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RESEARCH ARTICLE
Contents Vol 73(3)

Amino Acid and Secondary Structure Integrity of Sonicated Milk Proteins

Rachana Pathak https://orcid.org/0000-0002-0563-9845 A C , Thomas S. H. Leong https://orcid.org/0000-0002-4338-6957 A C , Gregory J. O. Martin https://orcid.org/0000-0002-7099-7913 B C and Muthupandian Ashokkumar https://orcid.org/0000-0002-8442-1499 A C D
+ Author Affiliations
- Author Affiliations

A School of Chemistry, The University of Melbourne, Parkville, Vic. 3010, Australia.

B Department of Chemical Engineering, The University of Melbourne, Parkville, Vic. 3010, Australia.

C The ARC Dairy Innovation Hub, The University of Melbourne, Parkville, Vic. 3010, Australia.

D Corresponding author. Email: masho@unimelb.edu.au

Australian Journal of Chemistry 73(3) 170-179 https://doi.org/10.1071/CH19372
Submitted: 2 August 2019  Accepted: 16 September 2019   Published: 23 October 2019

Abstract

This study investigated the effect of low-frequency (20 kHz) and high-frequency (414 kHz) ultrasound treatment on the amino acid and secondary structural integrity of dairy proteins. Sonicated skim milk proteins were hydrolysed and analysed with reverse-phase high-performance liquid chromatography to investigate the amino acid content of the processed samples. It was successfully demonstrated that both low-frequency and high-frequency ultrasound did not adversely affect the amino acid content, even after prolonged extreme processing conditions (6 h, 355 kHz). This finding was supplemented with protein secondary structure data (Fourier-transform (FT)-IR secondary derivatives of the amide I band, 1700–1600 cm−1) that showed that ultrasound was capable of causing structural modifications to the dairy proteins. This study shows that ultrasound can be used to influence protein–protein interactions in skim milk via alterations to the secondary structure without degrading the amino acids in the proteins.


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