Complex coacervation between flaxseed protein isolate and flaxseed gum. (June 2015)
- Record Type:
- Journal Article
- Title:
- Complex coacervation between flaxseed protein isolate and flaxseed gum. (June 2015)
- Main Title:
- Complex coacervation between flaxseed protein isolate and flaxseed gum
- Authors:
- Kaushik, Pratibha
Dowling, Kim
Barrow, Colin J.
Adhikari, Benu - Abstract:
- Abstract: Flaxseed protein isolate (FPI) and flaxseed gum (FG) were extracted, and the electrostatic complexation between these two biopolymers was studied as a function of pH and FPI-to-FG ratio using turbidimetric and electrophoretic mobility (zeta potential) tests. The zeta potential values of FPI, FG, and their mixtures at the FPI-to-FG ratios of 1:1, 3:1, 5:1, 10:1, 15:1 were measured over a pH range 8.0–1.5. The alteration of the secondary structure of FPI as a function of pH was studied using circular dichroism. The proportion of ɑ-helical structure decreased, whereas both β-sheet structure and random coil structure increased with the lowering of pH from 8.0 to 3.0. The acidic pH affected the secondary structure of FPI and the unfolding of helix conformation facilitated the complexation of FPI with FG. The optimum FPI-to-FG ratio for complex coacervation was found to be 3:1. The critical pH values associated with the formation of soluble (pHc) and insoluble (pHɸ1 ) complexes at the optimum FPI-to-FG ratio were found to be 6.0 and 4.5, respectively. The optimum pH (pHopt ) for the optimum complex coacervation was 3.1. The instability and dissolution of FPI–FG complex coacervates started (pHɸ2 ) at pH 2.1. These findings contribute to the development of FPI–FG complex coacervates as delivery vehicles for unstable albeit valuable nutrients such as omega-3 fatty acids. Highlights: Flaxseed protein and gum were extracted from raw flaxseed. Interactions of protein andAbstract: Flaxseed protein isolate (FPI) and flaxseed gum (FG) were extracted, and the electrostatic complexation between these two biopolymers was studied as a function of pH and FPI-to-FG ratio using turbidimetric and electrophoretic mobility (zeta potential) tests. The zeta potential values of FPI, FG, and their mixtures at the FPI-to-FG ratios of 1:1, 3:1, 5:1, 10:1, 15:1 were measured over a pH range 8.0–1.5. The alteration of the secondary structure of FPI as a function of pH was studied using circular dichroism. The proportion of ɑ-helical structure decreased, whereas both β-sheet structure and random coil structure increased with the lowering of pH from 8.0 to 3.0. The acidic pH affected the secondary structure of FPI and the unfolding of helix conformation facilitated the complexation of FPI with FG. The optimum FPI-to-FG ratio for complex coacervation was found to be 3:1. The critical pH values associated with the formation of soluble (pHc) and insoluble (pHɸ1 ) complexes at the optimum FPI-to-FG ratio were found to be 6.0 and 4.5, respectively. The optimum pH (pHopt ) for the optimum complex coacervation was 3.1. The instability and dissolution of FPI–FG complex coacervates started (pHɸ2 ) at pH 2.1. These findings contribute to the development of FPI–FG complex coacervates as delivery vehicles for unstable albeit valuable nutrients such as omega-3 fatty acids. Highlights: Flaxseed protein and gum were extracted from raw flaxseed. Interactions of protein and polysaccharide were studied as function of pH and different mixing ratios. Different phase boundaries related to structure-forming events were determined. Changes in the secondary structure of protein with lowering of pH were found facilitating the interactions of protein and polysaccharide. Optimum pH and protein-to-polysaccharide ratio for complexation was found to be 3.1 and 3:1. … (more)
- Is Part Of:
- Food research international. Volume 72(2015:Jun.)
- Journal:
- Food research international
- Issue:
- Volume 72(2015:Jun.)
- Issue Display:
- Volume 72 (2015)
- Year:
- 2015
- Volume:
- 72
- Issue Sort Value:
- 2015-0072-0000-0000
- Page Start:
- 91
- Page End:
- 97
- Publication Date:
- 2015-06
- Subjects:
- Flaxseed protein isolate -- Flaxseed gum -- Secondary structure -- Complex coacervation -- Zeta potential -- Turbidity
Food -- Analysis -- Periodicals
Food industry and trade -- Periodicals
Food industry and trade -- Canada -- Periodicals
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Food -- Periodicals
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Aliments -- Industrie et commerce -- Périodiques
Aliments -- Industrie et commerce -- Canada -- Périodiques
Aliments -- Recherche -- Périodiques
Food industry and trade
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664.005 - Journal URLs:
- http://www.sciencedirect.com/science/journal/09639969 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodres.2015.03.046 ↗
- Languages:
- English
- ISSNs:
- 0963-9969
- Deposit Type:
- Legaldeposit
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