Change in gastric-lipase adsorption on lipid layer by stigmasterols
Author:
Shin Gounhanul1, Hadinoto Kunn2, Park Jin-Won1
Affiliation:
1. Department of Chemical and Biomolecular Engineering, College of Energy and Biotechnology , Seoul National University of Science and Technology , 232 Gongneung-ro, Nowon-gu , Seoul , Republic of Korea 2. School of Chemistry, Chemical Engineering and Biotechnology , Nanyang Technological University , 62 Nanyang Drive, Blk N1.2 Level B2-31, 637459 , Singapore , Singapore
Abstract
Abstract
Gastric-lipase (GL) binding to a lipid layer was investigated for the phase of the layer adjusted with the ratio of stigmasterol to the lipid using surface plasmon resonance. While the layer was formed on the hydrophobic surface, more stigmasterol led to lower surface density only in the dipalmitoylphosphatidylcholine (DPPC) layer. The addition of stigmasterol was believed to transform the phase (condensed liquid-phase) of DPPC layer closer to the phase (expanded liquid-phase) of dioleoylphosphatidylcholine (DOPC) layer. At a ratio greater than 15:85, the effect of the stigmasterol on the DPPC was saturated. The adsorption behavior of GL showed the similar trend with the lipid formation. The adsorption increased with the increase in the ratio of stigmasterol to lipid up to 15:85. On the DOPC layer of the expanded liquid-phase, the most adsorption seemed to occur and was indistinguishable from that in the DPPC layer of 15:85. The surface density of the adsorbed GL was interpreted into the fraction of the stigmasterol-dependent DPPC, 0.33, 0.67, and 1.00 for 10:90, 5:95, and 0:100 of DPPC. Furthermore, the equilibrium constant was between 1 × 1013 M−1 and 2 × 1013 M−1 and the kinetics of the adsorption showed an increase in the adsorption rate constant with the increase of the ratio up to 15:85.
Publisher
Walter de Gruyter GmbH
Subject
Condensed Matter Physics,General Chemical Engineering,General Chemistry
Reference32 articles.
1. Pafumi, Y., Lairon, D., de la Porte, P. L., Juhel, C., Storch, J., Hamosh, M., Armand, M. Mechanisms of inhibition of triacylglycerol hydrolysis by human gastric lipase. J. Biol. Chem. 2002, 277, 28070–28079; https://doi.org/10.1074/jbc.m202839200. 2. Ollis, D. L., Cheah, E., Cygler, M., Dijkstra, B., Frolow, F., Franken, S. M., Harel, M., Remington, S. J., Silman, I., Schrag, J., Sussman, J. L., Verschueren, K. H. G., Goldman, A. The alpha/beta hydrolase fold. Protein Eng. 1992, 5, 197–211; https://doi.org/10.1093/protein/5.3.197. 3. Canaan, S., Roussel, A., Verger, R., Cambillau, C. Gastric lipase: crystal structure and activity. Biochim. Biophys. Acta 1999, 1441, 197–204; https://doi.org/10.1016/s1388-1981(99)00160-2. 4. Roussel, A., Miled, N., Berti-Dupuis, L., Rivi`ere, M., Spinelli, S., Berna, P., Gruber, V., Verger, R., Cambillau, C. Crystal structure of the open form of dog gastric lipase in complex with a phosphonate inhibitor. J. Biol. Chem. 2002, 277, 2266–2274; https://doi.org/10.1074/jbc.M109484200. 5. Chahinian, H., Snabe, T., Attias, C., Fojan, P., Petersen, S. B., Carrière, F. How gastric lipase, an interfacial enzyme with a Ser-His-Asp catalytic triad, acts optimally at acidic pH. Biochemistry 2006, 45, 993–1001; https://pubs.acs.org/doi/10.1021/bi0518803#.
Cited by
1 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
|
|