New insights into enzyme stabilisation via attachment to non-catalytic accessory domains

By necessity that turned into tradition, the chemical industry pollutes. This cannot continue, but it is hard to break bad habits. Industry uses catalysts to produce food, materials, and chemicals under harsh conditions that generate waste.

We know that using enzymes instead of conventional catalysts can reduce pollution, but it is rarely economic to make the change, because enzymes are inefficient and unstable in the solvents, detergents, pH, and temperatures that industry needs.

As enzymes that withstand high temperatures also tolerate other harsh conditions, extreme environments like hot springs are the source of many biocatalysts.

But these lack diversity, so instead we engineer stability into enzymes with useful activities, using computational tools to guide re-design, in an iterative process with a poor success rate.Recently, our team discovered highly stable enzymes in moderate temperature habitats, suggesting that such ecosystems have been overlooked, but could be a source of stable biotechnology.

The enzymes deconstruct biomass in a changeable environment, stabilised by attachment to carbohydrate binding modules (CBMs).

We hypothesise that these CBMs can be used to stabilise diverse types of enzyme.We have three aims: A) Understand why some enzymes in non-extreme environments show high heat stability. B) Show that this stability can be transferred to diverse kinds of enzymes. C) Create and share molecular biology tools so that useful biocatalysts can be stabilised.