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New enzyme Treatments from Old Observations

By Ryan Tam – Chemical Engineering Student @ Trinity College, Cambridge


Enzymes are biological catalysts that help speed up the rate of metabolic reactions within the body. The substrate, which is the molecule being broken down, fits into the active site of the enzyme like a lock and key mechanism. The human body is known to produce over a thousand enzymes, however, one enzyme it does not produce is cellulase.

Cellulase catalyses the decomposition of cellulose into simpler sugars and is produced by many types of different bacteria and fungi. The bacteria in our large intestine are able to digest some of the dietary fibre that we consume, which consists of cellulose. Cellulose is also present in the cell walls of yeast cells belonging to the Genus Candida; these are the types of pathogens responsible for causing genital yeast infections, athlete’s foot, and oral thrush.

The cell walls of yeast cells contain beta-glucans, which is a long-chain polymer consisting of beta-glucose; cellulose is a type of beta-glucan. The biofilm produced by these yeast cells also contains high levels of cellulose, which shields the yeast cells from the human immune system and allows them to grow unhindered. The cellulase enzyme is able to break down the cell wall of the yeast cells, and can also make the biofilm layer thinner, thereby exposing more of the pathogens to the immune system.

One advantage of using enzymes during treatment is that the yeast cells are unable to build resistance towards cellulase, unlike antifungal drugs. The presence of cellulase does not harm the human body, nor does it cause the pathogens to mutate. Ingesting the enzyme may also be more useful for treating fungal infections, especially genital and oral thrush, where antifungal creams may not be the most comfortable method of treatment.