Scientists designed new enzyme using Antarctic bacteria and computer calculations

Newswise — Researchers have achieved a groundbreaking milestone by utilizing extensive computer calculations to predict alterations in the optimal temperature of an enzyme. The enzyme in question was derived from a cold-adapted bacterium found in Antarctica, and the collaborative study involved scientists from Uppsala University and the University of Tromsø. Cold-adapted enzymes, commonly present in bacteria and fish residing in icy waters, have evolved to function efficiently even at extremely low temperatures, unlike enzymes found in warm-blooded animals and organisms thriving in higher temperatures.

Intrigued by the characteristics of these cold-adapted enzymes, the researchers set out to explore whether computer simulations of the catalytic chemical reaction could identify specific mutations in the Antarctic enzyme that would raise its optimal temperature. Remarkably, the calculations indicated that the insertion of 16 mutations from the corresponding pig enzyme into the bacterial variant could achieve this desired outcome.

To validate their findings, the researchers synthesized the hybrid enzyme and conducted experiments to assess its catalytic activity across different temperatures. The results confirmed their predictions, as the new variant exhibited an optimum temperature 6 °C higher than the original version. Notably, the hybrid enzyme also outperformed both the Antarctic and pig enzymes at 50 °C. Further validation was achieved through the elucidation of the hybrid enzyme's three-dimensional structure using X-ray crystallography, confirming that the structural modifications anticipated by the computer calculations had indeed occurred.

In recent years, computer-based enzyme design has emerged as a prominent and highly pursued field of research. The objective is to create enzymes with novel properties, employing computer calculations as a substitute for labor-intensive experimental approaches.

"For instance, this could involve developing enzymes that catalyze chemical reactions not naturally occurring in nature, or altering their properties to enhance their tolerance to heat, cold, high pressure, increased salinity, and other conditions. Consequently, this area has garnered substantial biotechnological interest," highlights Johan Åqvist, Professor of Theoretical Chemistry at Uppsala University.

https://www.science.org/doi/10.1126/sciadv.adi0963