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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Lipase specificity toward some acetylenic and olefinic alcohols in the esterification of pentanoic and stearic acids.

The esterification of five medium- and long-chain acetylenic alcohols (2-nonyn-1-ol, 10-undecyn-1-ol, 6-octadecyn-1-ol, 9-octadecyn-1-ol, and 13-docosyn-1-ol), seven olefinic alcohols (cis-3-nonen-1-ol, 10-undecen-1-ol, cis-6-octadecen-1-ol, cis-9-octadecen-1-ol, trans-9-octadecen-1-ol, trans-9, trans-11-octadecadien-1-ol, cis-9,cis-12-octadecadien-1-ol), and four short-chain unsaturated alcohols (allyl alcohol, 3-butyn-1-ol, 3-pentyn-1-ol, and cis-2-penten-1-ol) with pentanoic or stearic acid in the presence of various lipase preparations was studied. With the exception of 2-nonyn-1-ol, where Lipase AY-30 (Candida rugosa) was used as the biocatalyst, the esterification of C11, C18, and C22 acetylenic alcohols with pentanoic acid appeared to be generally unaffected by the presence of an acetylenic bond in the alcohol as relatively high yields of the corresponding esters (78-97%) were obtained. However, medium- and long-chain olefinic alcohols were discriminated by Lipase AY-30, Lipolase 100T (Rhizomucor miehei), and especially by porcine pancreatic lipase ( PPL), when esterification was conducted with pentanoic acid. Esterification of medium- and long-chain acetylenic or olefinic alcohols with a long-chain fatty acid, stearic acid, was very efficient except when Lipase AY-30 and Lipolase 100T were used. Short-chain unsaturated alcohols were much more readily discriminated. 3-Pentyn-1-ol and 3-butyn-1-ol were difficult (<5% yield) to esterify with pentanoic or stearic acid in the presence of Lipase AY-30 and PPL, respectively. Very low yields (<26%) of esters were produced when 3-butyn-1-ol and 3-pentyn-1-ol were reacted with pentanoic or stearic acid, when catalyzed by lipase from Candida cylindracea. No reaction took place between 3-butyn-1-ol and stearic acids in the presence of Lipase AY-30. Esterification of short-chain acetylenic and olefinic alcohols was most efficiently achieved with Lipolase 100T (Rhizomucor miehei), Lipozyme IM20 (Rh. miehei), or Novozyme 435 (Candida antarctica) as the biocatalyst.[1]


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