-
Tytuł:
-
Effect of change in pH, heat and ultrasound pre-treatments on binding interactions between quercetin and whey protein concentrate.
-
Autorzy:
-
Ji W; College of Food Science and Engineering, Gansu Agricultural University, Lanzhou, 730070, China; College of Science, Gansu Agricultural University, Lanzhou, 730070, China.
Yang F; College of Food Science and Engineering, Gansu Agricultural University, Lanzhou, 730070, China. Electronic address: .
Yang M; College of Science, Gansu Agricultural University, Lanzhou, 730070, China. Electronic address: .
-
Źródło:
-
Food chemistry [Food Chem] 2022 Aug 01; Vol. 384, pp. 132508. Date of Electronic Publication: 2022 Feb 19.
-
Typ publikacji:
-
Journal Article
-
Język:
-
English
-
Imprint Name(s):
-
Publication: Barking : Elsevier Applied Science Publishers
Original Publication: Barking, Eng., Applied Science Publishers.
-
MeSH Terms:
-
Hot Temperature*
Quercetin*
Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Whey Proteins/chemistry
-
Contributed Indexing:
-
Keywords: Antioxidant capacity; Change in pH; Heat treatment; Quercetin; Stability; Ultrasound treatment; Whey protein concentrate
-
Substance Nomenclature:
-
0 (Whey Proteins)
9IKM0I5T1E (Quercetin)
-
Entry Date(s):
-
Date Created: 20220301 Date Completed: 20220412 Latest Revision: 20220412
-
Update Code:
-
20240104
-
DOI:
-
10.1016/j.foodchem.2022.132508
-
PMID:
-
35231711
-
The effects of change in pH, heat and ultrasound pre-treatments on the binding mechanism of quercetin (Q) with whey protein concentrate (WPC) were investigated, as well as the antioxidant capacity and stability of Q in the complexes. The main interaction between WPC and Q was hydrophobic and was not affected by pre-treatments. The binding affinity for Q with WPC at pH 7.4 after heating at 80 °C for 30 min, was the strongest, resulting in a WPC-Q complex with a more compact structure, the smallest particle size (184.43 ± 10.47 nm) and the largest ζ-potential (-20.58 ± 0.60 mV). This complex also provided the greatest stabilization of Q, when exposed to 37 °C and light. Complexation of WPC with Q reduced the ABTS radical scavenging capacity of Q, but enhanced its DPPH radical scavenging capacity and reducing power. These findings provide valuable information for optimizing the formation conditions of WPC-Q.
(Copyright © 2022 Elsevier Ltd. All rights reserved.)