Ascorbyl palmitate synthesis in an organic solvent system using a Celite-immobilized commercial lipase (Lipolase 100L).
Ascorbyl palmitate was synthesized using a Celite-immobilized commercial lipase (Lipolase 100L) in dimethylsulfoxide (DMSO) as an organic solvent system. Lipase immobilized by surface adsorption onto Celite 545 matrix and subsequently exposed to 1 % glutaraldehyde showed 75 % binding of protein. The Celite-bound lipase was optimally active at 75 °C and pH 8.5 under shaking and showed maximum hydrolytic activity toward p-NPP as a substrate. The bound lipase was found to be stimulated only in the presence of Al3+and EDTA. All surfactants (Tween-20, Tween-80 and Triton X-100) had an inhibitory effect on lipase activity. The optimization of various reaction conditions of ascorbyl palmitate was achieved considering one factor at a time. The esterification of ascorbic acid and palmitic acid was carried out with 1 M ascorbic acid and 2.5 M palmitic acid in DMSO at 75 °C for 18 h under shaking (120 rpm). Molecular sieves had an important effect on the ester synthesis resulting in an enhanced yield. The by-product (H2O) produced in the reaction was scavenged by the molecular sieves (20 mg/ml) added in the reaction mixture which enhanced the ester yield to 80 %. The characterization of synthesized ester was done through FTIR spectroscopy.
Department of Biotechnology, Himachal Pradesh University, Summer Hill, Shimla, 171 005, India. shivikasharma25@gmail.com.
Shivika
S
Sharma
Department of Biotechnology, Himachal Pradesh University, Summer Hill, Shimla, 171 005, India.
Kriti
K
Kanwar
Department of Biotechnology, Himachal Pradesh University, Summer Hill, Shimla, 171 005, India.
Shamsher S
SS
Kanwar
Ascorbyl palmitate synthesis; Celite; Glutaraldehyde; Lipase; Molecular sieves