TY - JOUR
T1 - Use of high-intensity ultrasound as a pre-treatment for complex coacervation from whey protein isolate and iota-carrageenan
AU - Vargas, Sara A.
AU - Delgado-Macuil, R. J.
AU - Ruiz-Espinosa, Hector
AU - Amador-Espejo, Genaro
N1 - Publisher Copyright:
© The Author(s) 2022.
PY - 2023/12
Y1 - 2023/12
N2 - The aim of this work was to evaluate the influence of high intensity ultrasound (HIUS) treatment on the molecular conformation of whey protein isolated (WPI) as a previous step for complex coacervation with iota carrageenan (IC) and its effect on the surface functional properties of complex coacervates (CC). Both biopolymers were hydrated (1% w/w) separately. A WPI suspension was treated with an ultrasonic bath (40 kHz, 600 W, 30 and 60 min, 100% amplitude). A non-sonicated protein was used as a control. Coacervation was achieved by mixing WPI and IC dispersions (10 min). FTIR-ATR analysis (400–4000 cm−1) detected changes after sonication on WPI secondary structure (1600–1700 cm−1), electrostatic interaction between WPI and IC by electronegative IC charged groups like sulfate (1200–1260 cm−1), anhydrous oxygen of the 3.6 anhydro-D-galactose (940–1066 cm−1) and the electropositive regions of WPI. Rheology results showed pseudoplastic behavior of both IC and WPI-IC with a significant change in viscosity level. Further, HIUS treatment had a positive effect on the emulsifying properties of the WPI-IC coacervates, increasing the time foaming (30 min) and emulsion stability (1 month) percentage. HIUS and complex coacervation proved to be an efficient tool to improve the surface functional properties of WPI.
AB - The aim of this work was to evaluate the influence of high intensity ultrasound (HIUS) treatment on the molecular conformation of whey protein isolated (WPI) as a previous step for complex coacervation with iota carrageenan (IC) and its effect on the surface functional properties of complex coacervates (CC). Both biopolymers were hydrated (1% w/w) separately. A WPI suspension was treated with an ultrasonic bath (40 kHz, 600 W, 30 and 60 min, 100% amplitude). A non-sonicated protein was used as a control. Coacervation was achieved by mixing WPI and IC dispersions (10 min). FTIR-ATR analysis (400–4000 cm−1) detected changes after sonication on WPI secondary structure (1600–1700 cm−1), electrostatic interaction between WPI and IC by electronegative IC charged groups like sulfate (1200–1260 cm−1), anhydrous oxygen of the 3.6 anhydro-D-galactose (940–1066 cm−1) and the electropositive regions of WPI. Rheology results showed pseudoplastic behavior of both IC and WPI-IC with a significant change in viscosity level. Further, HIUS treatment had a positive effect on the emulsifying properties of the WPI-IC coacervates, increasing the time foaming (30 min) and emulsion stability (1 month) percentage. HIUS and complex coacervation proved to be an efficient tool to improve the surface functional properties of WPI.
KW - complex coacervation
KW - functional properties
KW - high intensity ultrasound
KW - iota-carrageenan
KW - whey protein isolate
UR - http://www.scopus.com/inward/record.url?scp=85138275244&partnerID=8YFLogxK
U2 - 10.1177/10820132221123716
DO - 10.1177/10820132221123716
M3 - Artículo
C2 - 36113116
AN - SCOPUS:85138275244
SN - 1082-0132
VL - 29
SP - 831
EP - 846
JO - Food Science and Technology International
JF - Food Science and Technology International
IS - 8
ER -