2016
DOI: 10.1007/s13205-016-0486-7
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Ascorbyl palmitate synthesis in an organic solvent system using a Celite-immobilized commercial lipase (Lipolase 100L)

Abstract: 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… Show more

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Cited by 11 publications
(5 citation statements)
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“…HK‐2 cells (human proximal endothelial cells) were cultured in medium (Opti‐MEM, Manassa, VA, USA) with epidermal growth factor human recombinant and bovine pituitary extract. Palmitate (P0500; Sigma, St. Louis, MO, USA) was dissolved in 0.1% dimethyl sulfoxide into final stock concentration 10 mmol/L, and dimethyl sulfoxide was used as the control. In the presence or absence of SGLT2 inhibitor or small interfering ribonucleic acid (siRNA)‐mediated knockdown of SGLT2, palmitate (adjusted to 150 μmol/L) or high glucose (30 mmol/L) were incubated in media for 48 h.…”
Section: Methodsmentioning
confidence: 99%
“…HK‐2 cells (human proximal endothelial cells) were cultured in medium (Opti‐MEM, Manassa, VA, USA) with epidermal growth factor human recombinant and bovine pituitary extract. Palmitate (P0500; Sigma, St. Louis, MO, USA) was dissolved in 0.1% dimethyl sulfoxide into final stock concentration 10 mmol/L, and dimethyl sulfoxide was used as the control. In the presence or absence of SGLT2 inhibitor or small interfering ribonucleic acid (siRNA)‐mediated knockdown of SGLT2, palmitate (adjusted to 150 μmol/L) or high glucose (30 mmol/L) were incubated in media for 48 h.…”
Section: Methodsmentioning
confidence: 99%
“…Santibañez, et al [20] used the enzyme immobilized in octyl-agarose obtaining a synthesis conversion of 57% at an AA:PA molar ratio of 1:5, using tert-butanol as solvent. Sharma, et al [22] evaluated the esterification of AA with PA, using 1 M AA and 2.5 M PA in dimethyl sulfoxide (DMSO) at 75 °C for 18 h, reaching 80% of synthesis conversion using the commercial lipase Lipolase 100 L. Recently, synthesis of AsPa in tert-butyl alcohol was carried out using immobilized lipase from Candida antarctica B at optimized reaction conditions obtaining in conversion of 90% [23]. Despite several studies have been published in this topic, there are no reports about the combined effect of higher AA:PA molar ratios and temperature, neither the evaluation of the influence of more polar solvents on the enzymatic performance in AsPa production, which could lead to high synthesis yield under softer reaction conditions.…”
Section: Introductionmentioning
confidence: 99%
“…(Thirunavukarasu et al, 2008). Tween 20 also increases the production of Bacillus altitudinis AP-MSU esterases (Palanichamy et al, 2012), but inhibition of lipase activity is detected in the presence of surfactants (Tween-20, Tween-80 and Triton X-100) tested on Celite-immobilized commercial lipase (Lipolase 100 L) (Sharma et al, 2016). It was also noted that lipases produced by Pseudomonas aeruginosa HFE733 are activated by beta-mercaptoethanol and cysteine (Jun et al, 2018).…”
Section: Effect Of Metal Ions and Additives On Lipase Activitymentioning
confidence: 99%