Herein, we prepared 1,3-dipalmitoyl-2-oleoyl glycerol (POP)-rich fats with reduced levels of diacylglycerols (DAGs), adversely affecting the tempering of chocolate, via two-step hexane fractionation of palm stearin. DAG content in the as-prepared fats was lower than that in POP-rich fats obtained by previously reported conventional two-step acetone fractionation. Cocoa butter equivalents (CBEs) were fabricated by blending the as-prepared fats with 1,3-distearoyl-2-oleoyl glycerol (SOS)-rich fats obtained by hexane fractionation of degummed shea butter. POP-rich fats achieved under the best conditions for the fractionation of palm stearin had a significantly lower DAG content (1.6 w/w%) than that in the counterpart (4.6 w/w%) prepared by the previously reported method. The CBEs fabricated by blending the POP- and SOS-rich fats in a weight ratio of 40:60 contained 63.7 w/w% total symmetric monounsaturated triacylglycerols, including 22.0 w/w% POP, 8.6 w/w% palmitoyl-2-oleoyl-3-stearoyl-rac-glycerol, 33.1 w/w% SOS, and 1.3 w/w% DAGs, which was not substantially different from the DAG content in cocoa butter (1.1 w/w%). Based on the solid-fat content results, it was concluded that, when these CBEs were used for chocolate manufacture, they blended with cocoa butter at levels up to 40 w/w%, without distinctively altering the hardness and melting behavior of cocoa butter.
This study sought to prepare a cognitive
enhancer l-α-glycerylphosphorylcholine
(l-α-GPC) using an immobilized Lecitase Ultra (LU,
phospholipase A1) to catalyze the hydrolysis of soy phosphatidylcholine
(PC). Immobilization of LU on Lewatit VP OC 1600 provided the highest
fixation level (83.1 g/100 g) and greatest catalytic activity achieving
100 g/100 g l-α-GPC within 20 h and was therefore selected
as the optimal system for biocatalysis. Immobilization of LU increased
its positional specificity compared to free LU, as shown by a decrease
in the production of the phosphocholine byproduct. Under the optimal
conditions determined by response surface methodology, PC was completely
hydrolyzed to l-α-GPC and required a simple purification
via phase separation of the biphasic media to obtain a yield of ∼26.4
g l-α-GPC from 100 g PC, with a purity of 98.5 g/100
g. Our findings suggest a possibility of using the immobilized LU
as a new biocatalyst for the l-α-GPC production.
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