Nothing Special   »   [go: up one dir, main page]

Virginia et al., 2016 - Google Patents

Study of HMG-CoA reductase inhibition activity of the hydrolyzed product of snakehead fish (Channa striata) skin collagen with 50 kDa collagenase from Bacillus …

Virginia et al., 2016

View PDF
Document ID
3072042026010998793
Author
Virginia A
Rachmawati H
Riani C
Retnoningrum D
Publication year
Publication venue
Scientia pharmaceutica

External Links

Snippet

Bioactive peptides produced from enzymatic hydrolysis fibrous protein have been proven to have several biological activities. Previous study showed that the hydrolysis product of snakehead fish skin collagen with 26 kDa collagenase from Bacillus licheniformis F11. 4 …
Continue reading at www.mdpi.com (PDF) (other versions)

Classifications

    • 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)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/52—Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
    • 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)
    • C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
    • 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
    • C07K14/78—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
    • C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00—Preparation of peptides or proteins
    • C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00—Preparation of peptides or proteins
    • C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
    • 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]

Similar Documents

Publication Publication Date Title
Bhagwat et al. Collagen and collagenolytic proteases: A review
JP7361021B2 (en) Recombinant collagen and elastin molecules and their uses
Kuba et al. Production of angiotensin I-converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase
Fontoura et al. Production of feather hydrolysates with antioxidant, angiotensin-I converting enzyme-and dipeptidyl peptidase-IV-inhibitory activities
Quirós et al. Stability to gastrointestinal enzymes and structure–activity relationship of β-casein-peptides with antihypertensive properties
El-Bessoumy et al. Production, isolation, and purification of L-asparaginase from Pseudomonas aeruginosa 50071 using solid-state fermentation
Ahmed et al. Application of bacterial collagenolytic proteases for the extraction of type I collagen from the skin of bigeye tuna (Thunnus obesus)
Banerjee et al. Isolation of novel bioactive regions from bovine Achilles tendon collagen having angiotensin I-converting enzyme-inhibitory properties
KR102351839B1 (en) Purification of triple helical proteins
Meshginfar et al. Physicochemical, antioxidant, calcium binding, and angiotensin converting enzyme inhibitory properties of hydrolyzed tomato seed proteins
Virginia et al. Study of HMG-CoA reductase inhibition activity of the hydrolyzed product of snakehead fish (Channa striata) skin collagen with 50 kDa collagenase from Bacillus licheniformis F11. 4
Friedrich et al. In vitro degradation of porcine skin epidermis by a fungal keratinase of Doratomyces microsporus
Roy et al. Yeast protease B‐digested skimmed milk inhibits angiotensin‐I‐converting‐enzyme activity
Pokora et al. The use of serine protease from Yarrowia lipolytica yeast in the production of biopeptides from denatured egg white proteins
Nishimura et al. Characterization of proteases activities in Ficus carica cultivars
US11447780B2 (en) Preparation of wheat cysteine protease triticain-alpha produced in soluble form and method of producing same
Yuliatmo et al. Increasing of angiotensin converting enzyme inhibitory derived from Indonesian native chicken leg protein using Bacillus cereus protease enzyme.
Ilie et al. Free radical scavenging, redox balance and wound healing activity of bioactive peptides derived from proteinase K-assisted hydrolysis of Hypophthalmichthys molitrix skin collagen
Hakim et al. Angiotensin-converting enzyme inhibitor activity of peptides derived from Kacang goat skin collagen through thermolysin hydrolysis
JP2015218142A (en) Collagen peptide
El-Sayed et al. Purification and characterization of L-amino acid oxidase from the solid-state grown cultures of Aspergillus oryzae ASH
JP2022102874A (en) Elastin peptide
Chakraborty et al. Purification and characterization of a streptomycete collagenase
Jamhari et al. Comparative study on angiotensin converting enzyme inhibitory activity of hydrolysate of meat protein of Indonesian local livestocks
Ekun et al. Antimicrobial properties and antioxidant activities of pigeon pea seed protein hydrolysates