SURFACTANT-MODIFIED LIPASE FOR THE CATALYSIS OF THE INTERESTERIFICATION OF TRIGLYCERIDES AND FATTY-ACIDS

The lipase-catalyzed interesterification of triglycerides and fatty ac ids in n-hexane was studied. Initially, lipase Saiken was modified wit h a surfactant of sorbitan esters so that its dispersibility in hydrop hobic organic media was improved. The surfactant-modified lipase forme d in the modification process carried out in a buffer solution has 1,3 -positional specificity and predominantly catalyzed the interesterific ation reaction in a microaqueous n-hexane system. The modification tec hnique converted inactive lipases to very active biocatalysts for the interesterification of triglycerides and fatty acids. The pH and the w eight ratio of surfactant to enzyme used during the lipase modificatio n process have shown significant effects in determining the recoveries of the protein and enzyme activity from the buffer solution, the prot ein content of the modified lipase complex after being freeze dried, a nd the interesterification activity of the complex. The water content in the reaction solution has strongly influenced the enzyme activity a s well as the distribution of the products. (C) 1995 John Wiley and So ns, Inc.