Characterization of sea cucumber (<i>stichopus japonicus</i>) ovum hydrolysates: calcium chelation, solubility and absorption into intestinal epithelial cells

Journal of the Science of Food and Agriculture - Tập 97 Số 13 - Trang 4604-4611 - 2017
Na Sun1, Pengbo Cui1, Songyi Lin1, Cuiping Yu1, Yue Tang1, Wei Ye1, Youling L. Xiong2, Wengang Jin1
1School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian, PR China
2Department of Animal and Food Sciences, University of Kentucky, Lexington, KT, USA

Tóm tắt

AbstractBACKGROUNDSea cucumber (Stichopus japonicus) ovum hydrolysates (SCOHs) chelated with calcium were produced to investigate the characteristics of calcium binding and solubility, as well as to study any effects on calcium absorption by human intestinal epithelial cells.RESULTSThe results of the present study show that the calcium‐binding capacity of SCOHs depended greatly on the type of proteases. The maximum level of Ca binding (0.38 mmol L–1) occurred when trypsin was used, with a peptide yield of 85.7%. Investigation of the possible chelating modes between SCOHs and calcium ions indicated that calcium ions bound to SCOHs primarily via interactions with carboxyl oxygen and amino nitrogen atoms of Glu and Asp and also that the phosphoserine residues might be also responsible for SCOH–calcium chelation. Moreover, SCOH–calcium complexes maintained the solubility of calcium under simulated gastrointestinal digestion, regardless of the presence of dietary components such as oxalate. Furthermore, SCOH–Ca led to higher peak intracellular [Ca2+]i in both Caco‐2 cells (338.3 nmol L–1 versus 269.6 nmol L–1) and HT‐29 cells (373.9 nmol L–1 versus 271.7 nmol L–1) than casein phosphopeptide‐Ca.CONCLUSIONCarboxyl oxygen and amino nitrogen atoms in the SCOHs could bind calcium ions, forming SCOH–calcium complexes. These complexes improved calcium solubility under simulated gastrointestinal digestion and also promoted calcium absorption in Caco‐2 and HT‐29 cells. © 2017 Society of Chemical Industry

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Tài liệu tham khảo

10.1111/j.1467-2979.2010.00397.x

Fishery Bureau of the Ministry of Agriculture Chinese Fisheries Yearbook. China Agriculture Press Beijing pp. 29 (2016).

Mine Y, 2006, Nutraceutical Proteins and Peptides in Health and Disease

10.1146/annurev.physiol.69.031905.161003

10.1177/0115426507022003286

10.1016/j.lwt.2014.04.034

10.1021/jf502412f

10.1017/S0022029914000715

10.1111/j.1750-3841.2008.00673.x

10.1007/s00217-012-1809-5

10.1016/j.tifs.2016.10.004

10.1271/bbb1961.47.2415

10.1271/bbb.65.1187

Lee SH, 2009, Article isolation of a calcium‐binding peptide from enzymatic hydrolysates of porcine blood plasma protein, Appl Biol Chem, 52, 290

10.1007/s10068-012-0221-z

10.3168/jds.S0022-0302(04)73524-9

10.1021/jf505817a

Sato R, 2012, Characterization of phosphopeptide derived from bovine beta‐casein: an inhibitor to intra‐intestinal precipitation of calcium phosphate, Brachytherapy, 11, 144

10.1039/C4FO00672K

10.1016/j.jff.2013.01.032

10.1016/j.foodchem.2004.10.028

10.1111/j.1750-3841.2008.00873.x

10.1016/j.jff.2014.03.022

10.1271/bbb.60721

10.1079/BJN20051615

Horowitz W, 2002, Official Methods of Analysis of AOAC International

10.1021/jf205280y

10.1111/j.1365-2621.1996.tb14174.x

10.1002/jsfa.5534

10.1016/S0021-9258(19)52451-6

10.1021/jf401868z

10.1007/s00217-015-2579-7

10.1016/S0021-9258(18)83166-0

10.1016/j.foodchem.2015.02.046

10.1016/j.foodchem.2012.06.016

10.1021/jm070800l

10.3168/jds.2011-5282

10.1021/ic981012c

10.1039/C4FO00811A

10.1007/978-1-4615-7658-7

10.1021/ja0453782

10.1016/0928-0987(95)00007-Z

10.1016/S0899-9007(02)00829-8