Structure – Functionality of lentil protein-polyphenol conjugates. (15th January 2022)
- Record Type:
- Journal Article
- Title:
- Structure – Functionality of lentil protein-polyphenol conjugates. (15th January 2022)
- Main Title:
- Structure – Functionality of lentil protein-polyphenol conjugates
- Authors:
- Parolia, Saakshi
Maley, Jason
Sammynaiken, Ramaswami
Green, Rick
Nickerson, Michael
Ghosh, Supratim - Abstract:
- Highlights: Lentil protein isolate was conjugated with plant polyphenols. Equilibrium binding constants decreased in the order quercetin > ellagic acid > rutin. Random coil secondary structure of the proteins significantly increased upon conjugation. Conjugates were less surface active than the original lentil proteins. Radical scavenging and reducing power of the conjugates was better than the polyphenols. Abstract: Lentil protein isolate (LPI) was conjugated with plant polyphenols (quercetin, rutin, ellagic acid), and the structural and functional characteristics of the conjugates were determined in comparison with the proteins and pure polyphenols. The interaction between polyphenols and protein was achieved by a grafting method at pH 9.0 in the presence of atmospheric oxygen. Surface plasmon resonance measurements showed polyphenols' direct interaction with LPI, with the order of binding strength quercetin > ellagic acid > rutin. The degree of conjugation also followed the same order. Structural analysis of the conjugates was performed using FTIR, intrinsic fluorescence, and surface hydrophobicity. A significant improvement in DPPḢ radical scavenging and ferric reducing antioxidant power of the conjugates was observed compared to the polyphenols. However, there was a decrease in the surface activity of the conjugates compared to LPI. Such conjugation provides a novel way to combine the advantages of using plant protein and polyphenols in developing a novel foodHighlights: Lentil protein isolate was conjugated with plant polyphenols. Equilibrium binding constants decreased in the order quercetin > ellagic acid > rutin. Random coil secondary structure of the proteins significantly increased upon conjugation. Conjugates were less surface active than the original lentil proteins. Radical scavenging and reducing power of the conjugates was better than the polyphenols. Abstract: Lentil protein isolate (LPI) was conjugated with plant polyphenols (quercetin, rutin, ellagic acid), and the structural and functional characteristics of the conjugates were determined in comparison with the proteins and pure polyphenols. The interaction between polyphenols and protein was achieved by a grafting method at pH 9.0 in the presence of atmospheric oxygen. Surface plasmon resonance measurements showed polyphenols' direct interaction with LPI, with the order of binding strength quercetin > ellagic acid > rutin. The degree of conjugation also followed the same order. Structural analysis of the conjugates was performed using FTIR, intrinsic fluorescence, and surface hydrophobicity. A significant improvement in DPPḢ radical scavenging and ferric reducing antioxidant power of the conjugates was observed compared to the polyphenols. However, there was a decrease in the surface activity of the conjugates compared to LPI. Such conjugation provides a novel way to combine the advantages of using plant protein and polyphenols in developing a novel food ingredient. … (more)
- Is Part Of:
- Food chemistry. Volume 367(2022)
- Journal:
- Food chemistry
- Issue:
- Volume 367(2022)
- Issue Display:
- Volume 367, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 367
- Issue:
- 2022
- Issue Sort Value:
- 2022-0367-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-01-15
- Subjects:
- Lentil protein isolate -- Polyphenols -- Protein-polyphenol conjugates -- SPR -- Antioxidant activity
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2021.130603 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 19328.xml