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 24 h while the enzyme immobilized on celite gave 83% enantiomeric excess at 18% conversion (E=13) during the same period of time. (C) 2009 Elsevier Ltd. All rights reserved.