beta-apo-10--carotenal has been researched along with beta-ionone* in 3 studies
3 other study(ies) available for beta-apo-10--carotenal and beta-ionone
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Synthesis and characterization of quantum dot nanoparticles bound to the plant volatile precursor of hydroxy-apo-10'-carotenal.
This study is focused on the synthesis and characterization of hydroxy-apo-10'-carotenal/quantum dot (QD) conjugates aiming at the in vivo visualization of β-ionone, a carotenoid-derived volatile compound known for its important contribution to the flavor and aroma of many fruits, vegetables, and plants. The synthesis of nanoparticles bound to plant volatile precursors was achieved via coupling reaction of the QD to C27-aldehyde which was prepared from α-ionone via 12 steps in 2.4% overall yield. The formation of the QD-conjugate was confirmed by measuring its fluorescence spectrum to observe the occurrence of fluorescence resonance energy transfer. Topics: Aldehydes; Carotenoids; Fluorescence Resonance Energy Transfer; Nanoparticles; Norisoprenoids; Quantum Dots | 2014 |
A peroxidase from Lepista irina cleaves beta,beta-carotene to flavor compounds.
Extracellular liquid of the edible fungus Lepista irina was found to effectively degrade beta,beta-carotene, beta-lonone, beta-cyclocitral, dihydroactinidiolide, and 2-hydroxy-2,6,6-trimethylcyclohexanone were formed as volatile breakdown products of beta,beta-carotene with mycelium-free culture supernatants, whereas beta-apo-10'-carotenal was identified as non-volatile degradation product. The key enzyme catalyzing the oxidative cleavage of beta,beta-carotene was purified with an overall yield of 63% and a purification factor of 43. Biochemical characterization showed a molecular mass of 50.5 kDa and an isoelectric point of 3.75. Fastest beta,beta-carotene degradation occurred at 34 degrees C and pH values between 3.5 and 4. Degenerate oligonucleotides were derived from N-terminal and internal amino acid sequences. By means of PCR-based cDNA-library screening a 1284 bp cDNA was identified which showed great overall similarity to Pleurotus eryngii polyvalent peroxidases. The obtained sequence contains an open reading frame of 1083 nucleotides, encoding a polypeptide of 361 amino acids. A 30 amino acid signal peptide was identified upstream of the N-terminal sequence of the mature enzyme. The L. irina versatile peroxidase represents the first microbial enzyme capable of carotenoid degradation that has been characterized on a molecular level, proving the participation of extracellular enzymes of white rot fungi in biotic carotenoid degradation processes. Topics: Amino Acid Sequence; Basidiomycota; beta Carotene; Biodegradation, Environmental; Carotenoids; Culture Media; Flavoring Agents; Hydrogen-Ion Concentration; Molecular Sequence Data; Norisoprenoids; Oxidation-Reduction; Peroxidase; Temperature; Time Factors; Volatilization | 2003 |
Identification and characterization of a mammalian enzyme catalyzing the asymmetric oxidative cleavage of provitamin A.
In vertebrates, symmetric versus asymmetric cleavage of beta-carotene in the biosynthesis of vitamin A and its derivatives has been controversially discussed. Recently we have been able to identify a cDNA encoding a metazoan beta,beta-carotene-15,15'-dioxygenase from the fruit fly Drosophila melanogaster. This enzyme catalyzes the key step in vitamin A biosynthesis, symmetrically cleaving beta-carotene to give two molecules of retinal. Mutations in the corresponding gene are known to lead to a blind, vitamin A-deficient phenotype. Orthologs of this enzyme have very recently been found also in vertebrates and molecularly characterized. Here we report the identification of a cDNA from mouse encoding a second type of carotene dioxygenase catalyzing exclusively the asymmetric oxidative cleavage of beta-carotene at the 9',10' double bond of beta-carotene and resulting in the formation of beta-apo-10'-carotenal and beta-ionone, a substance known as a floral scent from roses, for example. Besides beta-carotene, lycopene is also oxidatively cleaved by the enzyme. The deduced amino acid sequence shares significant sequence identity with the beta,beta-carotene-15,15'-dioxygenases, and the two enzyme types have several conserved motifs. To establish its occurrence in different vertebrates, we then attempted and succeeded in cloning cDNAs encoding this new type of carotene dioxygenase from human and zebrafish as well. As regards their possible role, the apocarotenals formed by this enzyme may be the precursors for the biosynthesis of retinoic acid or exert unknown physiological effects. Thus, in contrast to Drosophila, in vertebrates both symmetric and asymmetric cleavage pathways exist for carotenes, revealing a greater complexity of carotene metabolism. Topics: Amino Acid Sequence; Animals; beta Carotene; beta-Carotene 15,15'-Monooxygenase; Carotenoids; Catalysis; Chromatography, High Pressure Liquid; Cloning, Molecular; DNA, Complementary; Drosophila; Drosophila Proteins; Expressed Sequence Tags; Female; Gene Library; Humans; Lycopene; Male; Mass Spectrometry; Mice; Mice, Inbred BALB C; Models, Chemical; Molecular Sequence Data; Norisoprenoids; Oxygen; Oxygenases; Phenotype; Phylogeny; Retinaldehyde; RNA; Sequence Homology, Amino Acid; Terpenes; Time Factors; Tissue Distribution; Vitamin A; Zebrafish | 2001 |