Development and characterization of enzymatic biosensor based on lipase from porcine pancreas for propylparaben detection

Purpose The purpose of this paper is to study the immobilization of porcine pancreatic lipase (PPL), in an organic matrix by a covalent cross-linking method to sense propylparaben (PP) present in aqueous solution. Design/methodology/approach PPL immobilization was performed by the covalent cross-linking method, using bovine serum albumin (BSA) in the presence of saturated glutaraldehyde vapor (GA). The preparation of the enzymatic membrane involves the incorporation of porcine pancreatic lipase (PPL), bovine serum albumin (BSA) and glycerol into a phosphate buffer solution (PBS). Characterization of this sensor was performed by impedance spectroscopy (EIS) and scanning electron microscope (SEM). The effect of experimental conditions such as PPL activity, potential, scan rate, PP concentration, pH and presence of interfering elements were studied by cyclic voltammetry. Findings Under the optimal experimental conditions, a number of significant factors were optimized. The method exhibited good linearity in the range of 10–14 to 10–9 mol/L with a good correlation coefficient of 0.957, detection limit (LOD) of 3.66 × 10–15 mol/L and high sensitivity of 1.086 mA mol−1L. The authors also obtained a very good coverage rate of the surface equal to 91.44%, and hydrolytic activity of lipase is evaluated to 26.64 mmol min−1. The stability and the interference were also evaluated. The equivalent circuit used to explain the electrochemical behavior of modified electrode is a Randle circuit. Practical implications The main application of biosensors is the detection of biomolecules that are either indicators of a disease. For example, electrochemical biosensing techniques can be used as clinical tools to detect breast tumors, because these compounds (PP) were found in breast tumors. Originality/value The result registered in this paper indicates that the developed sensor is an efficient, fast, simple and inexpensive analytical tool that can be used for the analysis of water containing PP.

Evaluation on Antidiabetic Properties of Medicinal Plants from Myanmar

Objectives. To explore the effective and safe medicines for treating diabetes. Methods. Hydroalcoholic extracts of 130 medicinal plants belonging to 66 families were evaluated using porcine pancreatic lipase (PPL) inhibition and glucose uptake methods together with a literature review. Results. The extracts of 22 species showed the PPL inhibition activity; 18 extracts of 15 species stimulated glucose uptake in 3T3-L1 adipocytes. Among them, Mansonia gagei J.R. Drumm., Mesua ferrea L., and Centella asiatica (L.) Urb. exhibited both activities. The extracts of Caladium lindenii (André) Madison rhizomes and Azadirachta indica A. Juss. leaves presented the utmost lipase inhibitory activity with IC50 of 6.86 ± 0.25 and 11.46 ± 0.06 μg/mL, respectively. The extracts of Coptis teeta Wall. rhizomes and Croton tiglium L. seeds stimulated the maximum glucose uptake. Ten species are reported to have antidiabetic activity for the first time. Flavonoids and triterpenoids are the dominant antidiabetic compounds in selected medicinal plants from Myanmar. Conclusions. P. zeylanica, L. cubeba, H. crenulate, M. gagei, C. teeta, and M. ferrea are worthy to advance further study according to their strong antidiabetic activities and limited research on effects in in vivo animal studies, unclear chemical constitutes, and safety.

Extraction and Characterization of Coffee Silverskin Oil and Its Valorization by Enzymatic Hydrolysis

This study investigated the coffee silverskin (CS) crude oil extraction process and characterization of physicochemical properties and enzymatic hydrolysis for fatty acids production. The soxhlet and ultrasonic extractions showed CS oil yield similar to 3.8% and 3.1%, respectively. CS oil extracted by soxhlet presented favorable physicochemical properties with the quality and was used as the feedstock for fatty acids production by enzymatic hydrolysis. The porcine pancreatic lipase showed hydrolytic activity of 1156 U.g-1 ± 13.4. Therefore, we verified the potential of application in biotransformation reactions of oils with biocatalyst with fatty acids production and valorization of coffee industry waste.

Rapid screening lipase inhibitors in licorice extract by using porcine pancreatic lipase immobilized Fe3O4 magnetic nanoparticles

Chalcones, a class of natural lipase inhibitors, have received substantial attention from researchers in recent years. Although many kinds of chalcones are typically distributed in G. inflata, there is a...

A Comparison of the Resolution of Selective (+/-)-Glycidyl Butyrate by Using Free and Nano-SiO2 Immobilized Porcine Pancreatic Lipase

To explore the hydrolyzed properties of nano-SiO2 immobilized porcine pancreatic lipase, the selective hydrolysis of immobilized lipase for glycidyl butyrate was compared with the free enzyme. The hydrolysis selectivity of the immobilized biocatalyst was evaluated and compared with the free enzyme using the enantiomeric excess (ee) of resolving racemic glycidyl butyrate as the indicator. The enantiomeric excess of the immobilized biocatalyst could be increased by 4.5%–10.0% which compared with the free enzyme under every single technological condition. The ee was improved from 84.7% for free enzyme to 91.6% for the immobilized enzyme with 61.2% conversion. Compared with free enzyme, the conversion rate of the immobilized enzyme was increased slightly, but the % enantiomeric excess of the immobilized enzyme was increased greatly.