Abstract
Lipase (triacylglycerol acylhydolase) hydrolyzes ester bonds between glycerol and fatty acid of triacylglycerol. Interesterification and ester synthesis by immobilized lipase is carried out in the oils and fats industry.
Basic characteristics of commercially available immobilized (with anion-exchange regin) 1, 3-specific lipase from Rizomucor miehei (Lipozyme RM IM) were investigated and found to be influenced by water contents, reaction temperature, reaction mixture organic solvents differences in alcohol (chain length and primary/secondary) as substrate and carrier particle size. Heat stability of immobilized lipase increased significantly and halflife-time in the column was 1600 hrs.
Candida antarctica lipase B was immobilized with a less expensive silica based carrier. The performance of ester synthesis was compared with a commercial product immobilized with macroporous acrylic resin (Novozyme 435). The ester synthesis of 4 industrially important materials has been conducted and of these, the silica based immobilized material showed the poorest performance. The selection of carrier is thus important.
An 1, 3-specific lipase of Thermomyces lanuginosus produced by genetically modified microorganism with very high enzyme yield was immobilized with the silica based material and its performance for margarine interesterification was assessed. Due to 1, 3 specificity, more fatty acid at 2nd-position of original fat was noted to remain at the same position in contrast to chemical method. The solid fat content was essentially the same for the products produced by the two methods, thus indicating that the enzymatic method alone can be used.
Features of immobilized lipases are presented.
