Effect of visible light on catalytic hydrolysis of p-nitrophenyl palmitate by the Pseudomonas cepacia lipase immobilized on sol–gel support

Ganasen, Ponnarasy; Khan, Maksudur R.; Kalam, Md. Abul; Mahmud, Mohd Sabri

doi:10.1007/s00449-014-1213-6

Cited by 2 publications

(3 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It was also revealed that LPC had the highest catalytic activity in this assay with a distinct hyperbolic curve compared to the other esterases and LPL, releasing 8 nmols 4-nitrophenol in 30 min (Figure 2C,D). Ganasen et al studied the hydrolysis of 4-nitrophenyl palmitate with LPC on an immobilized support, at various substrate concentrations, and determined the hyperbolic curves of activity for all substrate concentrations, which are similar to our findings (Figure 2B) [30].…”

Section: Hydrolysis Of 4-nitrophenyl Palmitate Mediated By Esterases ...supporting

confidence: 88%

Evaluation of the Impact of Esterases and Lipases from the Circulatory System against Substrates of Different Lipophilicity

Lam

Ilies

2022

IJMS

View full text Add to dashboard Cite

Esterases and lipases can process amphiphilic esters used as drugs and prodrugs and impact their pharmacokinetics and biodistribution. These hydrolases can also process ester components of drug delivery systems (DDSs), thus triggering DDSs destabilization with premature cargo release. In this study we tested and optimized assays that allowed us to quantify and compare individual esterase contributions to the degradation of substrates of increased lipophilicity and to establish limitations in terms of substrates that can be processed by a specific esterase/lipase. We have studied the impact of carbonic anhydrase; phospholipases A1, A2, C and D; lipoprotein lipase; and standard lipase on the hydrolysis of 4-nitrophenyl acetate, 4-nitrophenyl palmitate, DGGR and POPC liposomes, drawing structure–property relationships. We found that the enzymatic activity of these proteins was highly dependent on the lipophilicity of the substrate used to assess them, as expected. The activity observed for classical esterases was diminished when lipophilicity of the substrate increased, while activity observed for lipases generally increased, following the interfacial activation model, and was highly dependent on the type of lipase and its structure. The assays developed allowed us to determine the most sensitive methods for quantifying enzymatic activity against substrates of particular types and lipophilicity.

show abstract

Section: Hydrolysis Of 4-nitrophenyl Palmitate Mediated By Esterases ...supporting

confidence: 88%

Evaluation of the Impact of Esterases and Lipases from the Circulatory System against Substrates of Different Lipophilicity

Lam

Ilies

2022

IJMS

View full text Add to dashboard Cite

show abstract

“…The study showed an enhancement in the enzyme activity due to the conformational changes that occurred in the α‐amylase when the protein was illuminated with visible polarized and non‐polarized light. Moreover, in our recent study, we reported that Pseudomonas cepacia lipase can accelerate the rate of hydrolysis of p‐ nitrophenyl palmitate in the presence of visible light irradiation . However, as far as the authors are concerned, no one has reported the lipase catalyzed esterification reactions under the influence of light.…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, in our recent study, we reported that Pseudomonas cepacia lipase can accelerate the rate of hydrolysis of p-nitrophenyl palmitate in the presence of visible light irradiation. [15] However, as far as the authors are concerned, no one has reported the lipase catalyzed esterification reactions under the influence of light. Therefore, the purpose of our current study is to explore the effect of light on the esterification reactions MONTH 2019 THE CANADIAN JOURNAL OF CHEMICAL ENGINEERING 1 catalyzed by Pseudomonas cepacia lipase.…”

Section: Introductionmentioning

confidence: 99%

Effect of light irradiation on esterification of oleic acid with ethanol catalyzed by immobilized Pseudomonas cepacia lipase

et al. 2019

Self Cite

View full text Add to dashboard Cite

The present study demonstrates the effect of light irradiation on the esterification of oleic acid catalyzed by immobilized Pseudomonas cepacia lipase. The reaction rates of all the experiments under light irradiation were found to be higher than dark conditions. The kinetics of reactions supported the Ping‐Pong Bi‐Bi mechanism with dead end inhibition by both the alcohol and acid substrates. Moreover, circular dichroism (CD) spectroscopy was used to analyze the effect of light on lipase enzyme. The CD spectroscopic studies confirmed that the conformational changes in the secondary structure of the lipase enzyme increased the reaction rate of light‐illuminated experiments, which might have opened up the active sites of enzymes and thus, resulted in higher reaction rates compared to dark reactions. These results have successfully demonstrated that the light illumination positively influenced the rate of P. cepacia enzyme‐catalyzed esterification reactions.

show abstract

Effect of visible light on catalytic hydrolysis of p-nitrophenyl palmitate by the Pseudomonas cepacia lipase immobilized on sol–gel support

Cited by 2 publications

References 18 publications

Evaluation of the Impact of Esterases and Lipases from the Circulatory System against Substrates of Different Lipophilicity

Evaluation of the Impact of Esterases and Lipases from the Circulatory System against Substrates of Different Lipophilicity

Effect of light irradiation on esterification of oleic acid with ethanol catalyzed by immobilized Pseudomonas cepacia lipase

Contact Info

Product

Resources

About