Lipase-catalyzed N-acylations of beta-amino alcohols such as ethanolamine and L-serine were investigated. To prepare N-acyl derivatives by taking advantage of the acyl migration, we first carried out a screening of suitable enzymes for the desired reaction. As a result, we found a higher activity far N-acylation with Lipase QL. This lipase had higher hydrolytic activity for the O-acyl compound but not the N-acyl compound The observation shows that N-acylation results from the esterification and successive acyl migration into the amino group. Using Lipase QL, we then investigated the N-acylation of ethanolamine or L-serine with fatty acids as acyl donors. The reaction parameters for the N-acylation were clarified.