Stabilization of Candida rugosa lipase during transacetylation with vinyl acetate.
An optimally prepared Candida rugosa lipase aggregate cross-linked with bovine serum albumin, was found to overcome acetaldehyde deactivation during transacetylation of a series of benzyl alcohols with vinyl acetate. The formulation, under the same reaction conditions, exhibited 4-30x enhancement in the reaction rate as compared to the celite immobilized lyophilized formulation and 25-133x enhancement as compared to the free lyophilized enzyme depending upon the alcohol chosen. The racemic 1-phenylethanol, taken as one of the alcohols, underwent a more efficient enantioselective transacetylation giving 80% enantiomeric excess of the product, (R)-1-phenylethyl acetate, at 38% conversion (E = 15) within 24h while the enzyme immobilized on celite gave 83% enantiomeric excess at 18% conversion (E = 13) during the same period of time.
Majumder
Abir B
AB
Chemistry Department, Indian Institute of Technology Delhi, Hauz Khas, New Delhi 110 016, India.
Gupta
Munishwar N
MN
D000107:Acetylation; D002175:Candida / Q000201:enzymology*; D008049:Lipase / Q000378:metabolism*; D014753:Vinyl Compounds / Q000378:metabolism*
D014753:Vinyl Compounds; D008049:Lipase; C011566:vinyl acetate