Isolation and identification of the angiotensin-I converting enzyme (ACE) inhibitory peptides derived from cottonseed protein: optimization of hydrolysis conditions. Issue 1 (1st January 2019)
- Record Type:
- Journal Article
- Title:
- Isolation and identification of the angiotensin-I converting enzyme (ACE) inhibitory peptides derived from cottonseed protein: optimization of hydrolysis conditions. Issue 1 (1st January 2019)
- Main Title:
- Isolation and identification of the angiotensin-I converting enzyme (ACE) inhibitory peptides derived from cottonseed protein: optimization of hydrolysis conditions
- Authors:
- Gao, Dandan
Zhang, Fumei
Ma, Zhongren
Chen, Shien
Ding, Gongtao
Tian, Xiaojing
Feng, Ruofei - Abstract:
- ABSTRACT: Peptides derived from food proteins have exhibited significant antihypertensive effects without side effects. In this study, the cottonseed protein was hydrolyzed by papain for preparing peptide with angiotensin I converting enzyme (ACE) inhibitory activity. The influence of hydrolysis temperature (33°C, 40°C, and 47°C), pH (6.5, 7.0, and 7.5), and enzyme to substrate (E/S) ratio (0.9%, 1.2%, and 1.5%) on the degree of hydrolysis (DH) and ACE-inhibitory activity were analyzed. The hydrolysis conditions were further optimized by central composite design (CCD) and response surface methodology (RSM). The DH of cottonseed protein and ACE inhibitory rate of hydrolysates reached 25.7% and 88.2%, respectively, under the optimal hydrolysis conditions (hydrolysis temperature 39°C, pH 7.5, and E/S ratio 1.04%). We further separated the cottonseed protein hydrolysates (CPH) using a combined strategy of ultrafiltration membrane bioreactor system, sephadex G-25 gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC). An ACE inhibitory peptide, named as FII-2-P, with ACE inhibitory IC50 value of 46.7 μg/mL, was obtained. MALDI-TOF-TOF mass spectrometry analysis revealed that the molecular weight of FII-2-P was 763.4 Da and its amino acids sequence was Phe-Pro-Ala-Ile-Gly-Met-Lys. These results demonstrated that the cottonseed protein is a potential source of ACE inhibitory ingredients to be used in the development of functional foods.
- Is Part Of:
- International journal of food properties. Volume 22:Issue 1(2019)
- Journal:
- International journal of food properties
- Issue:
- Volume 22:Issue 1(2019)
- Issue Display:
- Volume 22, Issue 1 (2019)
- Year:
- 2019
- Volume:
- 22
- Issue:
- 1
- Issue Sort Value:
- 2019-0022-0001-0000
- Page Start:
- 1296
- Page End:
- 1309
- Publication Date:
- 2019-01-01
- Subjects:
- Cottonseed protein -- hydrolysis -- ACE inhibitory peptides -- purification and identification -- response surface methodology
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664.0705 - Journal URLs:
- http://www.tandfonline.com/toc/ljfp20/current ↗
http://www.tandfonline.com/ ↗ - DOI:
- 10.1080/10942912.2019.1640735 ↗
- Languages:
- English
- ISSNs:
- 1094-2912
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4542.253100
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 12729.xml