Antioxidant and Hypolipidemic Potential of Peptides from Broccoli Stems and Leaves

To isolate bioactive broccoli peptides, crude proteins were flocculated from heated juice of broccoli stems and leaves and then hydrolyzed by proteases. Different proteases yielded different peptides with a significant effect on the bio-activities of broccoli peptides. Antioxidant activity of the broccoli peptides was investigated by measuring their DPPH (1,1-diphenyl-2-picrylhydrazyl) radicals scavenging action in comparison to native antioxidants, reduced glutathione (GSH) and soybean peptides. Broccoli peptides (obtained by Neutrase® hydrolysis) at 5.0 mg/mL exhibited 72.8% of radicals scavenging rates, resembling GSH at 1.0 mg/mL (72.1%), and was 2.8 times than that of soybean peptides at 5.0 mg/mL (25.7%). Subsequently, the hypolipidemic activities were measured by oral gastric gavage of broccoli peptides in hyperlipemic golden hamster. Treatment with broccoli peptides (obtained by papain hydrolysis) significantly decreased the serum TC and LDL-C levels (P < 0.01) in experimental rats. The constitution of amino acid and the distribution of molecular weight analysis showed broccoli peptides contained sixteen amino acids and a great percentage of low molecular weight peptides (<1 kDa, 77.67%). By analyzing the amino acid compositions and bio-activities, our results indicate the high nutritive value and possible applications of broccoli peptides for human health.

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Trans-tegumental absorption of L-alanine and L-leucine by a monogenean, Diclidophora merlangi

Parasitology ◽

10.1017/s0031182000047363 ◽

1978 ◽

Vol 76 (1) ◽

pp. 29-37 ◽

Cited By ~ 21

Author(s):

D. W. Halton

Keyword(s):

Amino Acids ◽

Molecular Weight ◽

Amino Acid ◽

Sea Water ◽

Low Molecular Weight ◽

Acid Uptake ◽

Neutral Amino Acids ◽

Freeze Dried ◽

Significant Difference

SummaryAn in vitro investigation has been made of the relative roles of the gut and tegument in the absorption of the neutral amino acids L-alanine and L-leucine by a marine fish-gill parasite, Diclidophora merlangi. The use of ligatures to preclude oral ingestion of trace-labelled medium has proved inadequate, invariably damaging the tegument, as revealed by stereoscan electron microscopy, and resulting in artifactual levels of absorption. Three alternative procedures have given consistently reliable data on the route of entry of low molecular weight substrates. (1) Ultrastructural examination of worms previously incubated in electron-dense cationic tracers has shown that, in vitro, there is no oral intake of sea water. (2) The suspending of worms in trace-labelled medium with the mouth out of the medium and comparing amino acid uptake with that of worms totally immersed in medium has revealed no statistically significant difference in the absorption levels. (3) Application of section (freeze-dried) auto-radiography to detect diffusible isotope has demonstrated directly transtegumental absorption of a neutral amino acid. It is concluded from these experiments that Diclidophora has a tegumental transport system for absorbing certain neutral amino acids, and whilst, clearly, the worm is sanguinivorous and digests blood in a well-developed gut, it may also be capable of supplementing this diet with low molecular weight organic nutrient absorbed directly from sea water via the tegument.

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Discussion: Amino-acid activation by individual enzymes

Proceedings of the Royal Society of London Series B Biological Sciences ◽

10.1098/rspb.1958.0079 ◽

1958 ◽

Vol 149 (936) ◽

pp. 401-402

Keyword(s):

Amino Acids ◽

Molecular Weight ◽

Amino Acid ◽

Distribution Pattern ◽

Mammary Tissue ◽

Low Molecular Weight ◽

Major Protein ◽

Acid Activation ◽

Amino Acid Activation ◽

Interesting Paper

I should like to comment on one aspect of Dr Gutfreund’s interesting paper. As he mentioned, we have found evidence that amino acids, after becoming enzymically activated by ATP through the formation of an enzyme-bound amino acyladenylate compound, are transferred to a low molecular weight RNA which, by accident or design, resides in the same crude activating enzyme fraction. It is gratifying that Dr Gutfreund has found a distribution pattern of amino acids on this RNA which roughly agrees with the pattern in the major protein products of mammary tissue. He points out, however, that there is no such correlation when one looks at the pattern of amino-acid activation. Indeed, because of this anomaly, some workers have devised theories of activation involving transacylation steps to account for activation of those amino acids for which an enzyme has not been found. Dr Gutfreund implies that there is much confusion and mystery here, and even suggests that the specificity of activation might be accounted for by soluble RNA , rather than by individual enzymes.

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The structure of a glycopeptide isolated from the yeast cell wall

Biochemical Journal ◽

10.1042/bj1090419 ◽

1968 ◽

Vol 109 (3) ◽

pp. 419-432 ◽

Cited By ~ 122

Author(s):

R. Sentandreu ◽

D. H. Northcote

Keyword(s):

Amino Acids ◽

Molecular Weight ◽

Cell Wall ◽

Amino Acid ◽

Yeast Cell ◽

Aspartic Acid ◽

Yeast Cell Wall ◽

Low Molecular Weight ◽

Elimination Reaction ◽

Sephadex Column

1. Glycopeptides containing mannose were extracted from isolated yeast cell walls by ethylenediamine and purified by treatment with Pronase and fractionation on a Sephadex column. 2. A glycopeptide that appeared homogeneous on electrophoresis and ultracentrifugation had a molecular weight of 76000, and contained a high-molecular-weight mannan and approx. 4% of amino acids. 3. The amino acid composition of the peptide was determined. It was rich in serine and threonine and also contained glucosamine. No cystine and methionine were detected. 4. The glycopeptide underwent a β-elimination reaction when treated with dilute alkali at low temperatures. The reaction resulted in the release of mannose, mannose disaccharides and possibly other low-molecular-weight mannose oligosaccharides. During the β-elimination reaction the dehydro derivatives of serine and threonine were formed. One of the linkages between carbohydrate and amino acids in the glycopeptide is an O-mannosyl bond from mannose and mannose oligosaccharides to serine and threonine. 5. After the β-elimination reaction the bulk of the mannose in the form of the large mannan component was still covalently linked to the peptide. This polysaccharide was therefore attached to the amino acids by a linkage different from the O-mannosyl bonds to serine and threonine that attach the low-molecular-weight sugars. 6. Mannan was prepared from the glycopeptide and from the yeast cell wall by treatment of the fractions with hot solutions of alkali. The mannan contained aspartic acid and glucosamine and some other amino acids. The aspartic acid and glucosamine were present in equimolar amounts; the aspartic acid was the only amino acid present in an amount equivalent to that of glucosamine. Thus there is the possibility of a linkage between the mannan and the peptide via glucosamine and aspartic acid. 7. Mannose 6-phosphate was shown to be part of the mannan structure. Information about the structure of the mannan and the linkage of the glucosamine was obtained by periodate oxidation studies. 8. The glucosamine present in the glycopeptide could not be released by treatment with an enzyme preparation obtained from the gut of Helix pomatia. This enzyme released glucosamine from the intact cell wall. Thus there are probably at least two polymers containing glucosamine in the cell wall. 9. The biosynthesis of the mannan polymer in the yeast cell wall is discussed with regard to the two types of carbohydrate–amino acid linkages found in the glycoprotein.

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Studien über Wespengift, I Niedermolekulare Bestandteile des Giftblasenextraktes von Paravespula vulgaris / Studies on Wasp Venom, I Low Molecular Weight Constituents of Venom Sac Extracts from Paravespula vulgaris

Zeitschrift für Naturforschung B ◽

10.1515/znb-1981-0621 ◽

1981 ◽

Vol 36 (6) ◽

pp. 757-762 ◽

Cited By ~ 2

Author(s):

Hartmut Klein ◽

Wittko Francke ◽

Wilfried A. König

Keyword(s):

Mass Spectrometry ◽

Amino Acids ◽

Fatty Acids ◽

Molecular Weight ◽

Gas Chromatography ◽

Acetic Acid ◽

Quantitative Analysis ◽

Amino Acid ◽

Low Molecular Weight ◽

Wasp Venom

Abstract Low molecular weight constituents of 3400 venom sacs of Paravespula vulgaris were extracted with water, diluted acetic acid, and methanol. After conversion to volatile derivatives carbohydrates, amino acids, fatty acids, other constituents of phospho lipids, and biogenic amines were identified by gas chromatography and mass spectrometry. Quantitative analysis was achieved for amino acids by amino acid analysis and for glucose by an enzymatic assay. Results are discussed with regard to biosynthesis of wasp toxins and phylogenetic aspects of hymenopteran venoms.

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

Theory and practice of meat processing ◽

10.21323/2414-438x-2021-6-1-10-22 ◽

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.

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Synthesis and evaluation of chiral β-amino acid-based low-molecular-weight organogelators possessing a methyl/trifluoromethyl side chain

New Journal of Chemistry ◽

10.1039/c8nj05668d ◽

2019 ◽

Vol 43 (7) ◽

pp. 2882-2887 ◽

Cited By ~ 1

Author(s):

Koichi Kodama ◽

Ryuta Kawamata ◽

Takuji Hirose

Keyword(s):

Amino Acids ◽

Molecular Weight ◽

Amino Acid ◽

Supramolecular Structures ◽

Side Chain ◽

Low Molecular Weight ◽

Side Chains ◽

Low Molecular Weight Organogelators

Impacts of side-chains and chirality of organogelators derived from β-amino acids are described with their supramolecular structures.

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Improving the nutritive characteristics of corn flakes enriched with functional components

Hemijska industrija ◽

10.2298/hemind160525012k ◽

2017 ◽

Vol 71 (6) ◽

pp. 495-502

Author(s):

Milenko Kosutic ◽

Lato Pezo ◽

Jelena Filipovic ◽

Vladimir Filipovic

Keyword(s):

Amino Acids ◽

Antioxidant Activity ◽

Amino Acid ◽

Nutritive Value ◽

Amino Acid Content ◽

Essential Amino Acids ◽

Antioxidant Potential ◽

Mean Values ◽

Corn Flakes ◽

Functional Components

This paper investigates the effects of simultaneous addition of sunflower (3, 6 or 9 g/100 g of sample) and dry residue of wild oregano (0.5 or 1 g/100 g of sample) on the essential amino acids pattern and antioxidant potential of flake products. The accepted experimental design plan was 3?4. Data point that Score and PDCAAS values in flake products increase with increasing share of sunflower. Maximum value of phenolic compounds and antioxidant activity were experienced of TPC 2.84 mg/g, DPPH 0.75 mg/ml, FRAP 1.57 mg/g with the product having maximum shares of sunflower and dry residue of wild oregano. Tukey?s HSD test showed statistically significant differences between most of the mean values of amino acids content and antioxidant activity in the observed corn flakes. The response surface method has been applied for evaluation of amino acid content and antioxidative potential of corn flakes. Sunflower in flake products positively contributed to the protein nutritive value and dry residues of wild oregano elevated antioxidant potential of flake products and also contributed to the food waste valorisation in the food industry. Corn flakes are new products with improved essential amino acid pattern, antioxidant activity and functional properties due to added dry residue of wild oregano and sunflower.

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CHARACTERIZATION OF THE PIGMENT OF MICROCOCCUS VIOLAGABRIELLAE

Canadian Journal of Microbiology ◽

10.1139/m64-086 ◽

1964 ◽

Vol 10 (5) ◽

pp. 659-675 ◽

Cited By ~ 4

Author(s):

J. N. Campbell ◽

J. L. Nichols ◽

Sheila A. Berry

Keyword(s):

Amino Acids ◽

Molecular Weight ◽

Amino Acid ◽

Cross Reactivity ◽

Low Molecular Weight ◽

Terminal Amino Acid ◽

Iron Chelate ◽

Peptide Moiety ◽

Terminal Amino

Production of the red insoluble pigment by Micrococcus violagabriellae was studied. Pigmentation was found to require oxygen and high levels of iron and to be stimulated by tryptophan alone among the amino acids. The pigment was isolated, purified, and analyzed chemically and spectrophotometrically. It was found to be similar to pulcherrimin from Candida pulcherrima. Immunological cross reactivity and analysis of derivatives confirmed the similarity between the bacterial and yeast pigments. From these data it is postulated that the pigment is an iron chelate of pulcherriminic acid with an associated low molecular weight peptide moiety with glycine as the sole N-terminal amino acid. The pigment appears to differ from that of C. pulcherrima solely with respect to this peptide and in the mode of aggregation of the molecule.

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Complete Covalent Structure of Human Platelet Factor 4

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657071 ◽

1979 ◽

Vol 42 (05) ◽

pp. 1652-1660 ◽

Cited By ~ 4

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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