UHT Milk Study Improves Understanding of Age-Related Diseases
25 Apr 2017 --- Researchers at Australian National University (ANU) are studying UHT milk to gain a better understanding of Alzheimer’s, Parkinson’s and type 2 diabetes, age-related diseases that cause millions of deaths each year.
The researchers are studying two unrelated proteins which aggregate in UHT milk over a period of months to form clusters called amyloid fibrils, causing the milk to transform from a liquid into a gel. According to ANU Professor John Carver, one of the study’s authors, the same type of protein clusters are found in plaque deposits in cases of Alzheimer’s and Parkinson’s.
“Parkinson’s, dementia and type 2 diabetes are big problems for the aging population in Australia and many other countries around the world,” Professor Carver says. “Our interest in milk proteins led to a discovery of the reason for this gelling phenomenon occurring in aged UHT milk.”
“The research does not suggest UHT milk can cause these age-related diseases,” Carver says, adding that milk proteins change structurally when heated briefly to around 140 degrees to produce UHT milk, causing the gelling phenomenon with long-term storage. Normal pasteurised milk did not form amyloid fibrils, the researchers said.
Along with the researchers at ANU, CSIRO, University of Wollongong and international researchers contributed to the study, which is published in the journal Small.
The study’s authors, ANU’s John Carver and Jared Raynes from CSIRO Food and Agriculture, tell NutritionInsight that “amyloid fibrillar co-aggregation may be important in diseases such as type 2 diabetes, where sufferers are at a greater risk of Alzheimer’s and Parkinson’s diseases (which are amyloid diseases), possibly due to the interaction of these amyloid-forming proteins. The co-aggregation of disease-related proteins will be a future research area that we will be investigating, as well as the interaction and role of common food additives in preventing these aggregated structures from occurring, particularly in milk proteins.”
“Another future project will also involve investigating co-aggregation of proteins for the production of novel amyloid-containing bio-nanomaterials with enhanced properties based upon the features of the different proteins that are incorporated into the bio-nanomaterials,” they add.
