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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5002271/ https://www.ncbi.nlm.nih.gov/pubmed/28330255 http://dx.doi.org/10.1007/s13205-016-0486-7 |
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author | Sharma, Shivika Kanwar, Kriti Kanwar, Shamsher S. |
author_facet | Sharma, Shivika Kanwar, Kriti Kanwar, Shamsher S. |
author_sort | Sharma, Shivika |
collection | PubMed |
description | 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 Al(3+) 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 (H(2)O) 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. |
format | Online Article Text |
id | pubmed-5002271 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-50022712016-08-29 Ascorbyl palmitate synthesis in an organic solvent system using a Celite-immobilized commercial lipase (Lipolase 100L) Sharma, Shivika Kanwar, Kriti Kanwar, Shamsher S. 3 Biotech Original Article 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 Al(3+) 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 (H(2)O) 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. Springer Berlin Heidelberg 2016-08-27 2016-12 /pmc/articles/PMC5002271/ /pubmed/28330255 http://dx.doi.org/10.1007/s13205-016-0486-7 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Original Article Sharma, Shivika Kanwar, Kriti Kanwar, Shamsher S. Ascorbyl palmitate synthesis in an organic solvent system using a Celite-immobilized commercial lipase (Lipolase 100L) |
title | Ascorbyl palmitate synthesis in an organic solvent system using a Celite-immobilized commercial lipase (Lipolase 100L) |
title_full | Ascorbyl palmitate synthesis in an organic solvent system using a Celite-immobilized commercial lipase (Lipolase 100L) |
title_fullStr | Ascorbyl palmitate synthesis in an organic solvent system using a Celite-immobilized commercial lipase (Lipolase 100L) |
title_full_unstemmed | Ascorbyl palmitate synthesis in an organic solvent system using a Celite-immobilized commercial lipase (Lipolase 100L) |
title_short | Ascorbyl palmitate synthesis in an organic solvent system using a Celite-immobilized commercial lipase (Lipolase 100L) |
title_sort | ascorbyl palmitate synthesis in an organic solvent system using a celite-immobilized commercial lipase (lipolase 100l) |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5002271/ https://www.ncbi.nlm.nih.gov/pubmed/28330255 http://dx.doi.org/10.1007/s13205-016-0486-7 |
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