The Activation Energies and Optimum Temperatures of Olive Oil Hydrolysis By Lipase Porcine Pancreas

Lipase activity is a perfect indicator for the monitoring of processes of bioremediation of degraded soils. Lipase is also used in the processes of oil hydrolysis in wastewater treatment. To be able to predict and model processes with used lipase in environmental operations, knowledge of the kinetic parameters of the process are required. The paper presents the determined values of activation energies and optimum temperatures for porcine pancreas lipase. The parameters were estimated based on the literature of the activity curves vs. temperature for hydrolysis of olive oil by lipase. It was noticed that concentration of gum arabic added as an emulsifier during lipase activity measurements influences on the obtained values of determined parameters. A mathematical model describing the effect of temperature on porcine pancreas lipase activity was used. Based on the comparison analysis, the optimum temperature Topt were obtained in the range from 313.30 ±0.56 to 319.62 ±0.96 K, activation energies Ea were from 51 ±10 to 82.6 ±9.9 kJ/mol, and values of deactivation energies Ed were in the range from 122.7 ±4.0 to 150.9 ±5.8 kJ/mol.

Fast Multipoint Immobilization of Lipase through Chiral L-Proline on MOF as Chiral Bioreactor

In this paper, we describe the facile preparation of a chiral catalyst by the combination of the amino acid, L-proline (Pro), and the enzyme, porcine pancreas lipase (PPL), immobilized on...

Evaluation of Strategies to Produce Highly Porous Cross-Linked Aggregates of Porcine Pancreas Lipase with Magnetic Properties

The preparation of highly porous magnetic crosslinked aggregates (pm-CLEA) of porcine pancreas lipase (PPL) is reported. Some strategies to improve the volumetric activity of the immobilized biocatalyst were evaluated, such as treatment of PPL with enzyme surface-modifying agents (polyethyleneimine or dodecyl aldehyde), co-aggregation with protein co-feeders (bovine serum albumin and/or soy protein), use of silica magnetic nanoparticles functionalized with amino groups (SMNPs) as separation aid, and starch as pore-making agent. The combination of enzyme surface modification with dodecyl aldehyde, co-aggregation with SMNPs and soy protein, in the presence of 0.8% starch (followed by hydrolysis of the starch with α-amylase), yielded CLEAs expressing high activity (immobilization yield around 100% and recovered activity around 80%), high effectiveness factor (approximately 65% of the equivalent free enzyme activity) and high stability at 40 °C and pH 8.0, i.e., PPL CLEAs co-aggregated with SMNPs/bovine serum albumin or SMNPs/soy protein retained 80% and 50% activity after 10 h incubation, respectively, while free PPL was fully inactivated after 2 h. Besides, highly porous magnetic CLEAs co-aggregated with soy protein and magnetic nanoparticles (pm-SP-CLEAs) showed good performance and reusability in the hydrolysis of tributyrin for five 4h-batches.

Mechanochemo-enzymatic Synthesis of Aromatic Aldehyde Oxime Esters

The synthesis of aromatic aldehyde oxime esters (considered fragrances, antifungal and antimicrobial compounds) was achieved by two reactions which combine the advantage of green chemistry and biocatalysis. In the first step, the mechanochemical oxime synthesis by means of grindstone milling of six solid aromatic aldehydes and hydroxylamine hydrochloride in the presence of FlorisilR, as the best support, yielded the aromatic aldehyde oximes 1–6 with high purity and good yields. In the second step the lipase catalyzed acetylation reaction at 40°C for three days of those oximes with vinyl and isopropenyl acetates as acyl donor substrates and ethyl acetate as the solvent, yielded the aromatic aldehyde oxime esters. With Candida antarctica lipase (Novozyme 435), the conversions of oximes 1–6 into their esters were ≥ 99% according to the 1H NMR results and it was the best biocatalyst compared with others such as Candida rugosa (CRL), porcine pancreas lipase and the recombinant lipase LipMatCCR11 from the thermophilic strain Geobacillus thermoleovorans CCR11 cloned and expressed in Escherichia coli BL21 (DE3), all of which showed lower yields.

Hydrolysis Activity of Virgin Coconut Oil Using Lipase from Different Sources

Two types of lipase, Candida rugosa lipase (CRL) and porcine pancreas lipase (PPL), were used to hydrolyze virgin coconut oil (VCO). The hydrolysis process was carried out under four parameters, VCO to buffer ratio, lipase concentration, pH, and temperature, which have a significant effect on hydrolysis of lipase. CRL obtained the best hydrolysis condition at 1 : 5 of VCO to buffer ratio, 1.5% of CRL concentration, pH 7, and temperature of 40°C. Meanwhile, PPL gave different results at 1 : 4 of VCO to buffer ratio, 2% of lipase concentration, pH 7.5, and 40°C. The highest hydrolysis degree of CRL and PPL was obtained after 16 hours and 26 hours, reaching 79.64% and 27.94%, respectively. Besides, the hydrolysis process was controlled at different time course (every half an hour) at the first 4 hours of reaction to compare the initial hydrolysis degree of these two lipase types. FFAs from hydrolyzed products were isolated and determined the percentage of each fatty acid which contributes to the FFAs mixture. As a result, medium chain fatty acids (MCFAs) made up the main contribution in composition of FFAs and lauric acid (C12) was the largest segment (47.23% for CRL and 44.23% for PPL).