The activation energies and optimum temperatures of olive oil hydrolysis by lipase porcine pancreas

• Autorzy: Miłek Justyna

Identyfikatory

DOI

10.2478/eces-2021-0026

• Języki publikacji: EN

Abstrakty

EN

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 T_opt were obtained in the range from 313.30 ±0.56 to 319.62 ±0.96 K, activation energies E_a were from 51 ±10 to 82.6 ±9.9 kJ/mol, and values of deactivation energies E_d were in the range from 122.7 ±4.0 to 150.9 ±5.8 kJ/mol.

Słowa kluczowe

EN

lipase; porcine pancreas; gum arabic; optimum temperature; activation energy; deactivation energy

PL

lipaza; trzustka wieprzowa; guma arabska; temperatura optymalna; energia aktywacji; energia dezaktywacji

• Wydawca: Towarzystwo Chemii i Inżynierii Ekologicznej
• Czasopismo: Ecological Chemistry and Engineering. S
• Rocznik: 2021
• Tom: Vol. 28, nr 3
• Strony: 389--398
• Opis fizyczny: Bibliogr. 28 poz., tab., wykr.

Twórcy

autor

Miłek Justyna

• Department of Chemical and Biochemical Engineering, Faculty of Chemical Technology and Engineering, Bydgoszcz University of Science and Technology, ul. Seminaryjna 3, 85-326 Bydgoszcz, Poland, phone [phone]

• https://orcid.org/0000-0002-6058-8948

Bibliografia

• [1] Joniec J, Furczak J, Kwiatkowska E. Application of biological indicators for estimation of remediation of soil degraded by sulphur industry. Ecol Chem Eng S. 2015;22(2):269-83. DOI: 10.1515/eces-2015-0016.
• [2] Baćmaga M, Kucharski J, Wyszkowska J, Tomkiel M, Borowik A. Response of actinomycetes, phosphatises and urease to soil contamination with herbicides. Ecol Chem Eng S. 2015;22(2):255-67. DOI: 10.1515/eces-2015-0015.
• [3] Wołejko E, Wydro U, Łoboda T. The ways to increase efficiency of soil bioremediation. Ecol Chem Eng S. 2016;23(1):155-74. DOI: 10.1515/eces-2016-0011.
• [4] Mendes AA, Oliveira PC, de Castro HF. Properties and biotechnological applications of porcine pancreatic lipase. J Mol Catal B: Enzym. 2012;78:119-34. DOI: 10.1016/j.molcatb.2012.03.004.
• [5] Treichel H, de Oliveira D, Mazutti MA, Di Luccio M, Oliveira JV. A review on microbial lipases production. Food Bioprocess Technol. 2010;3:182-96. DOI: 10.1007/s11947-009-0202-2.
• [6] Barros M, Fleuri LF, Macedo GA. Seed lipases: source, applications and properties - a review. Brazilian J Chem Eng. 2010;27:15-29. DOI: 10.1590/S0104-66322010000100002.
• [7] Jooyandeh H, Kaur A, Minhas KS. Lipases in dairy industry: A review. J Food Sci Technol. 2009;46(3):181-9. Available from: https://www.researchgate.net/publication/267867671_Lipases_in_dairy_industry_A_review.
• [8] Sharma R, Chisti Y, Banerjee UC. Production, purification, characterization, and applications of lipases. Biotechnol Adv. 2001;19:627-62. DOI: 10.1016/s0734-9750(01)00086-6.
• [9] Hasan F, Shah AA, Hameed A. Industrial applications of microbial lipases. Enzyme Microb Tech. 2006;39:235-51. DOI: 10.1016/j.enzmictec.2005.10.016.
• [10] Guerrand D. Lipases industrial applications: focus on food and agroindustries. OCL. 2017;24(4):D403. DOI: 10.1051/ocl/2017031.
• [11] Miłek J. Calculation of temperature optimum as well as activation and deactivation energy for the olive oil hydrolysis with porcine pancreas lipase. Przem Chem. 2020;99(4):585-7. DOI: 10.15199/62.2020.4.14.
• [12] Bagi K, Simon LM, Szajáni B. Immobilization and characterization of porcine pancreas lipase. Enzyme Microb Tech. 1997;20:531-5. DOI: 10.1016/S0141-0229(96)00190-1.
• [13] Paula AV, Urioste D, Santos JC, de Castro HF. Porcine pancreatic lipase immobilized on polysiloxane-polyvinyl alcohol hybrid matrix: catalytic properties and feasibility to mediate synthesis of surfactants and biodiesel. J Chem Technol Biotechnol. 2007;82:281-8. DOI: 10.1002/jctb.1669.
• [14] Lee D-G, Ponvel KM, Kim M, Hwang Sl, Ahn I-S, Lee C-H. Immobilization of lipase on hydrophobic nano-sized magnetite particles. J Mol Catal B: Enzym. 2009;57:62-6. DOI: 10.1371/journal.pone.0114385.
• [15] Silva NCA, Miranda JS, Bolina ICA, Silva WC, Hirata DB, de Castro HF, et al. Immobilization of porcine pancreatic lipase on poly-hydroxybutyrate particles for the production of ethyl esters from macaw palm oils and pineapple flavor. Biochem Eng J. 2014;82:139-49. DOI: 10.1016/j.bej.2013.11.015.
• [16] Guimarăes JR, de Lima Camargo Giordano R, Fernandez-Lafuenteand R, Tardioli PW. Evaluation of strategies to produce highly porous cross-linked aggregates of porcine pancreas lipase with magnetic properties. Molecules. 2018;23:2993. DOI: 10.3390/molecules23112993.
• [17] Zaitsev SY, Savina AA, Garnashevich LS, Tsarkova MS, Zaitsev IS. Effect of some charged polymers on the activity of pancreatic porcine lipase. BioNanoScience. 2019;9:773-7. DOI: 10.1007/s12668-019-00677-1.
• [18] Dong H, Li J, Li Y, Hu L, Luo D. Improvement of catalytic activity and stability of lipase by immobilization on organobentonite. Chem Eng J. 2012;181-182:590-6. DOI: 10.1016/j.cej.2011.11.095.
• [19] Tsujita T, Okuda H. Effect of bile salts on the interfacial inactivation of pancreatic carboxylester lipase. J Lipid Res. 1990;31:831-8. Available from: https://www.jlr.org/content/31/5/831.
• [20] Olusesan AT, Azura LK, Forghani B, Bakar FA, Mohamed AKS, Radu S, et al. Purification, characterization and thermal inactivation kinetics of a non-regioselective thermostable lipase from a genotypically identified extremophilic Bacillus subtilis NS 8. New Biotechnol. 2011;28:738-45. DOI: 10.1016/j.nbt.2011.01.002.
• [21] Vyazovkin S, Burnham AK, Criado JM, Pérez-Maqueda LA, Popescu C, Sbirrazzuolie N. ICTAC Kinetics Committee recommendations for performing kinetic computations on thermal analysis data. Thermochim Acta. 2011;520:1-19. DOI: 10.1016/j.tca.2011.03.034.
• [22] Miłek J. Determination the optimum temperature and activation energies for the hydrolysis of inulin hydrolysis by endo-inulinase Aspergillus niger. Chem Process Eng. 2020;41(2):229-36. DOI: 10.24425/CPE.2020.132545.
• [23] Miłek J. Application of the new method to determine of the kinetic parameters of inulin hydrolysis by exo-inulinase Aspergillus niger. J Therm Anal Calorim. 2021. DOI: 10.1007/s10973-020-10495-3.
• [24] Miłek J. The effect of pH on determination of activation energies and the optimum temperatures of hydrolysis of olive oil by lipase from porcine pancreas. Acta Bioeng Biomech. 2021;23(3):1-15. DOI: 10.37190/ABB-01827-2021-02.
• [25] Kambiré MS, Gnanwa JM, Boa D, Kouadio EJP, Kouamé LP. Modeling of enzymatic activity of free β-glucosidase from palm weevil, Rhynchophorus Palmarum Linn. (Coleoptera: Curculionidae) larvae: effects of pH and temperature. Biophys Chem. 2021;274:106611. DOI: 10.1016/j.bpc.2021.106611.
• [26] Falco FC, Espersen R, Svensson B, Gernaey KV, LantzAE. An integrated strategy for the effective production of bristle protein hydrolysate by the keratinolytic filamentous bacterium Amycolatopsis keratiniphila D2. Waste Manage. 2019;89:94-102. DOI: 10.1016/j.wasman.2019.03.067.
• [27] Soares CMF, Castro HF, Moraes FF, Zanin GM. Characterization and utilization of Candida rugosa lipase immobilized on controlled pore silica. Appl Biochem Biotechnol. 1999;77/79:745-57. DOI: 10.1385/abab:79:1-3:745.
• [28] Pereira EB, de Castro HF, de Moraes FF, Zanin GM. Kinetic studies of lipase from Candida rugosa. Appl Biochem Biotechnol. 2001;91-93:739-52. DOI: 10.1385/ABAB:91-93:1-9:739.

Uwagi

Opracowanie rekordu ze środków MNiSW, umowa Nr 461252 w ramach programu "Społeczna odpowiedzialność nauki" - moduł: Popularyzacja nauki i promocja sportu (2021).