Yassin Atif A A, Mohamed Ibrahim O, Ibrahim Mohd N, Yusoff Mohd S A
Department of Process and Food Engineering, Faculty of Engineering, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia.
Appl Biochem Biotechnol. 2003 Jul;110(1):45-52. doi: 10.1385/abab:110:1:45.
Immobilized PS-C 'Amano' II lipase was used to catalyze the interesterification of palm olein (POo) with 30, 50, and 70% stearic acid in n-hexane at 60 degrees C. The catalytic performance of the immobilized lipase was evaluated by determining the composition change of fatty acyl groups and triacylglycerol (TAG) by gas liquid chromatography and high-performance liquid chromatography, respectively. The interesterification process resulted in the formation of new TAGs, mainly tripalmitin and dipalmitostearin, both of which were absent in the original oil. These changes in TAG composition resulted in an increase in slip melting point, from the original 25.5 degrees C to 36.3, 37.0, and 40.0 degrees C in the modified POo with 30, 50, and 70% stearic acid, respectively. All the reactions attained steady state in about 6 h. This type of work will find great applications in food industries, such as confectionery.
固定化PS-C“天野”II脂肪酶用于催化棕榈油精(POo)与30%、50%和70%硬脂酸在正己烷中于60℃下进行酯交换反应。分别通过气相色谱法和高效液相色谱法测定脂肪酰基和三酰甘油(TAG)的组成变化,以评估固定化脂肪酶的催化性能。酯交换过程导致形成了新的TAG,主要是三棕榈酸甘油酯和二棕榈酸硬脂酸甘油酯,这两种物质在原始油脂中均不存在。TAG组成的这些变化导致熔点升高,在分别含有30%、50%和70%硬脂酸的改性POo中,熔点从原始的25.5℃分别升高到36.3℃、37.0℃和40.0℃。所有反应在约6小时内达到稳态。这类工作将在食品工业(如糖果业)中得到广泛应用。