ADELAIDE / Australia, 16 June 2026: Researchers at the University of Adelaide have uncovered the complex molecular mechanisms of a vital plant enzyme, a breakthrough that could pave the way for advances in medicine, pharmaceuticals, biotechnology and industrial chemistry.
The study, led by Professor Maria Hrmova from the School of Agriculture, Food and Wine, has revealed unprecedented insights into the structure and function of plant exo-hydrolytic enzymes, which play essential roles in plant growth, development and survival. The findings have been published in the scientific journal Biochimica et Biophysica Acta.
Over the past decade, Professor Hrmova and a multidisciplinary team of approximately 30 researchers investigated how these enzymes operate at the atomic level. Their research demonstrated that understanding the function of a single enzyme requires the analysis of as many as 50 crystal structures.
“There are up to 80,000 fundamental-to-life enzymes upon which nearly all biochemical reactions depend,” said Professor Hrmova. “Enzymes drive essential chemical reactions that produce building blocks, metabolites and energy sources required by living organisms.”
The research focused on plant exo-hydrolytic enzymes known as glycoside hydrolases, which are involved in critical biological processes including plant nutrition, seed germination, root growth and pollination.
Using a combination of X-ray and neutron crystallography, enzyme kinetics, mass spectrometry, nuclear magnetic resonance spectroscopy and advanced 3D molecular modelling, the team mapped enzyme activity with exceptional precision.
The researchers discovered a previously unknown catalytic process called substrate-product-assisted processivity, which enables the enzyme to remain attached to a substrate while converting it into a product through highly efficient hydrolytic reactions.
According to Professor Hrmova, the reactions occur at extremely rapid rates that cannot be captured using conventional experimental techniques. To overcome this challenge, the team employed computational modelling to track molecular movements at the nanoscale.
The study also revealed how water molecules influence enzyme efficiency and identified structural features that have evolved under natural selection pressures over time.
“These findings improve our understanding of enzyme catalysis and may help scientists develop bioengineered enzymes with enhanced catalytic rates, greater stability and reduced product inhibition,” Professor Hrmova said.
Researchers believe the discoveries could have significant applications in industrial biotechnology, enabling the development of new bio-based products and more efficient manufacturing processes that utilize engineered enzymes outside biological systems.
The findings offer valuable insights into the fundamental mechanisms of life while opening new opportunities for innovation across multiple scientific and industrial sectors.