Development of zero-trans shortenings with high thermo-oxidative stability by enzymatic transesterification

Novel zero-trans frying shortenings were formed by enzymatic transesterification by exploring a palm stearin and canola oil mixture and stearic acid as substrates. Both immobilized (Novozym 435, Lipase PS “Amano” IM) and non-immobilized (Lipomod TM 34P) enzymes were applied as biocatalysts. Palmitic acid, the fatty acid which defines the proper type of crystal formation, was present at the 15% level in the reaction mixtures. The novel structured lipids had comparable physical properties and offered similar frying performance to those of commercial shortening. Needle-shaped crystals were predominant both in the transesterification products and the commercial frying shortening. Furthermore, solid fat content profiles of the zero-trans structured lipids produced by Novozym 435 and Lipase PS “Amano” IM were close to those of the commercial shortening.

Synthesis of L-Ascorbyl Flurbiprofenate by Lipase-Catalyzed Esterification and Transesterification Reactions

The synthesis of L-ascorbyl flurbiprofenate was achieved by esterification and transesterification in nonaqueous organic medium with Novozym 435 lipase as biocatalyst. The conversion was greatly influenced by the kinds of organic solvents, speed of agitation, catalyst loading amount, reaction time, and molar ratio of acyl donor to L-ascorbic acid. A series of solvents were investigated, and tert-butanol was found to be the most suitable from the standpoint of the substrate solubility and the conversion for both the esterification and transesterification. When flurbiprofen was used as acyl donor, 61.0% of L-ascorbic acid was converted against 46.4% in the presence of flurbiprofen methyl ester. The optimal conversion of L-ascorbic acid was obtained when the initial molar ratio of acyl donor to ascorbic acid was 5 : 1. kinetics parameters were solved by Lineweaver-Burk equation under nonsubstrate inhibition condition. Since transesterification has lower conversion, from the standpoint of productivity and the amount of steps required, esterification is a better method compared to transesterification.

Chemoenzymatic Epoxidation of α-Pinene Catalyzed by Novozym 435

The synthesis of α-pinene oxide mediated by Novozym 435 (lipase from Candida antarctica) in a three-phase system was studied in this work. Novozyme 435 catalysed the formation of peroxyoctanoic acid directly from octanoic acid and hydrogen peroxide, which was then applied for in situ oxidation of α-pinene. The highest conversion of a-pinene (approximately 80%) was obtained when the reaction was performed at 30°C and initial hydrogen peroxide concentration in the water phase was set to be 30%. The parameters affecting the lipase activity were also investigated，where the peracid generated in organic phase was obvserved to greatly inactivate the enzyme compared to other components in the organic phase.