Interaction of Lipase with Lipid Model Systems
DOI:
https://doi.org/10.6000/1929-5995.2020.09.08Keywords:
Lipase, lipids, surface tension,, particle size distributionAbstract
The aim of this work was to study the interaction of lipases (as an important biopolymer) with models of biomembranes based on the phospholipid and cholesterol. Lipases (triacylglycerolacyl hydrolases) are widely distributed enzymes and well-known by their hydrolytic activity. The study of the lipase interactions with lipid vesicles in aqueous dispersions is of fundamental and practical interest. The pure phosphatidylcholine from egg yolk (ePC) and cholesterol (Chol) were obtained from Sigma-Aldrich. Lipase was obtained from hog pancreas. Measurements of the current and equilibrium surface tension (ST and eST) values were carried out using a BPA-1P device and ADSA program. The particle sizes in the prepared colloidal solutions were determined by the method of dynamic light scattering. An addition of lipase led to some decrease both, of ST and eST for the samples of ePC:Chol (in the ratios from19:1 to 1:1). The mean particle diameter (MPD) and effective particle diameter (EPD) values for the samples of ePC:Chol changed drastically by lipase addition. The EPD/MPD ratios increased from 1.7 to 2.0, from 1.8 to 2.6, from 2.3 to 6.5, from 1.5 to 2.9 for the samples of ePC:Chol at the ratios of 19:1, 14:1, 9:1, 7:1, respectively by lipase concentration increase. This general tendency can be explained by strong interaction of lipase with lipid membrane that leads to the formation of the mixed particles ePC:Chol:lipase with more narrow particle size distribution as compared to the initial EPD/MPD ratio (for the ePC:Chol mixture without lipase).
References
Zaitsev SYu, Savina AA, Zaitsev IS. Biochemical aspects of lipase immobilization at polysaccharides for biotechnology. Advances in Colloid and Interface Science 2019; (272): 102016. https://doi.org/10.1016/j.cis.2019.102016 DOI: https://doi.org/10.1016/j.cis.2019.102016
Javed S, Azeem F, Hussain S, Rasul I, Siddique MH, Riaz M, Afzal M, Kouser A, Nadeem H. Bacterial lipases: A review on purification and characterization. Progress in Biophysics and Molecular Biology 2018; 132: 23-34. https://doi.org/10.1016/j.pbiomolbio.2017.07.014 DOI: https://doi.org/10.1016/j.pbiomolbio.2017.07.014
Treichel H, de Oliveira D, Mazutti MA, Di Luccio M, Oliveira JV. A review on microbial lipases production. Food Bioprocess Technology 2010; 3: 182-96. DOI: https://doi.org/10.1007/s11947-009-0202-2
Gupta R, Gupta N, Rathi P. Bacterial lipases: an overview of production, purification and biochemical properties. Applied Microbiology and Biotechnology 2004; 64(6): 763–81. DOI: https://doi.org/10.1007/s00253-004-1568-8
Robles-Medina A, Gonzalez-Moreno PA, Esteban-Cerdan L, Molina-Grima E. Biocatalysis: Towards ever greener biodiesel production. Biotechnol Adv 2009; 27(4): 398-408. https://doi.org/10.1016/j.biotechadv.2008.10.008 DOI: https://doi.org/10.1016/j.biotechadv.2008.10.008
Sangeetha R. Bacterial lipases as potential industrial biocatalysts: An overview. Res. J. Microbiol. 2011; 6: 1–24.
https://dx.doi.org/10.3923/jm.2011.1.24 DOI: https://doi.org/10.3923/jm.2011.1.24
Salihu A, Alam MZ. Solvent tolerant lipases: A review. Process Biochem 2015; 50: 86–96. DOI: https://doi.org/10.1016/j.procbio.2014.10.019
Jaeger K-E, Dijkstra BW, Reetz MT. Bacterial biocatalysts: Molecular Biology, Three- Dimensional Structures and Biotechnological Applications of Lipases. Annual Review of Microbiology 1999; 53(1): 315-51. https://doi.org/10.1146/annurev.micro.53.1.315 DOI: https://doi.org/10.1146/annurev.micro.53.1.315
Jaeger K-E, Eggert T. Lipases for biotechnology. Current Opinion in Biotechnology 2002; 13(4): 390–97. https://doi.org/10.1016/s0958-1669(02)00341-5 DOI: https://doi.org/10.1016/S0958-1669(02)00341-5
Jaeger K-E, Reetz MT. Microbial lipases form versatile tools for biotechnology. Trends in Biotechnology 1998; 16(9): 396–403. https://doi.org/10.1016/s0167-7799(98)01195-0 DOI: https://doi.org/10.1016/S0167-7799(98)01195-0
Andualema B, Gessesse A. Microbial Lipases and Their Industrial Applications: Review. Biotechnology 2012; 11: 100-118.
https://dx.doi.org/10.3923/biotech.2012.100.118 DOI: https://doi.org/10.3923/biotech.2012.100.118
Sharma R, Chisti Y, Banerjee UC. Production, purification, characterization, and applications of lipases. Biotechnology Advances 2001; 19: 627-62. https://doi.org/10.1016/s0734-9750(01)00086-6 DOI: https://doi.org/10.1016/S0734-9750(01)00086-6
Savina AA, Abramova OV, Garnashevich LS, Zaitsev IS, Voronina OA, Tsarkova MS, Zaitsev SYu. Study of Catalytic Activity of Lipase and Lipase-Chitosan Complexes in Dynamics. Journal of Research Updates in Polymer Science 2019; 8: 15-20. DOI: https://doi.org/10.6000/1929-5995.2019.08.03
Kumar R., Goomber S, Kaur, J. Engineering lipases for temperature adaptation: Structure function correlation. Biochimica et Biophysica Acta - Proteins and Proteomics 2019; 1867: 140261. https://doi.org/10.1016/j.bbapap.2019.08.001 DOI: https://doi.org/10.1016/j.bbapap.2019.08.001
Sankar S., Ponnuraj K. Less explored plant lipases: Modeling and molecular dynamics simulations of plant lipases in different solvents and temperatures to understand structure-function relationship. International Journal of Biological Macromolecules 2020; 164: 3546-3558. https://doi.org/10.1016/j.ijbiomac.2020.08.227 DOI: https://doi.org/10.1016/j.ijbiomac.2020.08.227
Kurtovic I., Nalder TD., Cleaver H., Marshall S.N. Immobilisation of Candida rugosa lipase on a highly hydrophobic support: A stable immobilised lipase suitable for non-aqueous synthesis. Biotechnology Reports 2020; 28: e00535. https://doi.org/10.1016/j.btre.2020.e00535 DOI: https://doi.org/10.1016/j.btre.2020.e00535
Bharathi D, Rajalakshmi G. Microbial lipases: An overview of screening, production and purification. Biocatalysis and Agricultural Biotechnology 2019; 22: 101368 https://doi.org/10.1016/j.bcab.2019.101368 DOI: https://doi.org/10.1016/j.bcab.2019.101368
Bilala M., Iqbal HMN. Armoring bio-catalysis via structural and functional coordination between nanostructured
materials and lipases for tailored applications. International Journal of Biological Macromolecules 2020; In Press. https://doi.org/10.1016/j.ijbiomac.2020.10.239 DOI: https://doi.org/10.1016/j.ijbiomac.2020.10.239
Zaitsev SYu. Biological chemistry: from biologically active substances to organs and tissues of animals. Moscow: Capital Print Publishing; 2017.
Zaitsev SYu. Supramolecular Nanosized Systems at the Phase Interface: Concepts and Prospects for Bio-Nanotechnologies. Moscow: LENAND; 2010.
Zaitsev SYu. Membrane Structures Based on Synthetic and Natural Polymers. Moscow: Skryabin Moscow State Academy of Veterinary Medicine and Biotechnology; 2006.
Zaitsev SYu. Supramolecular Systems at the Phase Interface as Models of Biomembranes and Implications for Nanomaterials. Moscow, Donetsk: Nord Computer; 2006.
Torchilin V. Nanoparticulates as Drug Carriers. New York: World Scientific Publishing Co.; 2006. DOI: https://doi.org/10.1142/p432
Andresen TL, Jensen SS, Jorgensen K. Advanced strategies in liposomal cancer therapy: Problems and prospects of active and tumor specific drug release. Progress in Lipid Research 2005; 44: 68-97. DOI: https://doi.org/10.1016/j.plipres.2004.12.001
BrookhavenInstruments [homepage on the Internet]. Instruction Manual for 90Plus/BI-MAS (Multi Angle Particle Sizing Option Operation Manual) Brookhaven Instruments Corporation Holtsville, NY 11742 USA 2005-2010. 73 pages. www.BrookhavenInstruments.com
Chen J., Lin S., Sun N., Bao Z., Shen J., Lu X. Egg yolk phosphatidylcholine: Extraction, purification and its potential neuro-protective effect on PC12 cells. Journal of Functional Foods 2019; 56: 372-383. https://doi.org/10.1016/j.jff.2019.03.037 DOI: https://doi.org/10.1016/j.jff.2019.03.037
Bao Z., Zhang P., Chen J., Gao J., Lin S., Sun, N. Egg yolk phospholipids reverse scopolamine–induced spatial memory deficits in mice by attenuating cholinergic damage. Journal of Functional Foods 2020; 69: 103948. https://doi.org/10.1016/j.jff.2020.103948 DOI: https://doi.org/10.1016/j.jff.2020.103948
Dong XF., Zhai QH., Tong JM. Dietary choline supplementation regulated lipid profiles of egg yolk, blood,and liver and improved hepatic redox status in laying hens. Poultry Science 2019; 98: 3304-3312. https://doi.org/10.3382/ps/pez139 DOI: https://doi.org/10.3382/ps/pez139
Yamamoto Y., Harada K., Kasuga S., Hosokawa M. Phospholipase A2-Mediated preparation of phosphatidylcholine containing ricinoleic acid and its anti-inflammatory effect on murine macrophage-likeRAW264.7 cells. Biocatalysis and Agricultural Biotechnology 2019; 19: 101141. https://doi.org/10.1016/j.bcab.2019.101141 DOI: https://doi.org/10.1016/j.bcab.2019.101141
Janist N., Srichana P., Asawakarn T., Kijparkorn S. Effect of supplementing the laying hen diets with choline, folic acid, and vitamin B12 on production performance, egg quality, and yolk phospholipid. Livestock Science 2019; 223: 24-31 https://doi.org/10.1016/j.livsci.2019.02.019 DOI: https://doi.org/10.1016/j.livsci.2019.02.019
Gliozzi M., Musolino V., Bosco F., Scicchitano M., Scarano F., Nucera S., Zito MC., Ruga S., Carresi C., Macrì R., Guarnieri L., Maiuolo J., Tavernese A., Coppoletta AR., Nicita C., Mollace R., Palma E., Muscoli C., Mollace V. Cholesterol homeostasis: Researching a dialogue between the brain and peripheral tissues. Pharmacological Research 2020; 105215 In Press. https://doi.org/10.1016/j.phrs.2020.105215 DOI: https://doi.org/10.1016/j.phrs.2020.105215
Oakes V., Domene C. Influence of Cholesterol and Its Stereoisomers on Members of the Serotonin Receptor Family. Journal of Molecular Biology 2019; 431: 1633-1649 https://doi.org/10.1016/j.jmb.2019.02.030 DOI: https://doi.org/10.1016/j.jmb.2019.02.030
Zhang X., Huang Q., Wang X., Deng Z., Li J., Yan X., Jauhiainen M., Metso J., Libby P., Liu J., Shi G.-P. Dietary cholesterol is essential to mast cell activation and associated
obesity and diabetes in mice. Biochimica et Biophysica Acta - Molecular Basis of Disease 2019; 1865: 1690-1700. https://doi.org/10.1016/j.bbadis.2019.04.006 DOI: https://doi.org/10.1016/j.bbadis.2019.04.006
Wen X., Wu W., Fang W., Tang S., Xin H., Xie J., Zhang H. Effects of long-term heat exposure on cholesterol metabolism and immune responses in growing pigs. Livestock Science 2019; 230: 103857. https://doi.org/10.1016/j.livsci.2019.103857 DOI: https://doi.org/10.1016/j.livsci.2019.103857
Lin C.-W., Huang T.-W., Peng Y.-J., Lin Y.-Y., Mersmann HJ., Ding S.-T. A novel chicken model of fatty liver disease induced by high cholesterol and low choline diets. Poultry Science 2020; In Press. https://doi.org/10.1016/j.psj.2020.11.046 DOI: https://doi.org/10.1016/j.psj.2020.11.046
Bourlieu C, Paboeuf G, Chever S., Pezennec S, Cavalier JF, Adsorption of gastric lipase onto multicomponent model lipid monolayers with phase separation. Colloids and Surfaces B: Biointerfaces, Elsevier, 2016, 143, pp.97-106. https://doi.org/10.1016/j.colsurfb.2016.03.032 DOI: https://doi.org/10.1016/j.colsurfb.2016.03.032
Bénarouche A, Sams L, Bourlieu C, Vié V, Point V, Cavalier JF, Carrière F. Studying Gastric Lipase Adsorption Onto Phospholipid Monolayers by Surface Tensiometry, Ellipsometry, and Atomic Force Microscopy. Methods Enzymol. 2017; 583: 255-278. doi: 10.1016/bs.mie.2016.09.039. Epub 2016 Nov 14.PMID: 28063494 DOI: https://doi.org/10.1016/bs.mie.2016.09.039
Bourlieu C, Mahdoueni W, Paboeuf G, Gicquel E, Ménard O, Pezennec S, Bouhallab S, Deglaire A, Dupont D, Carrière F, Vié V. Physico-chemical behaviors of human and bovine milk membrane extracts and their influence on gastric lipase adsorption. Biochimie. 2020 Feb;169:95-105. doi: 10.1016/j.biochi.2019.12.003. Epub 2019 Dec 20.PMID: 31866313 DOI: https://doi.org/10.1016/j.biochi.2019.12.003
Zaitsev SYu. Dynamic surface tension measurements as general approach to the analysis of animal blood plasma and serum. Advances in Colloid and Interface Science 2016; (235): 201–213. https://doi.org/10.1016/j.cis.2016.06.007 DOI: https://doi.org/10.1016/j.cis.2016.06.007
Zaitsev SYu, Savina AA, Garnashevich LS, Tsarkova MS, Zaitsev IS. Effect of Some Charged Polymers on the Activity of Pancreatic Porcine Lipase. BioNanoScience 2019; 9 (4): 773-777. https://doi.org/10.1007/s12668-019-00677-1 DOI: https://doi.org/10.1007/s12668-019-00677-1
Savina AA., Garnashevich LS. Zaitsev IS, Tsarkova MS, Zaitsev SYu. Changes in lipase activity in the presence of synthetic and natural polymers. Moscow University Chemistry Bulletin. Series 2: Chemistry 2019; 74(6): 306–309. https://doi.org/10.3103/S0027131419060130 DOI: https://doi.org/10.3103/S0027131419060130
Downloads
Published
How to Cite
Issue
Section
License
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
Policy for Journals/Articles with Open Access
Authors who publish with this journal agree to the following terms:
- Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.
- Authors are permitted and encouraged to post links to their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work
Policy for Journals / Manuscript with Paid Access
Authors who publish with this journal agree to the following terms:
- Publisher retain copyright .
- Authors are permitted and encouraged to post links to their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work .