scholarly journals Comparative Analysis of Collagen-Containing Waste Biodegradation, Amino Acid, Peptide and Carbohydrate Composition of Hydrolysis Products

2021 ◽  
Vol 11 (23) ◽  
pp. 11511
Author(s):  
Stanislav Sukhikh ◽  
Svetlana Noskova ◽  
Svetlana Ivanova ◽  
Elena Ulrikh ◽  
Alexsander Izgaryshev ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Enzyme Preparation ◽  
Raw Materials ◽  
Collagenolytic Activity ◽  
Carbohydrate Composition ◽  
Process Duration ◽  
Amino Acid Peptide ◽  
Chondroitin Sulfates ◽  
Hydrolysis Products

This paper aimed to study the biodegradation of collagen-containing waste (pork skin) induced by collagenase and Neutrase 1.5 MG enzymes and compare the amino acid, peptide, and carbohydrate composition of hydrolysis products. It was found that the degree of biodegradation of collagen-containing raw materials (pork skin) reached 78% when using an enzyme preparation (collagenase with a concentration of 250 U/g of the substrate) at pH 7.0, 40 °C, and a 360 min process duration. It was shown that the content of peptides with a molecular weight of 6.5–14.0 kDa in the hydrolysis products (collagenase) of collagen-containing wastes was 13.4 ± 0.40%, while in the products of hydrolysis (Neutrase 1.5 MG) it was 12.8 ± 0.38%. The study found that the hydrolysis products (Neutrase 1.5 MG) of collagen-containing raw materials contain fewer hexoses, free hexosamines, and hyaluronic acid than the hydrolysis products (collagenase) of collagen-containing raw materials. The content of chondroitin sulfates is practically the same in all samples of hydrolysis products. Proteases with collagenolytic activity are widely used in industry. Recently, they have increasingly been used in pharmaceutical, food, and other industries. Collagenases are promising enzymes for the production of chondroprotectors used for the treatment of osteoarthritis.

DESIGNING BALANCED FEEDS FOR INDUSTRIAL AQUACULTURE USING PROTEIN HYDROLYSATES OF FISH BY-PASS RAW MATERIALS

Fisheries ◽  
2021 ◽  
Vol 2021 (4) ◽  
pp. 81-88
Author(s):  
Olga Mezenova ◽  
Dmitriy Pyanov ◽  
Svetlana Agafonova ◽  
Natalia Mezenova ◽  
V. Volkov
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Raw Materials ◽  
Protein Hydrolysates ◽  
Total Protein Content ◽  
Alternative Sources ◽  
Amino Acid Balance ◽  
Limiting Amino Acids ◽  
By Products

The perspective of the production of domestic compound feed for the development of industrial aquaculture in Russia is shown. Alternative sources of protein in mixed fodder for salmon and sturgeon have been investigated. The advantages of using protein hydrolysates instead of a part of fishmeal in compound feed are described. The advantages of protein hydrolysates from fish by-products are considered, the chemical composition and molecular fractional composition of sublimated protein hydrolysates obtained by enzymatic and thermal pathways from sardinella scales and ridges are studied. The presence in hydrolysates of 53.3 - 97.7% of low molecular weight peptides with a molecular weight of less than 10 kDa with a total protein content of 80.8-94.1% was established. Indicators of amino acid balance (scor) of hydrolyzates of scales and ridges of sardinella were calculated in relation to the established requirements for amino acids in salmonids. Indicators of amino acid balance (scor) of hydrolyzates of scales and ridges of sardinella were calculated in relation to the established requirements for amino acids in salmonids.It was found that the introduction of an enzymatically obtained hydrolyzate is more favorable for an increase in the content of limiting amino acids in mixed feed, and the use of sardinella scales for hydrolysis is more preferable than its ridges.

Preparation and fractionation of goat κ-casein: analysis of the glycan and peptide components

1978 ◽  
Vol 45 (2) ◽  
pp. 191-196 ◽  
Author(s):  
Francesco Addeo ◽  
Solange Soulier ◽  
Jean-Pierre Pelissier ◽  
Jean-Marc Chobert ◽  
Jean-Claude Mercier ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Deae Cellulose ◽  
Phosphate Content ◽  
Carbohydrate Composition ◽  
Neuraminic Acids ◽  
Main Fraction ◽  
Carbohydrate Contents

SummaryWhole goat κ-casein was prepared by chromatography of whole casein on hydroxyapatite. Chromatography of whole κ-casein on DEAE-cellulose separated 5 fractions. All of them were sensitive to chymosin. Their amino acid and carbohydrate composition, phosphate content and molecular weight were determined. Galactose, N-acetylgalactosamine, N-acetyl and N-glycolyl neuraminic acids were identified in whole κ-casein. It appears that goat κ-casein, like cow, buffalo and ewe κ-caseins, is composed of several fractions having identical peptide chains and differing in their carbohydrate contents. The main fraction, devoid of carbohydrate, was treated with chymosin. The para-κ-casein and caseinomacropeptide were isolated. Their amino acid composition and phosphate content were determined.

scholarly journals Obtaining and estimating the potential of protein nutraceuticals from highly mineralized collagen-containing beef raw materials

2021 ◽  
Vol 6 (1) ◽  
pp. 10-22
Author(s):  
N. Yu. Mezenova ◽  
S. V. Agafonova ◽  
O. Ya. Mezenova ◽  
L. S. Baidalinova ◽  
T. Grimm
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Raw Materials ◽  
Water Soluble ◽  
Biologically Active ◽  
Low Molecular Weight ◽  
Enzyme Preparations ◽  
Freeze Dried ◽  
Mineralized Collagen

Highly mineralized collagen-containing beef raw materials (tibia, fibula and costal bones) are a source of valuable protein nutraceuticals. They include high molecular weight proteins, oligopeptides and amino acids, which anabolic and physiological potential is used insufficiently. Protein nutraceuticals were obtained by high-temperature hydrolysis of beef raw materials in combination with enzymolysis by proteolytic enzyme preparations Alcalase 2,5 L, Protamex, Protosubtilin G3x. The water-soluble fraction of hydrolysates was studied after its separation and freeze-drying on the content of nitrogenous compounds, fats, minerals, formol-titrated nitrogen, fractional molecular composition. The mathematical dependencies of accumulation of low molecular weight products of protein hydrolysis on enzymolysis duration and doses of different enzyme preparations were obtained. The rational technological scheme of complex processing of beef raw materials with production of protein, fat and mineral-protein additives was proposed. The protein weight fraction in the freeze-dried protein hydrolysates was 69.5–89.6%. All studied protein additives contained peptides with a molecular weight of not more than 100 kDa. The content of low-molecular weight oligopeptides with a molecular weight of less than 10 kDa in the protein additives obtained by enzymatic thermal hydrolysis was more than 90%. The amino acid composition of protein additives produced by different hydrolytic methods was analyzed. Sensory and functional-technological properties of freeze-dried protein compositions were studied. The amino acid potential, high assimilability and physiological activity of protein nutraceuticals from collagen-containing beef raw materials were established. It is recommended to use them in the composition of specialized biologically active additives (BAAs) to food of the osteotropic direction in recipes of specialized and personalized products as a source of amino acids and active peptides.

scholarly journals Specialized sports nutrition products using protein hydrolysis compositions of collagen-containing fish raw materials

Vestnik MGTU ◽  
2021 ◽  
Vol 24 (4) ◽  
pp. 414-427
Author(s):  
N. Yu. Pomanenko (Mezenova) ◽  
O. Ya. Mezenova ◽  
Yu. O. Nekrasova
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Protein Content ◽  
Acid Composition ◽  
Raw Materials ◽  
Sports Nutrition ◽  
Protein Supplements ◽  
Active Peptides ◽  
Hydrolysis Of

The development of specialized sports nutrition with components of collagen-containing fish raw materials is due to the shortage of domestic products of this group, the problem of fish waste processing, scientific data on bioactive peptides of marine origin. Low-molecular active peptides and protein-mineral compositions in the form of powder and liquid dietary supplements were obtained from the scales of sardine and sardinella by methods of deep hydrolysis. During the hydrolysis of raw materials, fermentolysis was carried out with the Alcalase 2.5L enzyme, thermohydrolysis - at temperatures of 130-140 °C. The chemical composition of the scales of two fish species, the products of its hydrolysis, and the amino acid composition of its proteins have been studied. The amount of low-molecular-weight peptides in hydrolysates of sardine scales was investigated by various methods of hydrolysis. Rational methods of hydrolysis of scales - enzymatic and enzymatic-thermal - have been substantiated. They make it possible to obtain protein supplements with protein content of 83.9-85.2 % with a proportion of active peptides with a molecular weight of less than 10 kDa 91.7-98.1 %. A technology for obtaining protein supplements from fish scales has been developed, and their amino acid composition has been studied. The presence of irreplaceable and ergogenic amino acids, accompanying nitrogenous compounds, valuable in sports nutrition, was shown in the peptide supplement. An increased content of calcium, phosphorus and magnesium in the protein-mineral dietary supplement being important for the musculoskeletal tissues of an athlete has been established. On the basis of protein supplements in dry and liquid forms with the addition of beekeeping products, the technology of chewing marmalade for sports nutrition has been developed. Bioproduct "Apikolltonus" belongs to the class of gainers with a protein content of 20.5 %, a carbohydrate of 41.6 % with an amino acid value of BCAA (isoleucine : leucine : valine) 2 : 1 : 1.5. A multicomponent bar for sports nutrition has been developed using protein hydrolysates of scales, flaxseed and apple cakes, and pine nuts. The bar is functional in terms of the content of calcium and phosphorus, dietary fiber, flavonoids, and vitamin E. Recommendations for the use of new sports nutrition products are substantiated.

Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

1993 ◽  
Vol 51 ◽  
pp. 388-389
Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Vascular Tone ◽  
Cardiac Tissue ◽  
Ring Structure ◽  
Terminal Amino Acid ◽  
Amino Acid Peptide ◽  
Normal Human ◽  
Terminal Amino ◽  
The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

Isolation and Structural Charaderization of a Potent Inhibitor of Coagulation Factor Xa from the Leech Haementeria ghilianii

1989 ◽  
Vol 61 (03) ◽  
pp. 437-441 ◽  
Author(s):  
Cindra Condra ◽  
Elka Nutt ◽  
Christopher J Petroski ◽  
Ellen Simpson ◽  
P A Friedman ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Salivary Gland ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Western Blot ◽  
Potent Inhibitor ◽  
Factor Xa ◽  
Coagulation Factor ◽  
Sds Page ◽  
Bovine Factor

SummaryThe present work reports the discovery and charactenzation of an anticoagulant protein in the salivary gland of the giant bloodsucking leech, H. ghilianii, which is a specific and potent inhibitor of coagulation factor Xa. The inhibitor, purified to homogeneity, displayed subnanomolar inhibition of bovine factor Xa and had a molecular weight of approximately 15,000 as deduced by denaturing SDS-PAGE. The amino acid sequence of the first 43 residues of the H. ghilianii derived inhibitor displayed a striking homology to antistasin, the recently described subnanomolar inhibitor of factor Xa isolated from the Mexican leech, H. officinalis. Antisera prepared to antistasin cross-reacted with the H. ghilianii protein in Western Blot analysis. These data indicate that the giant Amazonian leech, H. ghilianii, and the smaller Mexican leech, H. officinalrs, have similar proteins which disrupt the normal hemostatic clotting mechanisms in their mammalian host’s blood.

Impairment of Platelet Aggregation by Echis colorata Venom Mediated by L-Amino Acid Oxidase or H2O2

1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Oxidase Activity ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Hemostatic Disorders

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.

Complete Covalent Structure of Human Platelet Factor 4

1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Disulphide Bonds ◽  
Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

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