Login Register Cart 0
Generic placeholder image

Current Pharmaceutical Design

Editor-in-Chief

ISSN (Print): 1381-6128
ISSN (Online): 1873-4286

Back
Journal Home About Journal Editorial Board Journal Insight Current Issue Volumes/Issues
Subscribe
Research Article

A Novel Low Molecule Peptides-calcium Chelate from Silkworm Pupae Protein Hydrolysate: Preparation, Antioxidant Activity, and Bioavailability

Author(s): Xiao-Meng Xun, Zhi-Ang Zhang, Zi-Xuan Yuan, Kamila Tuhong, Cheng-Hai Yan, Yu-Fan Zhan, Si-Jie He, Shun-Hui Liu, Guo-Ping Kang and Jun Wang*

Volume 29, Issue 9, 2023

Published on: 07 April, 2023

Page: [675 - 685] Pages: 11

DOI: 10.2174/1381612829666230404134044

Price: $65

Abstract

Background: The antioxidant properties of active peptides from silkworm pupae protein hydrolysate are of interest, and it serves as a novel source of calcium supplement.

Methods: Optimize the preparation parameters of silkworm pupae bioactive peptide-calcium chelate, and investigate the mechanism and bioavailability of silkworm pupae active peptide as a transport carrier to promote calcium ion absorption using simulated gastrointestinal digestion and Caco-2 monolayer cell model.

Results: The optimal process parameters for preparing peptide calcium chelate were the peptide calcium mass ratio of 3:1, pH of 6.7, a temperature of 35.6°C, and time of 32.8 min by Box-Behnken design, and the calciumchelating rate reached 84.67%. The DPPH radical scavenging activity of silkworm pupae protein hydrolysatecalcium chelate was 79.36 ± 4.31%, significantly higher than silkworm pupae protein hydrolysate (61.00 ± 9.56%). Fourier transform infrared spectroscopy shows that the COO-, N-H, C-H, and C-O groups participated in the formation of silkworm pupae protein hydrolysate-calcium chelate. The particle size of the silkworm pupae protein hydrolysate-calcium chelate was 970.75 ± 30.12 nm, which was significantly higher than that of silkworm pupae protein hydrolysate (253.14 ± 5.72 nm). The silkworm pupae protein hydrolysate-calcium chelate showed a calcium dissolution rate of 71.01 ± 1.91% in the simulated intestinal phase, significantly higher than that of CaCl2 (59.34 ± 1.24%). In the Caco-2 cell monolayers, the silkworm pupae protein hydrolysatecalcium chelate was more favorable for calcium transport.

Conclusion: A novel silkworm pupa protein hydrolysate-calcium chelate with high antioxidant activity was successfully prepared to improve the bioavailability of calcium.

Keywords: Silkworm pupae protein hydrolysate, calcium chelating, DPPH radical scavenging activity, digestion, Caco-2 cell, antioxidant.

« Previous Next »
[1]
Shkembi B, Huppertz T. Calcium absorption from food products: Food matrix effects. Nutrients 2021; 14(1): 180.
[http://dx.doi.org/10.3390/nu14010180] [PMID: 35011055]
[2]
Palacios C, Cormick G, Hofmeyr GJ, Garcia-Casal MN, Peña-Rosas JP, Betrán AP. Calcium-fortified foods in public health programs: considerations for implementation. Ann N Y Acad Sci 2021; 1485(1): 3-21.
[http://dx.doi.org/10.1111/nyas.14495] [PMID: 32986887]
[3]
Sriram K, Lonchyna VA. Micronutrient supplementation in adult nutrition therapy: practical considerations. JPEN J Parenter Enteral Nutr 2009; 33(5): 548-62.
[http://dx.doi.org/10.1177/0148607108328470] [PMID: 19454751]
[4]
Beggs MR, Bhullar H, Dimke H, Alexander RT. The contribution of regulated colonic calcium absorption to the maintenance of calcium homeostasis. J Steroid Biochem Mol Biol 2022; 220: 106098.
[http://dx.doi.org/10.1016/j.jsbmb.2022.106098] [PMID: 35339651]
[5]
Aditya S, Stephen J, Radhakrishnan M. Utilization of eggshell waste in calcium-fortified foods and other industrial applications: A review. Trends Food Sci Technol 2021; 115: 422-32.
[http://dx.doi.org/10.1016/j.tifs.2021.06.047]
[6]
Diep TT, Yoo MJY, Rush E. Effect of in vitro gastrointestinal digestion on amino acids, polyphenols and antioxidant capacity of tamarillo yoghurts. Int J Mol Sci 2022; 23(5): 2526.
[http://dx.doi.org/10.3390/ijms23052526] [PMID: 35269670]
[7]
Hou T, Liu W, Shi W, Ma Z, He H. Desalted duck egg white peptides promote calcium uptake by counteracting the adverse effects of phytic acid. Food Chem 2017; 219: 428-35.
[http://dx.doi.org/10.1016/j.foodchem.2016.09.166] [PMID: 27765248]
[8]
Fu Y, Zhang Y, Soladoye OP, Aluko RE. Maillard reaction products derived from food protein-derived peptides: insights into flavor and bioactivity. Crit Rev Food Sci Nutr 2020; 60(20): 3429-42.
[http://dx.doi.org/10.1080/10408398.2019.1691500] [PMID: 31738577]
[9]
Liao W, Chen H, Jin W, Yang Z, Cao Y, Miao J. Three newly isolated calcium-chelating peptides from tilapia bone collagen hydrolysate enhance calcium absorption activity in intestinal Caco-2 cells. J Agric Food Chem 2020; 68(7): 2091-8.
[http://dx.doi.org/10.1021/acs.jafc.9b07602] [PMID: 31927882]
[10]
Liu G, Sun S, Guo B, et al. Bioactive peptide isolated from casein phosphopeptides promotes calcium uptake in vitro and in vivo. Food Funct 2018; 9(4): 2251-60.
[http://dx.doi.org/10.1039/C7FO01709J] [PMID: 29557438]
[11]
Sun N, Cui P, Lin S, et al. Characterization of sea cucumber (Stichopus japonicus) ovum hydrolysates: Calcium chelation, solubility and absorption into intestinal epithelial cells. J Sci Food Agric 2017; 97(13): 4604-11.
[http://dx.doi.org/10.1002/jsfa.8330] [PMID: 28349531]
[12]
Brogan EN, Park YL, Matak KE, Jaczynski J. Characterization of protein in cricket (Acheta domesticus), locust (Locusta migratoria), and silk worm pupae (Bombyx mori) insect powders. Lebensm Wiss Technol 2021; 152: 112314.
[http://dx.doi.org/10.1016/j.lwt.2021.112314]
[13]
Wu Q, Jia J, Yan H, Du J, Gui Z. A novel angiotensin-І converting enzyme (ACE) inhibitory peptide from gastrointestinal protease hydrolysate of silkworm pupa (Bombyx mori) protein: Biochemical characterization and molecular docking study. Peptides 2015; 68: 17-24.
[http://dx.doi.org/10.1016/j.peptides.2014.07.026] [PMID: 25111373]
[14]
Cermeño M, Bascón C, Amigo-Benavent M, Felix M, FitzGerald RJ. Identification of peptides from edible silkworm pupae (Bombyx mori) protein hydrolysates with antioxidant activity. J Funct Foods 2022; 92: 105052.
[http://dx.doi.org/10.1016/j.jff.2022.105052]
[15]
Zhang Y, Wang N, Wang W, Wang J, Zhu Z, Li X. Molecular mechanisms of novel peptides from silkworm pupae that inhibit α-glucosidase. Peptides 2016; 76: 45-50.
[http://dx.doi.org/10.1016/j.peptides.2015.12.004] [PMID: 26724364]
[16]
Bian YR, Li WJ, Pan LH, et al. Sweet-flavored peptides with biological activities from mulberry seed protein treated by multifrequency countercurrent ultrasonic technology. Food Chem 2022; 367: 130647.
[http://dx.doi.org/10.1016/j.foodchem.2021.130647] [PMID: 34343806]
[17]
Liu FR, Wang L, Wang R, Chen ZX. Calcium-binding capacity of wheat germ protein hydrolysate and characterization of Peptide-calcium complex. J Agric Food Chem 2013; 61(31): 7537-44.
[http://dx.doi.org/10.1021/jf401868z] [PMID: 23865522]
[18]
Pan LH, Peng QM, Li WJ, et al. Antioxidant peptides derived from mulberry seed protein by ionic liquid-enhanced microfluidic hydrolysis with immobilized protease. Biomass Convers Biorefin 2022; 12(10): 4435-47.
[http://dx.doi.org/10.1007/s13399-022-02410-7]
[19]
Cui P, Lin S, Han W, Jiang P, Zhu B, Sun N. Calcium delivery system assembled by a nanostructured peptide derived from the sea cucumber ovum. J Agric Food Chem 2019; 67(44): 12283-92.
[http://dx.doi.org/10.1021/acs.jafc.9b04522] [PMID: 31610118]
[20]
Perego S, Del Favero E, De Luca P, et al. Calcium bioaccessibility and uptake by human intestinal like cells following in vitro digestion of casein phosphopeptide–calcium aggregates. Food Funct 2015; 6(6): 1796-807.
[http://dx.doi.org/10.1039/C4FO00672K] [PMID: 25927875]
[21]
Huang W, Lan Y, Liao W, et al. Preparation, characterization and biological activities of egg white peptides-calcium chelate. Lebensm Wiss Technol 2021; 149: 112035.
[http://dx.doi.org/10.1016/j.lwt.2021.112035]
[22]
Kroll RD. Effect of pH on the binding of calcium ions by soybean proteins Cereal Chem 1984; 61(6): 490-5.
[23]
Yao MZ, Lu WL, Chen TG, et al. Effect of metals ions on thermostable alkaline phytase from Bacillus subtilis YCJS isolated from soybean rhizosphere soil. Ann Microbiol 2014; 64(3): 1123-31.
[http://dx.doi.org/10.1007/s13213-013-0751-5]
[24]
Wu H, Liu Z, Zhao Y, Zeng M. Enzymatic preparation and characterization of iron-chelating peptides from anchovy (Engraulis japonicus) muscle protein. Food Res Int 2012; 48(2): 435-41.
[http://dx.doi.org/10.1016/j.foodres.2012.04.013]
[25]
Wu W, He L, Liang Y, et al. Preparation process optimization of pig bone collagen peptide-calcium chelate using response surface methodology and its structural characterization and stability analysis. Food Chem 2019; 284: 80-9.
[http://dx.doi.org/10.1016/j.foodchem.2019.01.103] [PMID: 30744872]
[26]
Qi B, Chen X, Shen F, Su Y, Wan Y. Optimization of enzymatic hydrolysis of wheat straw pretreated by alkaline peroxide using response surface methodology. Ind Eng Chem Res 2009; 48(15): 7346-53.
[http://dx.doi.org/10.1021/ie8016863]
[27]
Li B, He H, Shi W, Hou T. Effect of duck egg white peptide-ferrous chelate on iron bioavailability in vivo and structure characterization. J Sci Food Agric 2019; 99(4): 1834-41.
[http://dx.doi.org/10.1002/jsfa.9377] [PMID: 30255570]
[28]
Yu Y, Fan D. Characterization of the complex of human-like collagen with calcium. Biol Trace Elem Res 2012; 145(1): 33-8.
[http://dx.doi.org/10.1007/s12011-011-9167-x] [PMID: 21842278]
[29]
Wang X, Gao A, Chen Y, Zhang X, Li S, Chen Y. Preparation of cucumber seed peptide-calcium chelate by liquid state fermentation and its characterization. Food Chem 2017; 229: 487-94.
[http://dx.doi.org/10.1016/j.foodchem.2017.02.121] [PMID: 28372205]
[30]
Zhao L, Huang S, Cai X, Hong J, Wang S. A specific peptide with calcium chelating capacity isolated from whey protein hydrolysate. J Funct Foods 2014; 10: 46-53.
[http://dx.doi.org/10.1016/j.jff.2014.05.013]
[31]
Farrell HM Jr, Qi PX, Wickham ED, Unruh JJ. Secondary structural studies of bovine caseins: structure and temperature dependence of beta-casein phosphopeptide (1-25) as analyzed by circular dichroism, FTIR spectroscopy, and analytical ultracentrifugation. J Protein Chem 2002; 21(5): 307-21.
[http://dx.doi.org/10.1023/A:1019992900455] [PMID: 12206505]
[32]
Qu W, Feng Y, Xiong T, Li Y, Wahia H, Ma H. Preparation of corn ACE inhibitory peptide-ferrous chelate by dual-frequency ultrasound and its structure and stability analyses. Ultrason Sonochem 2022; 83: 105937.
[http://dx.doi.org/10.1016/j.ultsonch.2022.105937] [PMID: 35144194]
[33]
Sun R, Liu X, Yu Y, Miao J, Leng K, Gao H. Preparation process optimization, structural characterization and in vitro digestion stability analysis of Antarctic krill (Euphausia superba) peptides-zinc chelate. Food Chem 2021; 340: 128056.
[http://dx.doi.org/10.1016/j.foodchem.2020.128056] [PMID: 33032152]
[34]
Luo J, Yao X, Soladoye OP, Zhang Y, Fu Y. Phosphorylation modification of collagen peptides from fish bone enhances their calcium-chelating and antioxidant activity. Lebensm Wiss Technol 2022; 155: 112978.
[http://dx.doi.org/10.1016/j.lwt.2021.112978]
[35]
Lin HM, Deng SG, Huang SB. Antioxidant activities of ferrous-chelating peptides isolated from five types of low-value fish protein hydrolysates. J Food Biochem 2014; 38(6): 627-33.
[http://dx.doi.org/10.1111/jfbc.12103]
[36]
Luo J, Zhou Z, Yao X, Fu Y. Mineral-chelating peptides derived from fish collagen: Preparation, bioactivity and bioavailability. Lebensm Wiss Technol 2020; 134: 110209.
[http://dx.doi.org/10.1016/j.lwt.2020.110209]
[37]
Udechukwu MC, Downey B, Udenigwe CC. Influence of structural and surface properties of whey-derived peptides on zinc-chelating capacity, and in vitro gastric stability and bioaccessibility of the zinc-peptide complexes. Food Chem 2018; 240: 1227-32.
[http://dx.doi.org/10.1016/j.foodchem.2017.08.063] [PMID: 28946246]
[38]
Zhang X, Jia Q, Li M, et al. Isolation of a novel calcium-binding peptide from phosvitin hydrolysates and the study of its calcium chelation mechanism. Food Res Int 2021; 141: 110169.
[http://dx.doi.org/10.1016/j.foodres.2021.110169] [PMID: 33642025]
[39]
Artursson P, Palm K, Luthman K. Caco-2 monolayers in experimental and theoretical predictions of drug transport1PII of original article: S0169-409X(96)00415-2. The article was originally published in Advanced Drug Delivery Reviews 22 (1996) 67–84.1. Adv Drug Deliv Rev 2001; 46(1-3): 27-43.
[http://dx.doi.org/10.1016/S0169-409X(00)00128-9] [PMID: 11259831]
[40]
Ranaldi G, Consalvo R, Sambuy Y, Scarino ML. Permeability characteristics of parental and clonal human intestinal Caco-2 cell lines differentiated in serum-supplemented and serum-free media. Toxicol In Vitro 2003; 17(5-6): 761-7.
[http://dx.doi.org/10.1016/S0887-2333(03)00095-X] [PMID: 14599474]
[41]
Li H, Duan S, Yuan P, et al. Preparation of casein phosphopeptides calcium complex and the promotion in calcium cellular uptake through transcellular transport pathway. J Food Biochem 2021; 45(12): e14001.
[http://dx.doi.org/10.1111/jfbc.14001] [PMID: 34751452]
[42]
Kheeree N, Kuptawach K, Puthong S, et al. Discovery of calcium-binding peptides derived from defatted lemon basil seeds with enhanced calcium uptake in human intestinal epithelial cells, Caco-2. Sci Rep 2022; 12(1): 4659.
[http://dx.doi.org/10.1038/s41598-022-08380-0] [PMID: 35304505]

Rights & Permissions Print Cite
Article Metrics
48
4
Wayfinder Image
© 2024 Bentham Science Publishers | Privacy Policy