Focusing on Hofmeister series: Composition, structure and functional properties of pea protein extracted with food-related anions. (December 2022)
- Record Type:
- Journal Article
- Title:
- Focusing on Hofmeister series: Composition, structure and functional properties of pea protein extracted with food-related anions. (December 2022)
- Main Title:
- Focusing on Hofmeister series: Composition, structure and functional properties of pea protein extracted with food-related anions
- Authors:
- Liu, Yexue
Li, Xueying
Liu, Jiameng
Wei, Likun
Liu, Yihan
Lu, Fuping
Wang, Wenhang
Li, Qinggang
Li, Yu - Abstract:
- Abstract: Hofmeister series effects have important impacts on hydration and stability of proteins during dissolution. However, Hofmeister anions in plant protein extraction are not yet clear. Here, the effects on pea protein extraction of some common food-compatible anions (CO3 2−, Citrate 3−, SO4 2−, C3 H5 O3 − (lactate), CH3 COO −, and Cl − ) in their Na-form were investigated. Native gel electrophoresis of dialyzed proteins revealed that CO3 2−, Citrate 3−, and SO4 2− decreased the intensity of 11S legumin fraction compared to C3 H5 O3 −, CH3 COO −, and Cl − . Also, pea protein extracted by the first three anions showed a higher denaturation state and exposed more hydrophobic regions to the aqueous solvent, as shown by the circular dichroism and fluorescence probe measurements, respectively. Accordingly, the techno-functional properties of the obtained proteins varied, depending on the Hofmeister order of each anion. A notable exception was represented by the proteins extracted by carbonate (a salting-out salt), whose small particle size and high solubility at pH 7 were more akin to that of the proteins extracted by salting-in salts. An effect which may be due to the synergistic effect of bicarbonate (the main ionic species present at pH 8) and chloride (necessary to bring, as HCl, carbonate solution to pH 8). In summary, Hofmeister anions are suitable for plant protein extraction, providing a promising approach to confer tunable properties to pea proteins and this mayAbstract: Hofmeister series effects have important impacts on hydration and stability of proteins during dissolution. However, Hofmeister anions in plant protein extraction are not yet clear. Here, the effects on pea protein extraction of some common food-compatible anions (CO3 2−, Citrate 3−, SO4 2−, C3 H5 O3 − (lactate), CH3 COO −, and Cl − ) in their Na-form were investigated. Native gel electrophoresis of dialyzed proteins revealed that CO3 2−, Citrate 3−, and SO4 2− decreased the intensity of 11S legumin fraction compared to C3 H5 O3 −, CH3 COO −, and Cl − . Also, pea protein extracted by the first three anions showed a higher denaturation state and exposed more hydrophobic regions to the aqueous solvent, as shown by the circular dichroism and fluorescence probe measurements, respectively. Accordingly, the techno-functional properties of the obtained proteins varied, depending on the Hofmeister order of each anion. A notable exception was represented by the proteins extracted by carbonate (a salting-out salt), whose small particle size and high solubility at pH 7 were more akin to that of the proteins extracted by salting-in salts. An effect which may be due to the synergistic effect of bicarbonate (the main ionic species present at pH 8) and chloride (necessary to bring, as HCl, carbonate solution to pH 8). In summary, Hofmeister anions are suitable for plant protein extraction, providing a promising approach to confer tunable properties to pea proteins and this may enhance the usability and application fields of pea protein. Graphical abstract: Image 1 Highlights: Structure and functional properties of pea protein are impacted by Hofmeister effect. Na2 CO3 solution resulted in a highest extraction yield of pea protein. NaCl extraction promotes the protein secondary structure folding. Na2 CO3 solution had a more impact on protein conformation than others salt. NaCl extracted pea protein had highest gelling temperature. … (more)
- Is Part Of:
- Food hydrocolloids. Volume 133(2022)
- Journal:
- Food hydrocolloids
- Issue:
- Volume 133(2022)
- Issue Display:
- Volume 133, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 133
- Issue:
- 2022
- Issue Sort Value:
- 2022-0133-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-12
- Subjects:
- Pea -- Hofmeister anions -- Extraction -- Secondary structures -- Protein functionality
Hydrocolloids -- Periodicals
Food additives -- Periodicals
Colloïdes -- Périodiques
Aliments -- Additifs -- Périodiques
Colloids
Food additives
Periodicals
Electronic journals
664.06 - Journal URLs:
- http://www.sciencedirect.com/science/journal/0268005X ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodhyd.2022.107976 ↗
- Languages:
- English
- ISSNs:
- 0268-005X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.556000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 23555.xml