Public Summary of Deliverable 4.4
The primary goal of this task was to evaluate how enzymes used in laundry formulations maintain their stability when combined with different additives. This is particularly relevant in the context of modern laundry practices, where there is a growing trend towards using detergents at lower washing temperatures to promote sustainability [1]. To achieve this, in Radicalz we have selected a psychrophilic lipase enzyme, derived from a marine organism, known for its ability to function effectively at lower temperatures [2]. Using high-throughput stability characterization studies, the team analyzed how this enzyme performs in the presence of various additives at concentrations compatible with laundry detergents requirement. We have utilized innovative microfluidics techniques which enabled rapid and cost-effective screening of many biosurfactant additives. The insights gained from this research are expected to contribute to the development of more effective and sustainable consumer products, particularly in the laundry and house care sectors. By understanding how enzymes interact with additives, manufacturers can create products that are both efficient and environmentally friendly.
Institutions
- University of Exeter (GB)
- Universidad Autónoma de Madrid (ES)
Publication Details
- Journal
- Zenodo (CERN European Organization for Nuclear Research)
- Published
- 2025-05-31
- DOI
- https://doi.org/10.5281/zenodo.15847924
- Primary Topic
- Enzyme Catalysis and Immobilization
- Type
- article
- Field-Weighted Citation Impact
- 0.00