ADVERTISEMENT
2 /3 FREE ARTICLES LEFT THIS MONTH Remaining
Chemistry matters. Join us to get the news you need.

If you have an ACS member number, please enter it here so we can link this account to your membership. (optional)

ACS values your privacy. By submitting your information, you are gaining access to C&EN and subscribing to our weekly newsletter. We use the information you provide to make your reading experience better, and we will never sell your data to third party members.

ENJOY UNLIMITED ACCES TO C&EN

Biotechnology

Structure of plastic-munching enzyme MHETase solved

Mutations could move plastics biorecycling a step forward

by Laura Howes
April 21, 2019 | APPEARED IN VOLUME 97, ISSUE 16

 

09716-scicon8-figure2a.jpg
Credit: Gert Weber/HZB
MHETase has a lid (blue) and a hydrolase domain (orange) that work together to split MHET (yellow).

Plastic bottles and packaging made from poly(ethylene terephthalate) (PET) are ubiquitous, and plastic litter is a global problem, from the great Pacific garbage patch to the air we breathe. PET can be broken down and reused, but the process is not widely employed. In 2016, researchers discovered a bacterium that partially feeds on PET. The bacterium uses two enzymes: PETase converts PET to mono(2-hydroxyethyl) terephthalate (MHET) and then MHETase breaks that product into terephthalic acid and ethylene glycol. Researchers at the University of Greifswald and Helmholtz-Zentrum Berlin have now solved the crystal structure of MHETase (Nat. Commun. 2019, DOI: 10.1038/s41467-019-09326-3), showing how the enzyme closes around the substrate when it docks. After determining the active-site structure, the team made mutants that work at higher substrate concentrations and can break down another substrate, taking another step in the journey toward plastics biorecycling.

X

Article:

This article has been sent to the following recipient:

Leave A Comment

*Required to comment