Reaction selectivity of <Emphasis Type="Italic">Burkholderia cepacia</Emphasis> (PS-30) lipase as influenced by monoacylation of <Emphasis Type="Italic">sn</Emphasis>-glycerol |
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Authors: | Xun?Fu Email author" target="_blank">Kirk?L?ParkinEmail author |
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Affiliation: | (1) Department of Food Science, University of Wisconsin, Babcock Hall, 1605 Linden Dr., 53706 Madison, WI;(2) Present address: School of Pharmacy, University of Wisconsin, Rennebohm Hall, 777 Highland Ave., 53705 Madison, WI |
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Abstract: | Reaction selectivities were determined in multicompetitive reactions mediated by Burkholderia cepacia lipase (Amano PS-30) at a water activity of 0.19 in hexane. Saturated FA (C4–C18 even chain) and oleic acid (C18∶1) were
reacted with a single alcohol, glycerol, α-or β-MAG, containing C4, C10, C16, or C18∶1 individually as alcohol cosubstrate.
Similar odrinal patterns of FA selectivity, with C8, C10, and C16 preferred over others, were generally observed for incorporation
of FA into specific acylglycerol (AG) pools of the 24 specific cases evaluated. The three exceptions were enrichment of C14
and C18 in the MAG pool with α-C16-MAG, substrate, and a general suppression of >C8 incorporation into the TAG pool for reactions
with α-C10- and α-C16-MAG. PS-30 lipase selectivity toward MAG was in descending order: α/β-C4-MAG>β-C10-MAG>β-C16-MAG>α/β-C18∶1-MAG>α-C10-MAG>α-C16-MAG.
Selectivity in channeling CX of the original CX-MAG substrates into higher AG species was in descending order: α-C10-MAG∼α-C16-MAG>α-C18∶1-MAG>β-C10-MAG∼β-C16-MAG∼β-C18∶1-MAG
>α/β-C4-MAG. Generally, MAG were better acyl donors than FA for esterification reactions leading to DAG formation. These observations
are relevant to the design of biocatalytic processes intended to yield specifically structured TAG. |
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Keywords: | Burkholderia cepacia esterification fatty acid lipase monoacylglycerol selectivity |
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