A mechanism for red coloration in vertebrates.

Red coloration is a salient feature of the natural world. Many vertebrates produce red color by converting dietary yellow carotenoids into red ketocarotenoids via an unknown mechanism. Here, we show that two enzymes, cytochrome P450 2J19 (CYP2J19) and 3-hydroxybutyrate dehydrogenase 1-like (BDH1L), are sufficient to catalyze this conversion. In birds, both enzymes are expressed at the sites of ketocarotenoid biosynthesis (feather follicles and red cone photoreceptors), and genetic evidence implicates these enzymes in yellow/red color variation in feathers. In fish, the homologs of CYP2J19 and BDH1L are required for ketocarotenoid production, and we show that these enzymes are sufficient to produce ketocarotenoids in cell culture and when ectopically expressed in fish skin. Finally, we demonstrate that the red-cone-enriched tetratricopeptide repeat protein 39B (TTC39B) enhances ketocarotenoid production when co-expressed with CYP2J19 and BDH1L. The discovery of this mechanism of ketocarotenoid biosynthesis has major implications for understanding the evolution of color diversity in vertebrates.

The Metabolism and Potential Bioactivity of Chlorophyll and Metallo-chlorophyll Derivatives in the Gastrointestinal Tract.

Chlorophyll is the vivid chromophore which imparts the green color to plant leaves, and is consumed by humans through green vegetables. The basic porphyrin structure of chlorophyll binds magnesium in plants, but can bind different divalent metals (e.g., copper, zinc, iron) facilitated by food processing techniques and/or chemical synthesis. This review covers the known elements of chlorophyll and metallo-chlorophyll absorption, distribution, metabolism, excretion in vitro and in vivo. The review discusses what is understood about the ability of these novel metallo-chlorophyll derivatives to deliver essential metals. This review also detail chlorophyll and metallo-chlorophyll toxin binding properties which largely occur during digestion, focusing on toxins including dioxins, heterocyclic aromatic amines, polyaromatic hydrocarbons, and aflatoxin. Finally, the article highlights the gaps in the understanding of the metabolism and metal and toxin-binding bioactivity of this family of molecules.

Comparison of the carotenoid profiles of commonly consumed smear-ripened cheeses.

The objective of this study was to identify the carotenoids imparting the orange colour to the rind, and pale yellow color to the core, of selected smear-ripened cheeses. The cheeses investigated were Charloe, Ashbrook, Taleggio, and Limburger, and were sourced from artisanal markets. Samples of the rind and core were extracted using non-polar solvents, followed by saponification to hydrolyze triglycerides to remove fatty acids, and to release carotenoid esters. Extracts were tested using ultra-high pressure liquid chromatograph-diode array detector-high resolution mass spectrometry (UHPLC-DAD-MS and -MS/MS), and identities of α- and ß-carotene, lycopene, and ß-cryptoxanthin confirmed with authentic standards. ß-Carotene was the predominant species in both the rind and core, absorbing ~70% of the signal at 450 nm in all cheese extracts tested, as well as minor quantities of ß-cryptoxanthin and α-carotene. Carotenoids unique to the rind included lycopene as well as the rare bacterial carotenoids previously identified in bacterial isolates of cheeses (i.e. decaprenoxanthin, sarcinaxanthin, and echinenone). This is the first detailed characterisation of carotenoids extracted directly from smear-ripened cheeses, and reveals that smear-ripened cheese can contribute both provitamin A carotenoids as well as C50 carotenoids to the human diet.

Novel Processing Technologies as Compared to Thermal Treatment on the Bioaccessibility and Caco-2 Cell Uptake of Carotenoids from Tomato and Kale-Based Juices.

This research aimed to measure the impact of novel food processing techniques, i.e., pulsed electric field (PEF) and ohmic heating (OH), on carotenoid bioaccessibility and Caco-2 cell uptake from tomato juice and high-pressure processing (HPP) and PEF on the same attributes from kale-based juices, as compared with raw (nonprocessed) and conventional thermally treated (TT) juices. Lycopene, ß-carotene, and lutein were quantitated in juices and the micelle fraction using high-performance liquid chromatography (HPLC)-diode array detection and in Caco-2 cells using HPLC-tandem mass spectrometry. Tomato juice results were as follows: PEF increased lycopene bioaccessibility (1.5 ± 0.39%) by 150% (P = 0.01) but reduced ß-carotene bioaccessibility (28 ± 6.2%) by 44% (P = 0.02), relative to raw juice. All processing methods increased lutein uptake. Kale-based juice results were as follows: TT and PEF degraded ß-carotene and lutein in the juice. No difference in bioaccessibility or cell uptake was observed. Total delivery, i.e., the summation of bioaccessibility and cell uptake, of lycopene, ß-carotene, and lutein was independent of type of processing. Taken together, PEF and OH enhanced total lycopene and lutein delivery from tomato juice to Caco-2 cells as well as TT, and may produce a more desirable product due to other factors (i.e., conservation of heat-labile micronutrients, fresher organoleptic profile). HPP best conserved the carotenoid content and color of kale-based juice and merits further consideration.

Characterization of Wild Blueberry Polyphenols Bioavailability and Kinetic Profile in Plasma over 24-h Period in Human Subjects.

SCOPE: Understanding the metabolic fate of polyphenols from plant foods can aid in developing dietary recommendations that maximize their health benefits. Wild blueberries (WBB) provide a distinctive composition of dietary anthocyanins and chlorogenic acid (CGA). METHODS AND RESULTS: This is a single blind, randomized, two-arm crossover controlled study. Human subjects ingested a WBB beverage (25 g freeze dried WBB powder) or placebo beverage with a meal and plasma was collected over 24 h. Anthocyanins, CGA and their metabolites were characterized and quantified in beverages and in plasma using targeted and non-targeted mass analyses. Bioavailability of WBB anthocyanins and 3-CGA was 1.1 and 0.2%, respectively. Parent anthocyanins and 3-CGA peaked ≈2 h post ingestion, while phase II metabolites, including glucuronide conjugates of peonidin, delphinidin, cyanidin and petunidin peaked ≈ 2.6, 6.3, 7 and 8.8 h, respectively. Phenolic acids (metabolites) peaked between 0.5 and 24 h. Biphasic responses were evident suggesting preferential enterohepatic recycling for some compounds. CONCLUSION: The data indicate bioavailability of early and late phase WBB metabolites peaking at different times during the 24 h period, which may be important for maximizing their biological activity.

Isolation and partial characterization of a bacteriocin produced by Lactobacillus plantarum BM-1 isolated from a traditionally fermented Chinese meat product.

Lactobacillus plantarum BM-1 isolated from a traditionally fermented Chinese meat product was found to produce a novel bacteriocin that is active against a wide range of gram-positive and gram-negative bacteria. Production of the bacteriocin BM-1 started early in the exponential phase and its maximum activity (5120 AU/mL) was recorded early during the stationary phase (16 hr). Bacteriocin BM-1 is sensitive to proteolytic enzymes but stable in the pH range of 2.0-10.0 and heat-resistant (15 min at 121°C). This bacteriocin was purified through pH-mediated cell adsorption-desorption and cation-exchange chromatography on an SP Sepharose Fast Flow column. The molecular weight of the purified bacteriocin BM-1 was determined to be 4638.142 Da by electrospray ionization Fourier transform mass spectrometry. Furthermore, the N-terminal amino acid sequence was obtained through automated Edman degradation and found to comprise the following 15 amino acid residues: H2 N-Lys-Tyr-Tyr-Gly-Asn-Gly-Val-Tyr-Val-Gly-Lys-His-Ser-Cys-Ser. Comparison of this sequence with that of other bacteriocins revealed that bacteriocin BM-1 contains the consensus YGNGV amino acid motif near the N-terminus. Based on its physicochemical characteristics, molecular weight, and N-terminal amino acid sequence, plantaricin BM-1 is a novel class IIa bacteriocin.