Characterization of structural, functional and antioxidant properties and amino acid composition of pepsin-derived glutelin-1 hydrolysate from walnut processing by-products. Issue 31 (26th May 2021)
- Record Type:
- Journal Article
- Title:
- Characterization of structural, functional and antioxidant properties and amino acid composition of pepsin-derived glutelin-1 hydrolysate from walnut processing by-products. Issue 31 (26th May 2021)
- Main Title:
- Characterization of structural, functional and antioxidant properties and amino acid composition of pepsin-derived glutelin-1 hydrolysate from walnut processing by-products
- Authors:
- Wang, Jing
Wang, Guoliang
Chen, Ning
An, Feiran
Zhang, Runguang
Zhang, Yufeng
Rahman, Mati Ur
Zhang, Youlin - Abstract:
- Abstract : Pepsin-mediated hydrolysis can be used as an effective tool to improve the functional and antioxidant properties of walnut glutelin-1. Abstract : Glutelin-1 of defatted walnut meal protein (DWPG-1) was modified by pepsin enzymatic hydrolysis to improve its functional properties and antioxidant activities. The amino acid composition, structural characteristics, physicochemical and functional properties as well as antioxidant activities of the hydrolysate were compared with those of unmodified DWPG-1. The analysis of X-ray diffraction patterns, surface microstructure and particle size distribution indicated that enzymatic hydrolysis changed the structures of DWPG-1. Compared with the natural unhydrolyzed protein, the hydrolysate showed better physicochemical properties, such as surface hydrophobicity, solubility, emulsifying properties, foaming properties and water absorption capacity. In addition, the hydrolysate also exhibited significantly stronger antioxidant activities than DWPG-1. In conclusion, the results of this study prove that pepsin-mediated hydrolysis of walnut glutelin-1 can effectively modify the structure, function and antioxidant activity of DWPG-1, and could be used as an effective technology to produce bioactive multifunctional hydrolysates.
- Is Part Of:
- RSC advances. Volume 11:Issue 31(2021)
- Journal:
- RSC advances
- Issue:
- Volume 11:Issue 31(2021)
- Issue Display:
- Volume 11, Issue 31 (2021)
- Year:
- 2021
- Volume:
- 11
- Issue:
- 31
- Issue Sort Value:
- 2021-0011-0031-0000
- Page Start:
- 19158
- Page End:
- 19168
- Publication Date:
- 2021-05-26
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d1ra00657f ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 16864.xml