Naslov
Characterization of lipases from Burkholderia cepacia and Pseudomonas fluorescens

Autori
Ostojčić, Marta ; Budžaki, Sandra ; Strelec, Ivica

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
3rd YOUNG SCIENTISTS’ DAY - BOOK OF ABSTRACTS / Drenjančević, Ines - Osijek : Josip Juraj Strossmayer University of Osijek Faculty of Medicine Osijek, 2021, 33-33

ISBN
978-953-7736-55-2

Skup
3. dani mladih istraživača = 3rd Young Scientists Days Conference

Mjesto i datum
Osijek, Hrvatska, 30.11.2021

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Recenziran

Ključne riječi
lipase , pH optimum ; temperature optimum ; substrate specificity ; kinetics parameters

Sažetak
Lipases (EC 3.1.1.3.), triacylglycerol acylhydrolases, are enzymes that, in addition to the triacylglycerol hydrolysis reaction, successfully catalyse the reactions of esterification, interesterification, transesterification, acidolysis and aminolysis, under appropriate reaction conditions. According to the literature, lipases are very active in a wide pH and temperature range, and hydrolyse differently toward different substrates, depending primarily on the microorganism from which they originate. The aim of this research was to characterize lipases from bacteria Burkholderia cepacia (BCL) and Pseudomonas fluorescens (PFL). Using a titrimetric test for lipase activity, with olive oil as a substrate, the linearity of the test reaction, kinetics parameters, and the pH and temperature optimum for each lipase were determined. In addition, the substrate specificity of lipases according to selected commercially available, cold-pressed and waste oils was examined. The results showed that the steady state of the enzymatic hydrolysis of triacylglycerol for both lipases lasted up to 30 min. Lipases optimally hydrolysed olive oil as substrate at pH 8 and temperature of 50 °C. Analysis of experimental data in GraphPad Prism 8 revealed that both enzymes do not follow Michaelis-Menten kinetics, but obey allostery. Allosteric kinetic parameters for BCL were Vmax=16.45 U mL-1, K0.5=32.29 mmol L-1 and h=1.653, and for PFL Vmax=11.97 U mL-1, K0.5=22.92 mmol L-1 and h=1.262. It was found that both lipases have the highest specificity for commercially available oils. All the obtained data will be used for further characterization of lipases as well as for setting initial conditions of their immobilization on appropriate carriers.

Izvorni jezik
Engleski

Znanstvena područja
Biotehnologija, Prehrambena tehnologija

POVEZANOST RADA