Dataset Information

Quantitative analysis of mycosporine-like amino acids in marine algae by capillary electrophoresis with diode-array detection.

ABSTRACT: Marine species have evolved a variety of physical or chemical strategies to diminish damage from elevated environmental ultraviolet radiation. Mycosporine-like amino acids, a group of widely distributed small water soluble compounds, are biologically relevant because of their photo-protective potential. In addition, presumed antioxidant and skin protective strategies raise the interest for possible medicinal and cosmetic applications. In this study the first CE method for the quantification of mycosporine-like amino acids in marine species is presented. A borate buffer system consisting of 30mM sodium tetraborate in water at a pH-value of 10.3 enabled the baseline separation of five MAAs, namely palythine, mycosporine-serinol, asterina-330, shinorine and porphyra-334, in 27min. Separation voltage, temperature and detection wavelength were 25kV, 25°C and 320nm, respectively. The optimized method was fully validated and applied for the quantitative determination of MAAs in the marine macroalgae Palmaria palmata, Porphyra umbilicalis, and Porphyra sp., as well as the lichen Lichina pygmaea.

SUBMITTER: Hartmann A

PROVIDER: S-EPMC5388179 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Quantitative analysis of mycosporine-like amino acids in marine algae by capillary electrophoresis with diode-array detection.

Hartmann Anja A Murauer Adele A Ganzera Markus M

Journal of pharmaceutical and biomedical analysis 20170204

Marine species have evolved a variety of physical or chemical strategies to diminish damage from elevated environmental ultraviolet radiation. Mycosporine-like amino acids, a group of widely distributed small water soluble compounds, are biologically relevant because of their photo-protective potential. In addition, presumed antioxidant and skin protective strategies raise the interest for possible medicinal and cosmetic applications. In this study the first CE method for the quantification of m ...[more]

PMID: 28213175

Similar Datasets

Project description:BackgroundMycosporine-like amino acids (MAAs), including shinorine and porphyra-334, are gaining attention as safe natural sunscreens. The production of MAAs has been achieved in diverse microbial hosts, including Saccharomyces cerevisiae. While S. cerevisiae is the most extensively studied model yeast, the oleaginous yeast Yarrowia lipolytica has emerged as a promising candidate for the synthesis of valuable products. In this study, we explored the potential of Y. lipolytica as a host for producing MAAs, utilizing its advantages such as a robust pentose phosphate pathway flux and versatile carbon source utilization.ResultsWe produced MAAs in Y. lipolytica by introducing the MAA biosynthetic genes from cyanobacteria Nostoc punctiforme and Anabaena variabilis. These genes include mysA, mysB, and mysC responsible for producing mycosporine-glycine (MG) from sedoheptulose 7-phosphate (S7P). The two strains utilize different enzymes, D-Ala-D-Ala ligase homologue (MysD) in N. punctiforme and NRPS-like enzyme (MysE) in A. variabilis, for amino acid conjugation to MG. MysE specifically generated shinorine, a serine conjugate of MG, while MysD exhibited substrate promiscuity, yielding both shinorine and a small amount of porphyra-334, a threonine conjugate of MG. We enhanced MAAs production by selecting mysA, mysB, and mysC from A. variabilis and mysD from N. punctiforme based on their activities. We further improved production by strengthening promoters, increasing gene copies, and introducing the xylose utilization pathway. Co-utilization of xylose with glucose or glycerol increased MAAs production by boosting the S7P pool through the pentose phosphate pathway. Overexpressing GND1 and ZWF1, key genes in the pentose phosphate pathway, further enhanced MAAs production. The highest achieved MAAs level was 249.0 mg/L (207.4 mg/L shinorine and 41.6 mg/L of porphyra-334) in YP medium containing 10 g/L glucose and 10 g/L xylose.ConclusionsY. lipolytica was successfully engineered to produce MAAs, primarily shinorine. This achievement involved the introduction of MAA biosynthetic genes from cyanobacteria, establishing xylose utilizing pathway, and overexpressing the pentose phosphate pathway genes. These results highlight the potential of Y. lipolytica as a promising yeast chassis strain for MAAs production, notably attributed to its proficient expression of MysE enzyme, which remains non-functional in S. cerevisiae, and versatile utilization of carbon sources like glycerol.

Dataset Information

Quantitative analysis of mycosporine-like amino acids in marine algae by capillary electrophoresis with diode-array detection.

Publications

Quantitative analysis of mycosporine-like amino acids in marine algae by capillary electrophoresis with diode-array detection.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets