Publications by authors named "Eva E Dominnik"
Article Synopsis
- β-carotene (BCR) is a key carotenoid that acts as a colorant, antioxidant, and provitamin A, but its hydrophobic nature makes it challenging to distribute in water.
- The crystal structure of a BCR-binding protein (BBP) from male locusts reveals how this protein efficiently binds BCR, forming a unique tubular structure that accommodates the carotenoid.
- BBP can also bind various xanthophylls depending on their oxygen content but does not bind lycopene, highlighting its potential use in solubilizing BCR for applications.
Carotenoids are hydrophobic pigments binding to diverse carotenoproteins, many of which remain unexplored. Focusing on yellow gregarious locusts accumulating cuticular carotenoids, here we use engineered Escherichia coli cells to reconstitute a functional water-soluble β-carotene-binding protein, BBP. HPLC and Raman spectroscopy confirmed that recombinant BBP avidly binds β-carotene, inducing the unusual vibronic structure of its absorbance spectrum, just like native BBP extracted from the locust cuticles.
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