Comparative Studies on the Susceptibility of (<i>R</i>)-2,3-Dipalmitoyloxypropylphosphonocholine (DPPnC) and Its Phospholipid Analogues to the Hydrolysis or Ethanolysis Catalyzed by Selected Lipases and Phospholipases
Susceptibility of soybean phosphatidylcholine, 1,2-dipalmitoyl-<i>sn</i>-glycero-3-phosphocholine (DPPC) and its phosphono analogue (<i>R</i>)-2,3-dipalmitoyloxypropylphosphonocholine (DPPnC) towards selected lipases and phospholipases was compared. The ethanolysis of substra...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-01-01
|
| Series: | Catalysts |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2073-4344/11/1/129 |
| _version_ | 1797410782157209600 |
|---|---|
| author | Paweł Mituła Czesław Wawrzeńczyk Witold Gładkowski |
| author_facet | Paweł Mituła Czesław Wawrzeńczyk Witold Gładkowski |
| author_sort | Paweł Mituła |
| collection | DOAJ |
| description | Susceptibility of soybean phosphatidylcholine, 1,2-dipalmitoyl-<i>sn</i>-glycero-3-phosphocholine (DPPC) and its phosphono analogue (<i>R</i>)-2,3-dipalmitoyloxypropylphosphonocholine (DPPnC) towards selected lipases and phospholipases was compared. The ethanolysis of substrates at <i>sn</i>-1 position was carried out by lipase from <i>Mucor miehei</i> (Lipozyme<sup>®</sup>) and lipase B from <i>Candida antarctica</i> (Novozym 435) in 95% ethanol at 30 °C, and the hydrolysis with Lecitase<sup>TM</sup> Ultra was carried out in hexane/water at 50 °C. Hydrolysis at <i>sn</i>-2 position was carried out in isooctane/Tris-HCl/AOT system at 40 °C using phospholipase A<sub>2</sub> (PLA<sub>2</sub>) from porcine pancreas and PLA<sub>2</sub> from bovine pancreas or 25 °C using PLA<sub>2</sub> from bee venom. Hydrolysis in the polar part of the studied compounds was carried out at 30 °C in acetate buffer/ethyl acetate system using phospholipase D (PLD) from <i>Streptococcus</i> sp. and PLD from white cabbage or in Tris-HCl buffer/methylene chloride system at 35 °C using PLD from <i>Streptomyces chromofuscus</i>. The results showed that the presence of C-P bond between glycerol and phosphoric acid residue in DPPnC increases the rate of enzymatic hydrolysis or ethanolysis of ester bonds at the <i>sn</i>-1 and <i>sn</i>-2 position and decreases the rate of hydrolysis in the polar head of the molecule. The most significant changes in the reaction rates were observed for reaction with PLD from <i>Streptococcus</i> sp. and PLD from <i>Streptomyces chromofuscus</i> that hydrolyzed DPPnC approximately two times slower than DPPC and soybean PC. The lower susceptibility of DPPnC towards enzymatic hydrolysis by phospholipases D gives hope for the possibility of using DPPnC-like phosphonolipids as the carriers of bioactive molecules that, instead of choline, can be bounded with diacylpropylphosphonic acids (DPPnA). |
| first_indexed | 2024-03-09T04:35:11Z |
| format | Article |
| id | doaj.art-b8d761fac4b8413eb826a42dc31ed950 |
| institution | Directory Open Access Journal |
| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-09T04:35:11Z |
| publishDate | 2021-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Catalysts |
| spelling | doaj.art-b8d761fac4b8413eb826a42dc31ed9502023-12-03T13:29:12ZengMDPI AGCatalysts2073-43442021-01-0111112910.3390/catal11010129Comparative Studies on the Susceptibility of (<i>R</i>)-2,3-Dipalmitoyloxypropylphosphonocholine (DPPnC) and Its Phospholipid Analogues to the Hydrolysis or Ethanolysis Catalyzed by Selected Lipases and PhospholipasesPaweł Mituła0Czesław Wawrzeńczyk1Witold Gładkowski2Institute of Environmental Engineering, Wroclaw University of Environmental and Life Sciences, Grunwaldzki Square 24, 50-363 Wroclaw, PolandDepartment of Chemistry, Wroclaw University of Environmental and Life Sciences, Norwida 25, 50-375 Wroclaw, PolandDepartment of Chemistry, Wroclaw University of Environmental and Life Sciences, Norwida 25, 50-375 Wroclaw, PolandSusceptibility of soybean phosphatidylcholine, 1,2-dipalmitoyl-<i>sn</i>-glycero-3-phosphocholine (DPPC) and its phosphono analogue (<i>R</i>)-2,3-dipalmitoyloxypropylphosphonocholine (DPPnC) towards selected lipases and phospholipases was compared. The ethanolysis of substrates at <i>sn</i>-1 position was carried out by lipase from <i>Mucor miehei</i> (Lipozyme<sup>®</sup>) and lipase B from <i>Candida antarctica</i> (Novozym 435) in 95% ethanol at 30 °C, and the hydrolysis with Lecitase<sup>TM</sup> Ultra was carried out in hexane/water at 50 °C. Hydrolysis at <i>sn</i>-2 position was carried out in isooctane/Tris-HCl/AOT system at 40 °C using phospholipase A<sub>2</sub> (PLA<sub>2</sub>) from porcine pancreas and PLA<sub>2</sub> from bovine pancreas or 25 °C using PLA<sub>2</sub> from bee venom. Hydrolysis in the polar part of the studied compounds was carried out at 30 °C in acetate buffer/ethyl acetate system using phospholipase D (PLD) from <i>Streptococcus</i> sp. and PLD from white cabbage or in Tris-HCl buffer/methylene chloride system at 35 °C using PLD from <i>Streptomyces chromofuscus</i>. The results showed that the presence of C-P bond between glycerol and phosphoric acid residue in DPPnC increases the rate of enzymatic hydrolysis or ethanolysis of ester bonds at the <i>sn</i>-1 and <i>sn</i>-2 position and decreases the rate of hydrolysis in the polar head of the molecule. The most significant changes in the reaction rates were observed for reaction with PLD from <i>Streptococcus</i> sp. and PLD from <i>Streptomyces chromofuscus</i> that hydrolyzed DPPnC approximately two times slower than DPPC and soybean PC. The lower susceptibility of DPPnC towards enzymatic hydrolysis by phospholipases D gives hope for the possibility of using DPPnC-like phosphonolipids as the carriers of bioactive molecules that, instead of choline, can be bounded with diacylpropylphosphonic acids (DPPnA).https://www.mdpi.com/2073-4344/11/1/129phosphonolipidsphospholipidsenzymatic hydrolysislipasesphospholipases |
| spellingShingle | Paweł Mituła Czesław Wawrzeńczyk Witold Gładkowski Comparative Studies on the Susceptibility of (<i>R</i>)-2,3-Dipalmitoyloxypropylphosphonocholine (DPPnC) and Its Phospholipid Analogues to the Hydrolysis or Ethanolysis Catalyzed by Selected Lipases and Phospholipases Catalysts phosphonolipids phospholipids enzymatic hydrolysis lipases phospholipases |
| title | Comparative Studies on the Susceptibility of (<i>R</i>)-2,3-Dipalmitoyloxypropylphosphonocholine (DPPnC) and Its Phospholipid Analogues to the Hydrolysis or Ethanolysis Catalyzed by Selected Lipases and Phospholipases |
| title_full | Comparative Studies on the Susceptibility of (<i>R</i>)-2,3-Dipalmitoyloxypropylphosphonocholine (DPPnC) and Its Phospholipid Analogues to the Hydrolysis or Ethanolysis Catalyzed by Selected Lipases and Phospholipases |
| title_fullStr | Comparative Studies on the Susceptibility of (<i>R</i>)-2,3-Dipalmitoyloxypropylphosphonocholine (DPPnC) and Its Phospholipid Analogues to the Hydrolysis or Ethanolysis Catalyzed by Selected Lipases and Phospholipases |
| title_full_unstemmed | Comparative Studies on the Susceptibility of (<i>R</i>)-2,3-Dipalmitoyloxypropylphosphonocholine (DPPnC) and Its Phospholipid Analogues to the Hydrolysis or Ethanolysis Catalyzed by Selected Lipases and Phospholipases |
| title_short | Comparative Studies on the Susceptibility of (<i>R</i>)-2,3-Dipalmitoyloxypropylphosphonocholine (DPPnC) and Its Phospholipid Analogues to the Hydrolysis or Ethanolysis Catalyzed by Selected Lipases and Phospholipases |
| title_sort | comparative studies on the susceptibility of i r i 2 3 dipalmitoyloxypropylphosphonocholine dppnc and its phospholipid analogues to the hydrolysis or ethanolysis catalyzed by selected lipases and phospholipases |
| topic | phosphonolipids phospholipids enzymatic hydrolysis lipases phospholipases |
| url | https://www.mdpi.com/2073-4344/11/1/129 |
| work_keys_str_mv | AT pawełmituła comparativestudiesonthesusceptibilityofiri23dipalmitoyloxypropylphosphonocholinedppncanditsphospholipidanaloguestothehydrolysisorethanolysiscatalyzedbyselectedlipasesandphospholipases AT czesławwawrzenczyk comparativestudiesonthesusceptibilityofiri23dipalmitoyloxypropylphosphonocholinedppncanditsphospholipidanaloguestothehydrolysisorethanolysiscatalyzedbyselectedlipasesandphospholipases AT witoldgładkowski comparativestudiesonthesusceptibilityofiri23dipalmitoyloxypropylphosphonocholinedppncanditsphospholipidanaloguestothehydrolysisorethanolysiscatalyzedbyselectedlipasesandphospholipases |