Characterisation of antioxidant peptides from enzymatic hydrolysate of golden melon seeds protein. (30th July 2021)
- Record Type:
- Journal Article
- Title:
- Characterisation of antioxidant peptides from enzymatic hydrolysate of golden melon seeds protein. (30th July 2021)
- Main Title:
- Characterisation of antioxidant peptides from enzymatic hydrolysate of golden melon seeds protein
- Authors:
- Chen, Lihua
Li, Dongna
Zhu, Chuchu
Rong, Yuzhi
Zeng, Wenhua - Abstract:
- Summary: The purpose of present research was to study novel antioxidant peptides from Golden melon seeds. Alkaline protease was used to hydrolyse the Golden melon seeds protein to obtain the hydrolysed peptides. These antioxidant peptides were purified and identified by ultrafiltration, gel filtration chromatography and RP‐HPLC‐ESI‐MS/MS. Results showed that the peptide fraction (GMSHp3) with molecular weight (MW) <3 kDa obtained by ultrafiltration had the highest antioxidant capacity. This fraction was further purified via gel filtration chromatography into six sub‐fractions, among which GMSHp3‐3 exhibited the highest hydroxyl radical scavenging effect. Fraction GMSHp3‐3 was further purified via RP‐HPLC‐ESI‐MS/MS and sequenced as six potential antioxidant peptides with amino acids sequences of RMSFPVMCRN, LMRVLAQLG, ALAPLVALPAA, LVGKPAPD, LPAAHKA and AHAAGYGG, among which LMRVLAQLG, LPAAHKA and AHAAGYGG possessed effective ferric reducing power. These results indicated that novel antioxidant peptides from golden melon seeds protein hydrolysates might be potential antioxidant source of functional foods or nutraceutical supplements. Abstract : Golden melon seeds protein hydrolysate was produced under the condition of alcalase, and the novel antioxidant peptides were isolated and purified by ultrafiltration, gel filtration chromatography, and RP‐HPLC‐ESI‐MS/MS. Then the identified peptides were further synthesized, their antioxidant capacities and secondary structures wereSummary: The purpose of present research was to study novel antioxidant peptides from Golden melon seeds. Alkaline protease was used to hydrolyse the Golden melon seeds protein to obtain the hydrolysed peptides. These antioxidant peptides were purified and identified by ultrafiltration, gel filtration chromatography and RP‐HPLC‐ESI‐MS/MS. Results showed that the peptide fraction (GMSHp3) with molecular weight (MW) <3 kDa obtained by ultrafiltration had the highest antioxidant capacity. This fraction was further purified via gel filtration chromatography into six sub‐fractions, among which GMSHp3‐3 exhibited the highest hydroxyl radical scavenging effect. Fraction GMSHp3‐3 was further purified via RP‐HPLC‐ESI‐MS/MS and sequenced as six potential antioxidant peptides with amino acids sequences of RMSFPVMCRN, LMRVLAQLG, ALAPLVALPAA, LVGKPAPD, LPAAHKA and AHAAGYGG, among which LMRVLAQLG, LPAAHKA and AHAAGYGG possessed effective ferric reducing power. These results indicated that novel antioxidant peptides from golden melon seeds protein hydrolysates might be potential antioxidant source of functional foods or nutraceutical supplements. Abstract : Golden melon seeds protein hydrolysate was produced under the condition of alcalase, and the novel antioxidant peptides were isolated and purified by ultrafiltration, gel filtration chromatography, and RP‐HPLC‐ESI‐MS/MS. Then the identified peptides were further synthesized, their antioxidant capacities and secondary structures were analyzed by ferric reducing power and FT‐IR spectroscopy. … (more)
- Is Part Of:
- International journal of food science & technology. Volume 56:Number 11(2021)
- Journal:
- International journal of food science & technology
- Issue:
- Volume 56:Number 11(2021)
- Issue Display:
- Volume 56, Issue 11 (2021)
- Year:
- 2021
- Volume:
- 56
- Issue:
- 11
- Issue Sort Value:
- 2021-0056-0011-0000
- Page Start:
- 5904
- Page End:
- 5912
- Publication Date:
- 2021-07-30
- Subjects:
- Amino acids sequence -- Antioxidant peptide -- Enzymatic hydrolysate -- Golden melon seeds -- Hydroxyl radicals
Food industry and trade -- Periodicals
664 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=ifs&close=1996#C1996 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/ijfs.15250 ↗
- Languages:
- English
- ISSNs:
- 0950-5423
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4542.253200
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 19963.xml