Inhibitory Effect and Mechanism of Ethyl <i>p</i>-hydroxycinnamate on Pancreatic Lipase

Yangjun YU; Ling WU; Junzhu HE; Hui NI; Yuanfan YANG

doi:10.13386/j.issn1002-0306.2020060193

Volume 42 Issue 9

Apr. 2021

Turn off MathJax

Article Contents

Abstract

References

Science and Technology of Food Industry > 2021 > 42(9): 94-99. > DOI: 10.13386/j.issn1002-0306.2020060193

YU Yangjun, WU Ling, HE Junzhu, et al. Inhibitory Effect and Mechanism of Ethyl p -hydroxycinnamate on Pancreatic Lipase[J]. Science and Technology of Food Industry, 2021, 42(9): 94−99. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306. 2020060193.

Citation:

PDF (1175 KB)

Inhibitory Effect and Mechanism of Ethyl p-hydroxycinnamate on Pancreatic Lipase

Yangjun YU^1,,
Ling WU^{1, 2, 3},
Junzhu HE¹,
Hui NI^{1, 2, 3},
Yuanfan YANG^{1, 2, 3, ,}

1.
Jimei University, College of Food and Biological Engineering, Xiamen 361021, China
2.
Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering, Xiamen 361021, China
3.
Research Center of Food Biotechnology of Xiamen City, Xiamen 361021, China

More Information

Received Date: June 15, 2020
Available Online: February 03, 2021

Graphical Abstract

Abstract

Abstract

In order to explore lipid lowering activity of ethyl p-hydroxycinnamate, enzyme reaction kinetics and molecular docking techniques were used to study the inhibitory type and mechanism of ethyl p-hydroxycinnamate on pancreatic lipase. The kinetics results showed that ethyl p-hydroxycinnamate was a reversible competitive inhibitor of pancreatic lipase (semi-inhibitory concentration IC₅₀ was 41.07 μg/mL), with the maximum reaction rate V_max of 2.61 μmol/L·min and the inhibitory constant K_i of 114.35 μg/mL. Molecular docking results showed that ethyl p-hydroxycinnamate could form a strong hydrogen bond with the amino acid residues Ser152 and His263 in the triplet catalyzed by pancreatic lipase. Ethyl p-hydroxycinnamate could interacted with the amino acid residues of pancreatic lipase through Van der Waals force, hydrogen bond force, and competed with the substrate p-NPB for the active site of the enzyme. This study provided a theoretical basis for the application of ethyl p-hydroxycinnamate in functional foods.
- ethyl p-hydroxycinnamate,
- pancreatic lipase,
- inhibitory effect,
- molecular docking

FullText(HTML)

References (31)

References

[1]	Chen Y J, Peng Q, Yang Y, et al. The prevalence and increasing trends of overweight, general obesity, and abdominal obesity among Chinese adults: A repeated cross-sectional study[J]. BMC Public Health,2019,19(1):1293−1941. doi: 10.1186/s12889-019-7633-0
[2]	Hruby A, Manson J E, Qi L, et al. Determinants and consequences of obesity[J]. American Journal of Public Health,2016,106(9):1656−1662. doi: 10.2105/AJPH.2016.303326
[3]	Mohammad M, Al-masri I M, Issa A, et al. Inhibition of pancreatic lipase by berberine and dihydroberberine: An investigation by docking simulation and experimental validation[J]. Medicinal Chemistry Research,2013,22(5):2273−2278. doi: 10.1007/s00044-012-0221-9
[4]	McDougall G J, Kulkarni N N, Stewart D. Berry polyphenols inhibit pancreatic lipase activity in vitro[J]. Food Chemistry,2009,115(1):193−199. doi: 10.1016/j.foodchem.2008.11.093
[5]	Leung W Y S, Thomas G N, Chan J C N, et al. Weight management and current options in pharmacotherapy: Orlistat and sibutramine[J]. Clinical Therapeutics,2003,25(1):58−80. doi: 10.1016/S0149-2918(03)90009-9
[6]	褚盼盼, 门玉倩, 孔令悦, 等. 黑豆红色素抑制胰脂肪酶催化反应动力学研究[J]. 食品科技,2018,43(5):302−307.
[7]	杨采风. 壳聚糖羟基肉桂酸衍生物的制备及其抑菌活性的研究[D]. 镇江: 江苏科技大学, 2016.
[8]	Ohkatsu Y, Satoh T. Antioxidant and photo-antioxidant activities of chalcone derivatives[J]. Journal of the Japan Petroleum Institute,2008,51(5):298−308. doi: 10.1627/jpi.51.298
[9]	张永兵. 竹叶提取物对酪氨酸酶和黑色素瘤细胞的影响[D]. 北京: 中国林业科学研究院, 2009.
[10]	Gao H Y, Wang H Y, Li G Y, et al. Constituents from zhuyeqing liquor and their inhibitory effects on nitric oxide production[J]. Phytochemistry Letters,2014(7):150−155.
[11]	倪辉, 孙旭, 杜希萍, 等. 从茶花粉中分离纯化对羟基肉桂酸乙酯的方法及其应用: 中国, 201810744484.9[P]. 2018-07-19.
[12]	单萍, 赵淑娥. 紫外-荧光分光光度法联用测定熊果酸对胰脂肪酶的抑制作用[J]. 江西科学,2014,32(3):309−311, 407. doi: 10.3969/j.issn.1001-3679.2014.03.012
[13]	Chai W, Ou-Yang C, Ma Z, et al. Anti-α-glucosidase and antityrosinase activity of condensed tannins from the bark of Clausena lansium (Lour.) Skeels with antiproliferative and apoptotic properties in B16 mouse melanoma cells[J]. Process Biochemistry,2019,86:205−214. doi: 10.1016/j.procbio.2019.08.005
[14]	耿江枫. 苦丁茶冬青胰脂肪酶抑制活性成分研究[D]. 贵阳: 贵州师范大学, 2016.
[15]	Du X, Bai M, Huang Y, et al. Inhibitory effect of astaxanthin on pancreatic lipase with inhibition kinetics integrating molecular docking simulation[J]. Journal of Functional Foods,2018,48:551−557. doi: 10.1016/j.jff.2018.07.045
[16]	Wang Y, Zhang G, Yan J, et al. Inhibitory effect of morin on tyrosinase: Insights from spectroscopic and molecular docking studies[J]. Food Chemistry,2014,163:226−233. doi: 10.1016/j.foodchem.2014.04.106
[17]	王远, 郑雯, 蔡珺珺, 等. 辣木叶黄酮结构分析及其对胰脂肪酶的抑制作用[J]. 食品科学,2018,39(2):31−37. doi: 10.7506/spkx1002-6630-201802006
[18]	孔霄, 高春燕. 地参游离酚对α-葡萄糖苷酶和胰脂肪酶的抑制作用研究[J]. 中国预防医学杂志,2018,19(8):564−568.
[19]	王静, 刁翠茹, 王华丽, 等. 鼠尾草酸对α-淀粉酶的抑制作用[J]. 食品科学,2020,41(3):12−17. doi: 10.7506/spkx1002-6630-20181211-137
[20]	张静, 米佳, 禄璐, 等. 黑果枸杞花色苷提取物对胰脂肪酶活性的影响[J]. 食品科学,2020,41(5):8−14. doi: 10.7506/spkx1002-6630-20190620-234
[21]	Cioni F, Maioli C. Evaluation of the tolerability and efficacy of a noncompetitive, reversible inhibitor of the alpha-amylase and alpha-glucosidase enzymes with a specific, standardized polyphenolic composition on the modulation of postprandial glycemic peaks in overweight patients with impaired fasting glucose[J]. Progress In Nutrition,2018,20(2):290−297.
[22]	Huang W Y, Chen H J, Lin C C, et al. Kinetics investigation on mushroom tyrosinase inhibition of proso millet[J]. Journal of Chemistry,2018,2018:1−5.
[23]	丁小梅, 何善生, 王力, 等. 螺旋藻多糖对酪氨酸酶的抑制作用及抗氧化性能[J]. 中国食品学报,2019,19(10):86−92.
[24]	张丽娜. 水翁花对胰脂肪酶和α-淀粉酶抑制活性及作用机制初步探讨[D]. 上海: 华东理工大学, 2012.
[25]	吴忠高, 倪辉, 杨远帆, 等. 茶花粉提取物抑制α-淀粉酶活性的研究[J]. 中国农学通报,2016,32(26):27−32. doi: 10.11924/j.issn.1000-6850.casb16030116
[26]	Yang Y F, Sun X, Ni H, et al. Identification and characterization of the tyrosinase inhibitory activity of caffeine from camellia pollen[J]. Journal of Agricultural and Food Chemistry,2019,67(46):12741−12751. doi: 10.1021/acs.jafc.9b04929
[27]	Polzonetti V, Egidi D, Vita A, et al. Involvement of oleuropein in (some) digestive metabolic pathways[J]. Food Chemistry,2004,88(1):11−15. doi: 10.1016/j.foodchem.2004.01.029
[28]	Taha M, Ismail N H, Lalani S, et al. Synthesis of novel inhibitors of alpha-glucosidase based on the benzothiazole skeleton containing benzohydrazide moiety and their molecular docking studies[J]. European Journal of Medicinal Chemistry,2015,92:387−400. doi: 10.1016/j.ejmech.2015.01.009
[29]	Hemachandran H, Anantharaman A, Mohan S, et al. Unraveling the inhibition mechanism of cyanidin-3-sophoroside on polyphenol oxidase and its effect on enzymatic browning of apples[J]. Food Chemistry,2017,227:102−110. doi: 10.1016/j.foodchem.2017.01.041
[30]	Hermoso J, Pignol D, Kerfelec B, et al. Lipase activation by nonionic detergents: The crystal structure of the porcine lipase-cloipase[J]. Journal of Biological Chemistry,1996,271(30):18007−18016. doi: 10.1074/jbc.271.30.18007
[31]	Yu H, Dong S, Wang L, et al. The effect of triterpenoid saponins on pancreatic lipase in vitro: Activity, conformation, kinetics, thermodynamics and morphology[J]. Biochemical Engineering Journal,2017,125:1−9. doi: 10.1016/j.bej.2017.05.010