Solubilisation of micellar casein powders by high-power ultrasound

•Aged Micellar Casein Powders (MCP) were solubilised by ultrasound.•The particle size was reduced from >30 μm to ∼100 nm.•The solubility was increased from 95%•No physical damage was inflicted to the milk proteins. High protein milk ingredients, such as micellar casein powder (MCP), exhibit poor...

Full description

Saved in:
Bibliographic Details
Published in:Ultrasonics sonochemistry 2020-10, Vol.67, p.105131-105131, Article 105131
Main Authors: Wu, Sinong, Li, Guantian, Xue, Yu, Ashokkumar, Muthupandian, Zhao, Haibo, Liu, Dasong, Zhou, Peng, Sun, Yang, Hemar, Yacine
Format: Article
Language:English
Subjects:
Caseins - chemistry
Chromatography, High Pressure Liquid
Electrophoresis, Polyacrylamide Gel
High-power ultrasound
Micellar casein powder
Micelles
Particle Size
Powders
Solubility
Sonication
Structure
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:•Aged Micellar Casein Powders (MCP) were solubilised by ultrasound.•The particle size was reduced from >30 μm to ∼100 nm.•The solubility was increased from 95%•No physical damage was inflicted to the milk proteins. High protein milk ingredients, such as micellar casein powder (MCP), exhibit poor solubility upon reconstitution in water, particularly after long-time storage. In this study, ultrasonication (20 kHz, power density of 0.75 W/ml) was used to improve the solubility of aged MCP powders. For all the MCP powders (concentration varying from 0.5 to 5%, and storage of MCP at 50 °C for up to 10 days) it was found that short time ultrasonication (2.5 min) reduced the size of the protein particles from >30 μm to ∼0.1 μm, as measured by light scattering. This resulted in an improvement of solubility (>95%) for all the MCP powders. Cryo-electron microscopy and small x-ray angle scattering showed that the MCP powders dissolved into particles with morphologies and internal structure similar to native casein micelles in bovine milk. SDS-PAGE and RP-HLPC showed that ultrasonication did not affect the molecular weight of the individual casein molecules. Compared to overhead stirring using a 4-blade stirrer, ultrasonication required less than 10 times the drawn electrical energy density to achieve a particle size 10 times smaller.
ISSN:1350-4177
1873-2828
DOI:10.1016/j.ultsonch.2020.105131