Australasian Science: Australia's authority on science since 1938

Future Chemistry from the Distant Past

Credit: bluebay2014/Adobe

Credit: bluebay2014/Adobe

By James Behrendorff, Yosephine Gumulya & Elizabeth Gillam

Enzymes resurrected from the past can survive tough industrial conditions better than their modern-day counterparts, leading to safer drugs and better biofuels.

The full text of this article can be purchased from Informit.

Enzymes are protein-based catalysts that allow the chemistry of life to occur on reasonable timescales. Without them, life as we know it would not be possible. The breadth of chemical reactions catalysed by enzymes is staggering. It’s the basis to all the biochemical diversity seen in nature, like the flavours and fragrances found in foods, the drugs isolated from natural sources, and the powerful hormones that regulate growth and development.

For much of the past two centuries, chemists have been attempting to reproduce naturally occurring chemicals, but many of these molecules are extremely difficult or practically impossible to produce by conventional synthetic chemistry. Where this is possible, it often requires extreme temperatures or the use of toxic chemicals.

Since naturally occurring enzymes catalyse reactions at mild temperatures and without harsh chemicals, it seems logical to use them to catalyse challenging chemical reactions in laboratories. Why, then, haven’t they replaced conventional synthetic approaches yet?

A big part of the problem is durability. Enzymes are not built to last forever, and they haven’t evolved to work under industrial conditions. Enzymes are structurally flexible, and they are often exposed to highly reactive chemical intermediates. With prolonged use or fluctuating operational conditions, they tend to unfold and...

The full text of this article can be purchased from Informit.