Cosmetics industry to benefit from Dyadic’s EU biocatalyst project

By Andrew MCDOUGALL

- Last updated on GMT

Cosmetics industry to benefit from Dyadic’s EU biocatalyst project

Related tags Enzyme

Biotech firm Dyadic International has embarked on a new EU-funded project aimed at developing biocatalysts for the cosmetic industry.

The Florida-based firm, which is focused on the discovery, development, manufacture and sale of enzymes and other proteins for a range of industries, is participating in the new OPTIBIOCAT collaboration in the search for cost-effective industrial production of biocatalysts.

"OPTIBIOCAT involves a highly skilled and multidisciplinary partnership of 16 partners from eight EU countries,”​ explains Dyadic's Chief Operating Officer, Danai Brooks.

“Our participation in the project further highlights the strength and recognition of our C1 technology platform in producing novel enzymes at commercial scale."

Dyadic’s C1 technology platform is a fungal expression system for gene discovery, expression and the production of enzymes and other proteins, which was developed over two decades ago.

Collaboration

The biocatalysts developed in this collaboration will be based on feruloyl acid esterases (FAE) and glucuronyl esterases (GE) which are expected to be used in the production of phenolic fatty- and sugar- esters with antioxidant activity for the cosmetic industry.

They will also be tested for use in the production of other potential compounds with improved biological activity and properties.

"We will utilize both our proprietary C1 enzyme library as well as our patented C1 technology to produce the specific targeted FAE and GE enzymes,”​ says Wim van der Wilden, General Manager of Dyadic Netherlands.

“In addition, strain improvement and fermentation optimization will then be implemented to reduce production costs and allow for industrial scale production. Our C1 platform will be a key enabling technology in this large consortium."

Dyadic says that FAE and GE available within the consortium, including those from its own proprietary enzyme library, may be improved by site-directed mutagenesis and directed evolution to further improve the desired properties.

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