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

2021 ◽  
Vol 28 (3) ◽  
pp. 389-398
Author(s):  
Justyna Miłek

Abstract 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.

Molecules ◽  
2021 ◽  
Vol 26 (14) ◽  
pp. 4117
Author(s):  
Justyna Miłek

The present paper reports the determination of the activation energies and the optimum temperatures of starch hydrolysis by porcine pancreas α-amylase. The parameters were estimated based on the literature data on the activity curves versus temperature for starch hydrolysis by α-amylase from porcine pancreas. It was assumed that both the hydrolysis reaction process and the deactivation process of α-amylase were first-order reactions by the enzyme concentration. A mathematical model describing the effect of temperature on porcine pancreas α-amylase activity was used. The determine deactivation energies Ea were from 19.82 ± 7.22 kJ/mol to 128.80 ± 9.27 kJ/mol, the obtained optimum temperatures Topt were in the range from 311.06 ± 1.10 K to 326.52 ± 1.75 K. In turn, the values of deactivation energies Ed has been noted in the range from 123.57 ± 14.17 kJ/mol to 209.37 ± 5.17 kJ/mol. The present study is related to the starch hydrolysis by α-amylase. In the industry, the obtained results the values Ea, Ed, Topt can be used to design and optimize starch hydrolysis by α-amylase porcine pancreas. The obtained results might also find application in research on the pharmaceutical preparations used to treat pancreatic insufficiency or prognosis of pancreatic cancer.


2017 ◽  
Author(s):  
Chau Tran Diem Ai ◽  
Vo Thi Hong Linh ◽  
Tran Thi Ngoc Yen ◽  
Nguyen Thi Nguyen ◽  
Phan Ngoc Hoa

Materials ◽  
2020 ◽  
Vol 14 (1) ◽  
pp. 119
Author(s):  
Dana H. Abdeen ◽  
Muataz A. Atieh ◽  
Belabbes Merzougui

The inhibition behavior of carbon nanotubes (CNTs) and Gum Arabic (GA) on the corrosion of 316L stainless steel in CNTs–water nanofluid under the effect of different temperatures was investigated by electrochemical methods and surface analysis techniques. Thereby, 316L stainless steel samples were exposed to CNTs–water nanofluid under temperatures of 22, 40, 60 and 80 °C. Two concentrations of the CNTs (0.1 and 1.0 wt.% CNTs) were homogenously dispersed in deionized water using the surfactant GA and tested using three corrosion tests conducted in series: open circuit test, polarization resistance test, and potentiodynamic scans. These tests were also conducted on the same steel but in solutions of GA-deionized water only. Tests revealed that corrosion increases with temperature and concentration of the CNTs–water nanofluids, having the highest corrosion rate of 32.66 milli-mpy (milli-mil per year) for the 1.0 wt.% CNT nanofluid at 80 °C. In addition, SEM observations showed pits formation around areas of accumulated CNTs that added extra roughness to the steel sample. The activation energy analysis and optical surface observations have revealed that CNTs can desorb at higher temperatures, which makes the surface more vulnerable to corrosion attack.


Scientifica ◽  
2018 ◽  
Vol 2018 ◽  
pp. 1-6 ◽  
Author(s):  
T. A. V. Nguyen ◽  
Truong D. Le ◽  
Hoa N. Phan ◽  
Lam B. Tran

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).


1991 ◽  
Vol 17 (3) ◽  
pp. 449-454 ◽  
Author(s):  
Tadashi Hano ◽  
Michiaki Matsumoto ◽  
Takaaki Ohtake ◽  
Fumiaki Hori

2018 ◽  
Vol 13 (7) ◽  
pp. 1934578X1801300
Author(s):  
Margarita A. Arthur-Santiago ◽  
Rosa María Oliart-Ros ◽  
María G. Sánchez-Otero ◽  
Gerardo Valerio-Alfaro

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.


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