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Oxidative demethylation of algal carbohydrates by cytochrome P450 monooxygenases.

In Nature Chemical Biology on 1 April 2018 by Reisky, L., Büchsenschütz, H. C., et al.

Sugar O-methylation shields algal polysaccharides against microbial hydrolytic enzymes. Here, we describe cytochrome P450 monooxygenases from marine bacteria that, together with appropriate redox-partner proteins, catalyze the oxidative demethylation of 6-O-methyl-D-galactose, which is an abundant monosaccharide of the algal polysaccharides agarose and porphyran. This previously unknown biological function extends the group of carbohydrate-active enzymes to include the class of cytochrome P450 monooxygenases.

Glucaminium-based ionic liquids are a new class of solvents capable of extracting boron-species from water with high efficiency. The complexation behavior of these ILs with borate was thoroughly studied using (11)B NMR. Two different complexes, namely, monochelate complex and bischelate complex, were observed. (11)B NMR was used extensively to determine the formation constants for monochelate and bischelate complexes. The IL concentration was observed to have a significant effect on the IL-borate complexes. Using an in situ dispersive liquid-liquid microextraction (in situ DLLME) method, the extraction efficiency for boron species was increased dramatically when lithium bis[(trifluoromethyl)sulfonyl]imide (LiNTf(2)) was used as the metathesis salt in an aqueous solution containing 0.1M sodium chloride. IL regeneration after extraction was achieved using 0.1M hydrochloric acid. The extraction efficiency of boron species was consistent when the IL was employed after three regeneration cycles. The selectivity of the IL for boron species in synthetic seawater samples was similar to performing the same extraction from Milli-Q water samples.
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