Enzymatic protein hydrolysates and ultrafiltered peptide fractions from Cowpea Vigna unguiculata L bean with in vitro antidiabetic potential

Castañeda-Pérez, Eduardo; Jiménez-Morales, Karina; Quintal-Novelo, Carlos; Moo-Puc, Rosa; Chel‐Guerrero, Luis; Betancur‐Ancona, David

doi:10.1007/s13738-019-01651-0

Cited by 24 publications

(31 citation statements)

References 36 publications

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“…Legume bioactive peptides, 2–20 amino-acid residues in length, attract more and more attention [ 9 ]. When the processes undergoing in the gastrointestinal tract of mammals are simulated, cowpea seed protein extracts exposed to enzymatic hydrolysis demonstrate antioxidant, anticancer, and antidiabetic activities [ 4 , 5 , 20 , 21 ]. With extension of the seed germination time, protein extracts from germinating cowpea seeds have been observed to demonstrate increased activity.…”

Section: Resultsmentioning

confidence: 99%

Composition of Primary and Secondary Metabolite Compounds in Seeds and Pods of Asparagus Bean (Vigna unguiculata (L.) Walp.) from China

et al. 2020

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Asparagus bean immature pods and seeds are popular as food products for healthy and functional nutrition. Gas chromatography with mass spectrometry was used to compare metabolomic profiles of seeds and pods yielded by old Chinese landraces and the modern cultivars ‘Yunanskaya’ and ‘Sibirskiy razmer’. About 120 compounds were identified. The content of a majority among groups of compounds was higher in pods than in seeds. The amount of free amino acids in pods was 47 times higher, polyols and phytosterols 5 times higher, phenolics 4 times higher, and organic acids and saponins 3 times higher than in seeds. Differences were found in the relative content of compounds. Among phenolic compounds, the dominant one for seeds was protocatechuic acid, and for pods 4-hydroxycinnamic acid. Only polyols were identified in seeds, but pods additionally contained ethanolamine, phytol, and phytosphingosine. The ratio for nonsaturated/saturated fatty acids was 2.2 in seeds and 1.4 in pods. Seeds contained more stigmasterol, and pods more β-sitosterol. Aglycones of saponins were identified: cycloartenol in seeds, α- and β-amyrins in pods. Oligosaccharides dominated in both seeds and pods. Landraces manifested higher protein content in pods, while modern cultivars had pods with higher contents of organic acids, polyols, monosaccharides, and fatty acids. The results obtained confirm the high nutritional value of asparagus bean seeds and pods, and the prospects of their use in various diets.

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Section: Resultsmentioning

confidence: 99%

Composition of Primary and Secondary Metabolite Compounds in Seeds and Pods of Asparagus Bean (Vigna unguiculata (L.) Walp.) from China

et al. 2020

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“…[58] Other types A novel type of α-amylase inhibitor, made up of two subunit chains (α + β) each with a cupin structure, had led to the discovery that this cupin structure is the main α-amylase site . [77] The peptides produced by enzymatic hydrolysis usually do not have high-level structures, and it is the composition and sequence of amino acids in a peptide that determines its biological activity. Studies have shown that watermelon polypeptide fragments hydrolyzed by alkaline protease have stronger α-amylase inhibition, and their hydrolyzates exhibit noncompetitive inhibition effects on α-amylase .…”

Section: Yesmentioning

confidence: 99%

Proteinaceous α-amylase inhibitors: purification, detection methods, types and mechanisms

Zhou

Zhang

et al. 2021

International Journal of Food Properties

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α-Amylase is abundant in plants and animals. α-Amylase inhibitors can reduce endogenous α-amylase activity, playing an essential role in agricultural pest control, and preventing and treating human disease. In the agricultural field, α-Amylase inhibitors can restrict pest that relies on the starch of crops. Acarbose is an α-amylase inhibitor used to treat diabetes. Some αamylase inhibitors are represented by antinutritional factors, while others are proteinaceous. Depending on their structures and sources, researchers have divided them into seven types: The knottin-like type, the γ-thionin-like type, the cereal type, the Kunitz type, the thaumatin-like type, and the lectin-like type. This paper introduces the methods for separating, purifying, and detecting proteinaceous α-amylase inhibitors while examining the structure and inhibition mechanism of several proteinaceous α-amylase inhibitors. Finally, it explores the potential applications of α-amylase inhibitors.

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“…The kind of enzyme utilized in bioactive peptide preparations defines hydrolysate properties and the peptides that can be separated [32]. In previous studies, successive enzymatic systems, such as Alcalase ® -Flavourzyme ® (AF) and pepsin-pancreatin (PP), were used for the generating of hydrolysates and peptides which had useful effects on antidiabetics [31][32][33][34][35], antihypertension [32], hypocholesterolemia activity [36], antioxidant activity [37], and functional properties [7,38].…”

Section: Introductionmentioning

confidence: 99%

Antibacterial Peptides Produced by Alcalase from Cowpea Seed Proteins

et al. 2021

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Cowpea seed protein hydrolysates (CPH) were output from cowpea seeds applying alcalase® from Bacillus licheniformis. CPH with an elevated level of hydrolysis was fractionated by size exclusion chromatography (SEC). Both CPH and SEC-portions showed to contain antimicrobial peptides (AMPs) as they inhibited both Gram-positive bacteria, such as Listeria monocytogenes LMG10470 (L. monocytogenes), Listeria innocua. LMG11387 (L. innocua), Staphylococcus aureus ATCC25923 (S.aureus), and Streptococcus pyogenes ATCC19615 (St.pyogenes), and Gram-negative bacteria, such as Klebsiella pnemoniae ATCC43816 (K. pnemoniae), Pseudomonas aeroginosa ATCC26853 (P. aeroginosa), Escherichia coli ATCC25468) (E.coli) and Salmonella typhimurium ATCC14028 (S. typhimurium).The data exhibited that both CPH and size exclusion chromatography-fraction 1 (SEC-F1) showed high antibacterial efficiency versus almost all the assessed bacteria. The MIC of the AMPs within SEC-F1 and CPHs were (25 µg/mL) against P. aeruginosa, E.coli and St. pyogenes. However, higher MICsof approximately 100–150 µg/mL showed for both CPHs and SEC-F1 against both S. aureus and L. innocua; it was 50 µg/mL of CPH against S.aureus. The Electro-spray-ionization-mass-spectrometry (ESI-MS) of fraction (1) revealed 10 dipeptides with a molecular masses arranged from 184 Da to 364 Da and one Penta peptide with a molecular mass of approximately 659 Da inthe case of positive ions. While the negative ions showed 4 dipeptides with the molecular masses that arranged from 330 Da to 373 Da. Transmission electron microscope (TEM) demonstrated that the SEC-F1 induced changes in the bacterial cells affected. Thus, the results suggested that the hydrolysis of cowpea seed proteins by Alcalase is an uncomplicated appliance to intensify its antibacterial efficiency.

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Enzymatic protein hydrolysates and ultrafiltered peptide fractions from Cowpea Vigna unguiculata L bean with in vitro antidiabetic potential

Cited by 24 publications

References 36 publications

Composition of Primary and Secondary Metabolite Compounds in Seeds and Pods of Asparagus Bean (Vigna unguiculata (L.) Walp.) from China

Composition of Primary and Secondary Metabolite Compounds in Seeds and Pods of Asparagus Bean (Vigna unguiculata (L.) Walp.) from China

Proteinaceous α-amylase inhibitors: purification, detection methods, types and mechanisms

Antibacterial Peptides Produced by Alcalase from Cowpea Seed Proteins

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