[go: up one dir, main page]

Bhadkaria et al., 2023 - Google Patents

Peptide fraction from moth bean (Vigna aconitifolia (Jacq.)) seed protein hydrolysate demonstrates multifunctional characteristics

Bhadkaria et al., 2023

Document ID
9816116117494663116
Author
Bhadkaria A
Narvekar D
Kanekar S
Devasya R
Srivastava N
Bhagyawant S
Publication year
Publication venue
Process Biochemistry

External Links

Snippet

Present study ascribe multifunctional characterstics of moth bean bioactive peptides obtained by enzymatic hydrolysis of seed proteins. Alcalase derived protein hydrolysates were further subjected to fractionation by ultrafiltration and gel filtration chromatography …
Continue reading at www.sciencedirect.com (other versions)

Classifications

    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/43—Enzymes; Proenzymes; Derivatives thereof
    • A61K38/46—Hydrolases (3)
    • A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
    • A61K38/4813—Exopeptidases (3.4.11. to 3.4.19)
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/168—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K36/00—Medicinal preparations of undetermined constitution containing material from algae, lichens, fungi or plants, or derivatives thereof, e.g. traditional herbal medicines
    • A61K36/18—Magnoliophyta (angiosperms)
    • A61K36/185—Magnoliopsida (dicotyledons)
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • A61K38/39—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin, cold insoluble globulin [CIG]
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)

Similar Documents

Publication Publication Date Title
Clemente et al. The cytotoxic effect of Bowman–Birk isoinhibitors, IBB1 and IBBD2, from soybean (Glycine max) on HT29 human colorectal cancer cells is related to their intrinsic ability to inhibit serine proteases
Wang et al. Preparation and identification of antioxidant peptides from cottonseed proteins
Fuentes et al. Sequential alcalase and flavourzyme treatment for preparation of α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides from oat protein
Wang et al. Preparation of bioactive peptides with antidiabetic, antihypertensive, and antioxidant activities and identification of α‐glucosidase inhibitory peptides from soy protein
Zheng et al. Isolation of novel ACE‐inhibitory peptide from naked oat globulin hydrolysates in silico approach: Molecular docking, in vivo antihypertension and effects on renin and intracellular endothelin‐1
Karimi et al. Fractionation of hydrolysate from corn germ protein by ultrafiltration: In vitro antidiabetic and antioxidant activity
Cheung et al. Angiotensin-I converting enzyme inhibitory activity of hydrolysates from oat (Avena sativa) proteins by in silico and in vitro analyses
Fitzgerald et al. Isolation and characterization of bioactive pro-peptides with in vitro renin inhibitory activities from the macroalga Palmaria palmata
Wang et al. Dipeptidyl peptidase IV inhibitory peptides derived from oat (Avena sativa L.), buckwheat (Fagopyrum esculentum), and highland barley (Hordeum vulgare trifurcatum (L.) Trofim) proteins
Hu et al. Antioxidant and anti-inflammatory potential of peptides derived from in vitro gastrointestinal digestion of germinated and heat-treated foxtail millet (Setaria italica) proteins
Jiang et al. Evaluation of antioxidant peptides generated from Jiuzao (residue after Baijiu distillation) protein hydrolysates and their effect of enhancing healthy value of Chinese Baijiu
Losso The biochemical and functional food properties of the Bowman-Birk inhibitor
Ciau‐Solís et al. In vitro renin–angiotensin system inhibition and in vivo antihypertensive activity of peptide fractions from lima bean (Phaseolus lunatus L.)
Luo et al. Isolation and identification of antioxidant peptides from tartary buckwheat albumin (Fagopyrum tataricum Gaertn.) and their antioxidant activities
O'Keeffe et al. Identification of angiotensin converting enzyme inhibitory and antioxidant peptides in a whey protein concentrate hydrolysate produced at semi‐pilot scale
Bhadkaria et al. Peptide fraction from moth bean (Vigna aconitifolia (Jacq.)) seed protein hydrolysate demonstrates multifunctional characteristics
Gu et al. Identification and characterization of two novel α-glucosidase inhibitory peptides from almond (Armeniaca sibirica) oil manufacture residue
US20080081035A1 (en) Therapeutic protease compositions
Olagunju et al. Thermoase‐hydrolysed pigeon pea protein and its membrane fractions possess in vitro bioactive properties (antioxidative, antihypertensive, and antidiabetic)
Kuerban et al. Identification, protein antiglycation, antioxidant, antiproliferative, and molecular docking of novel bioactive peptides produced from hydrolysis of Lens culinaris
Bhadkaria et al. Purification, molecular docking and in vivo analyses of novel angiotensin-converting enzyme inhibitory peptides from protein hydrolysate of moth bean (Vigna aconitifolia (Jacq.) Màrechal) seeds
Karnchanatat et al. Zingipain, a cysteine protease from Zingiber ottensii Valeton rhizomes with antiproliferative activities against fungi and human malignant cell lines
Zhu et al. Antioxidant function and application of plant-derived peptides
Ding et al. Identification and characterization of dipeptidyl peptidase IV inhibitory peptides from wheat gluten proteins
Madadlou Food proteins are a potential resource for mining cathepsin L inhibitory drugs to combat SARS-CoV-2