98524-19-7Relevant articles and documents
Stereospecific production of 9R-hydroxy-10E,12Z-octadecadienoic acid from linoleic acid by recombinant Escherichia coli cells expressing 9R-lipoxygenase from Nostoc sp. SAG 25.82
Kim, Kyoung-Rok,Seo, Min-Ho,Park, Jin-Byung,Oh, Deok-Kun
, p. 56 - 63 (2014/05/06)
One of the most significant properties of lipoxygenase (LOX) as a biocatalyst is its stereo-selective oxygenation. In this study, the stereo-specific production of 9R-hydroxy-10E,12Z-octadecadienoic acid (9R-HODE) from linoleic acid was achieved using whole recombinant Escherichia coli cells expressing LOX from Nostoc sp. SAG 25.82. The optimal conditions for the production of 9R-HODE were pH 7.5, 25 °C, 40 g l-1 cells, 15 g l-1 linoleic acid, 2% (v/v) methanol, 1 working volume/oxygen volume/min (vvm) oxygenation rate, and 250 rpm agitation speed in 500 ml-baffled flask containing a working volume of 50 ml. Under these optimized conditions, whole recombinant cells expressing 9R-LOX protein produced 14.3 g l-1 9R-HODE for 1 h, with a conversion yield of 95% (w/w) and a productivity of 14.3 g l-1 h-1. The oxygen supply method significantly influenced stereo- and regio-selectivity of the oxygenation of linoleic acid. Among the oxygen supply methods tested, oxygenation (1 vvm) with agitation (250 rpm) resulted in the highest 9R/13S-HODE ratio of the products at 96:4. This is the first application using whole recombinant cells harboring R-specific LOX for the stereo-selective production of an R-specific hydroxy fatty acid.
Lipase Catalysed Regio- and Enantio-selective Hydrolysis: Molecular Recognition Phenomenon and Synthesis of (R)-Dimorphecolic Acid
Bhalerao, U. T.,Dasaradhi, L.,Neelakantan, P.,Fadnavis, N. W.
, p. 1197 - 1198 (2007/10/02)
Molecular recognition has been observed in hydrolysis of racemic esters of (E)-9=acetoxy-11-bromoundec-10-enoic acid by a lipase of Candida cylindracea (E.C. 3.1.1.3) where optically active (R)-(E)-9-acetoxy-11-bromoundec-10-enoic acid 99percent> was obtained which was used in synthesis of (R)-dimorphecolic acid.