Enzymatic asymmetrization of prochiral 2-benzyl-1,3-propanediol through esterification in solvent media

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DOIResolve DOI: http://doi.org/10.1023/A:1005644005243
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TypeArticle
Journal titleBiotechnology Letters
Volume22
Issue8
Pages709713; # of pages: 5
AbstractThe enzymatic esterification of the prochiral substrate, 2-benzyl-1,3-propanediol, has been studied in solvent media. Among the five tested lipases, Lipozyme and Novozym 435 led to higher reaction rates. Novozym 435 catalyzed faster reactions at low water activity and in solvents having log P above 2. However, the two positions of the diol, pro-(R) and pro-(S), led to the same reaction rate trends and no prochiral selectivity was obtained. When using Lipozyme in toluene, the reaction rates for the formation of both (R) and (S) products presented an optimum at a water activity of 0.22. In this case, the prochiral selectivity increased with the water activity, from a value of 5 at aw aw = 0.22, at which point it remained constant.
Publication date
AffiliationNational Research Council Canada; NRC Biotechnology Research Institute
Peer reviewedNo
NPARC number12330129
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Record identifier5cf860a2-8af0-4baa-804d-862da1bc97bb
Record created2009-09-10
Record modified2016-05-09
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