Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Broccoli protein-derived ace and dpp-iv inhibitory peptides, preparation method and application thereof

A technology derived from DPP-IV and protein, which is applied in the field of broccoli protein-derived ACE and DPP-IV inhibitory peptides and their preparation, can solve problems such as the impact on kidney function, and achieve the effects of strong activity, simple structure, and wide application prospects

Active Publication Date: 2021-06-01
NINGBO UNIV
View PDF2 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Patients often need to take some antihypertensive and hypoglycemic drugs, but these drugs will produce many side effects, especially have a great impact on kidney function

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Broccoli protein-derived ace and dpp-iv inhibitory peptides, preparation method and application thereof
  • Broccoli protein-derived ace and dpp-iv inhibitory peptides, preparation method and application thereof
  • Broccoli protein-derived ace and dpp-iv inhibitory peptides, preparation method and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0044] (1) Squeeze fresh broccoli stems and leaves as raw materials, heat the obtained juice to 90°C, keep it warm for 10 minutes, centrifuge the sediment, and dry it to obtain the crude broccoli protein extract;

[0045] (2) Enzymatic preparation of polypeptide extracts from broccoli stems and leaves

[0046] Use broccoli protein crude extract as raw material, add distilled water according to the mass ratio of solid to liquid 1:20, and add Aclase alkaline protease with 2.0% broccoli protein crude extract mass under the condition of temperature 60°C and pH 8.0, and enzymatically hydrolyze for 3 hours Finally, inactivate the enzyme, cool down, centrifuge, rotate evaporate, concentrate and then freeze-dry to obtain the broccoli polypeptide extract;

[0047] (3) Ultrafiltration and gel filtration of broccoli peptide extract

[0048] The broccoli polypeptide extract was ultrafiltered with Valflow 50, and then separated with a G-15 gel column (Sephadex G-15). The elution condition...

Embodiment 2

[0055] Experimental steps include:

[0056] 1. Detection method of angiotensin-converting enzyme (ACE) inhibitory activity

[0057] Add 80uL 5mmol / L HHL (hippuryl-histidyl-leucine) (dissolved in HEPES buffer, pH8.3) and 30uL sample solutions of different concentrations (dissolved in double-distilled water) in a centrifuge tube, mix After placing in a water bath at 37°C for 5min, add 40uL 0.025U / mL ACE (dissolved in HEPES buffer, pH 8.3), incubate at 37°C for 1h, then add 150uL 1M hydrochloric acid to terminate the reaction. The blank group added hydrochloric acid while adding ACE, the control group used 30ul double distilled water instead of the sample solution, and captopril (10ng / mL) was used as a positive control. After the reaction was completed, the content of hippuric acid (HA) in the sample was detected by RP-HPLC, and the content of hippuric acid in the detection sample was calculated by comparing with the peak area of ​​the standard hippuric acid. Chromatographic co...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

PropertyMeasurementUnit
volume ratioaaaaaaaaaa
volume ratioaaaaaaaaaa
volume ratioaaaaaaaaaa
Login to View More

Abstract

The invention discloses a series of ACE and DPP‑IV inhibitory peptides derived from broccoli protein and their preparation methods and applications. The amino acid sequences of the peptides are the following six types: Peptide 1: Leu‑Pro‑Gly‑Val‑Leu‑Pro‑Pro Val‑Ala; Peptide 2: Tyr‑Leu‑Tyr‑Ser‑Pro‑Ala‑Tyr; Peptide 3: Leu‑Pro‑Gly‑Val‑Leu‑Pro; Peptide 4: Val‑Pro‑Leu‑Val‑Met; Peptide 5: Leu‑Pro‑Gly‑Val; Peptide 6: Tyr‑Leu‑Tyr‑Ser‑Pro‑Ala; this peptide has both ACE and DPP‑IV inhibitory functions, and can be used in the preparation of health food or medicine. The ACE and DPP-IV inhibitory peptide derived from broccoli protein of the present invention has both ACE and DPP-IV inhibitory functions, and is very suitable for preparing auxiliary blood pressure lowering foods and blood pressure lowering medicines.

Description

technical field [0001] The invention relates to the field of polypeptides derived from broccoli protein, in particular to ACE and DPP-IV inhibitory peptides derived from broccoli protein and its preparation method and application. Background technique [0002] Broccoli is a vegetable crop with strong seasonality. The flower bulbs are harvested from November to March of the next year. The stems and leaves of the plants after the flower bulbs are harvested are piled up in the field as waste, which is seriously Pollution of the environment in the main broccoli producing areas. According to calculations, the yield of broccoli stems and leaves is generally 2.5-3 tons per mu. Only based on the 70,000-mu broccoli planting base in Shangpan Town, Linhai City, Zhejiang Province, the total amount can reach 175,000-210,000 tons. Excessive accumulation of broccoli stems and leaves seriously affects the virtuous cycle of the ecological environment of the soil plowing layer. The nitrogen ...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Patents(China)
IPC IPC(8): C07K7/06C07K5/103C07K1/36C07K1/34C07K1/16C12P21/06A23L33/18A61K38/08A61K38/07A61P9/12
CPCA23V2002/00A61K38/00A23L33/18A61P9/12C07K1/16C07K1/34C07K1/36C07K5/101C07K7/06C12P21/06A23V2200/326
Inventor 党亚丽高新昌周亭屹郝丽
Owner NINGBO UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products