Is long-life milk the answer to age-related diseases?

Friday, 21st April, 2017

ANU's Professor John Carver's UHT milk research linked to Alzheimer's and Parkinson's. Photo: ANU

LONG-LIFE milk could hold the key to better understanding age-related diseases including Alzheimer's, Parkinson's and type 2 diabetes.

The new study on why ultra-high temperature (UHT) milk goes off could open the door to improved treatment for aged related diseases, and even lead to prevention.

About 500 million people worldwide suffer from these diseases, which cause millions of deaths each year.

A team of international and Australian scientists from Australian National University in Canberra, the CSIRO and University of Wollongong led the study into why long-life milk goes bad.

The researchers found that gel formed when UHT milk was left out for a long time was similar to plaque deposits that can occur in the human body and cause some diseases.

Co-lead researcher, ANU's John Carver said two unrelated proteins aggregate in UHT milk over a period of months to form clusters called amyloid fibrils, which cause the milk to transform from a liquid into a gel.

He said 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 ageing population in Australia and many other countries around the world," said Professor Carver from the ANU Research School of Chemistry.

"Our interest in milk proteins led to a discovery of the reason for this gelling phenomenon occurring in aged UHT milk."

He said if scientists could stop long-life milk going off and forming the protein clusters, this could hold the key to finding a cure for diseases.

Professor Carver said the research "does not suggest UHT milk can cause these age-related diseases".

He said milk proteins changed structurally when heated briefly to around 140 degrees to produce UHT milk, causing the gelling phenomenon with long-term storage.

He said normal pasteurised milk did not form amyloid fibrils.

The study was published in the journal Small.

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