The team at Leicester University has discovered a new phenomenon occurring at the atomic level that dictates how enzymes work. Their study of enzymes - which are vital for catalysis within industry - reveals that chemical reactions can proceed through energy barriers.
The vast majority of studies have concentrated on understanding how enzymes facilitate passage of a reaction over an energy barrier. However, the Leicester University study has revealed that passage through, rather than over, the barrier can occur - a process that relies on quantum mechanical effects such as tunnelling.
"Quantum tunnelling is akin to traversing a landscape by tunnelling at the foot of a hill rather than walking over the summit," said Michael Sutcliffe of the department of biochemistry at the University of Leicester.
"In the quantum world, small particles like the electron and hydrogen atom are able to 'tunnel' through energy barriers (or hills), and the Leicester team has demonstrated this occurs in enzyme-catalysed reactions."
Enzymes are used in many industrial contexts and play a vital role in food and beverage applications such as brewing and meat tenderising.
In many large breweries for example, auxiliary enzymes from are used to increase brewhouse efficiency, control the brewing process, and produce beer of a consistently high quality.
Auxiliary enzymes can be used to ensure smooth brewing operations at all stages, to optimise adjunct liquefaction, to produce low-carbohydrate beer ('light beer'), to shorten the beer maturation time, and to produce beer from enhanced malts and cereals.
And in meat tenderising, the two most often used enzymes are Papain and Bromelain, both derived from plant sources. Other sources of enzymes for meat tenderisation, include Bacillus subtilis, Aspergillus oryzae, and even pancreatin derived from the pancreas gland (typically porcine).
In any case, by showing that small particles like the electron and hydrogen atom are able to 'tunnel' through energy barriers, and that this occurs in enzyme-catalysed reactions, new approaches may be needed in using enzymes in the future.
"This research is a very fundamental work into how enzymes work," Sutcliffe's colleague professor Nigel Scrutton told FoodProductionDaily.com. "This new underpinning theory affects a whole range of industrial processes."
"These new ideas are breaking all the rules of classical models of enzyme catalysis."
Indeed, the research flies in the face of conventional wisdom on how enzyme reactions work.
"Since the discovery of enzymes just over a century ago, we have witnessed an explosion in our understanding of enzyme catalysis, leading to a more detailed appreciation of how they work," said Scrutton.
"However, despite the huge efforts to redesign enzyme molecules for specific applications (such as food processing and brewing), progress in this area has been generally disappointing. This stems from our limited understanding of the subtleties by which enzymes enhance reaction rates."
Since electron and hydrogen transfer is common to virtually all naturally occurring enzymes, the discovery has wide ranging implications for our understanding of how enzymes work.