
Г.В. КУБАНКОВА
Keyword(s):  
Amino Acids ◽  
Liquid Chromatography ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
High Performance ◽  
Near Infrared ◽  
Soybean Proteins ◽  
Calibration Equation ◽  
Calibration Equations

Из 20 аминокислот, входящих в состав растительных белков, 17 лучше всего определяются с помощью высокоэффективной жидкостной хроматографии. Но эта технология затратна по времени, в том числе из-за подготовки проб, что делает ее малопригодной при проведении массовых анализов, например при оценке селекционного материала. В этом случае наиболее приемлемы технологии, основанные на сканировании в ближнем инфракрасном диапазоне излучения. Несмотря на то что ИК-сканеры способны по одному калибровочному уравнению выявлять большое количество компонентов, необходима постоянная коррекция при определении состава аминокислот и приведении его в процентное соотношение. В статье рассматриваются варианты создания калибровочных уравнений для расчета аминокислотного состава белков сои с помощью компьютерных программ (Nir 42, ISI), обеспечивающих работу ИК-сканеров типа NIR-4250 или FOSS NIRSystem 5000. Установлено, что при создании калибровочных уравнений содержание каждой аминокислоты наиболее корректно выражать в абсолютных единицах (г на 100 г белка), а не относительных (%). 17 of the 20 amino acids, included in the composition of plant proteins, are most effectively determined using liquid chromatography. The technology of high-performance liquid chromatography is to a certain extent costly in time, among other things because of sample preparation that makes it unsuitable for mass analysis, for example, when evaluating a breeding material. In this case, the technology based on scanning in the near infrared radiation band are the most acceptable. Despite the fact that IR scanners are able to determine a sufficiently large number of components on the basis of one calibration equation, a constant correction is required when determining the composition of amino acids and reducing it to a percentage ratio. The options for creating calibration equations for determining the amino acid composition of soybean proteins for computer programs (Nir 42, ISI), which provide the operation of IR scanners, such as NIR-4250 or FOSS NIRSystem 5000 are considered in the article. It was found that when creating calibration equations, it is most correct to set for each amino acid its mass content (g per 100 g of protein), and not the relative portion (in %).

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