In this study Roselle seed protein isolates were digested using pepsin followed by pancreatin at different time in order to produce hydrolysate with good antioxidant. The prepared hydrolysates were as effective as antioxidants in model systems, in scavenging of free radicals. This effect was concentration-dependent and was also influenced by the hydrolysis time. Among all the hydrolysates, the 3 hours Roselle seed protein hydrolysate showed the highest antioxidant activity. Then it was separated into four fractions (I, II, III and IV) by filtration on Sephadex G-15. The antioxidant activities of the fractions were investigated using different in vitro methods. All fractions were effective antioxidants, with fraction III showing the highest antioxidant activity. The Reverse phase high performance liquid chromatography purification was then performed to the fraction (FIII). From the resultant, five isolated peptides from the active peak (FIII-3), were identified by liquid chromatography/ tandem mass spectrometry (LC-MS/MS), to contain Thr-Val-Glu-Asn-Leu/ Ala-Leu-Gly-Ala-Asp-Cys-Asp-Val/ Tyr-Thr-Met-Phe-Ser-Thr-Ser-Trp-Phe/ His-Asn-Asp-Pro-Glu-Phe/ Thr-Pro-Glu-Cys-Asn-Val amino acid structural sequences. The study confirmed that peptides with strong antioxidant activities from Roselle seed protein can be successfully provided through enzymatic digestion. In addition, five purified peptides are mainly responsible for the potent free radical scavenging of the fraction and the hydrolysate. Thus, they could be included as antioxidant constituents in the food industry due to their role in food quality preservation and would be expected to protect against oxidative damage in living systems. For the first time, antioxidant peptides were purified and identified from prepared Roselle seed protein hydrolysates.
| Published in | Journal of Food and Nutrition Sciences (Volume 10, Issue 4) |
| DOI | 10.11648/j.jfns.20221004.11 |
| Page(s) | 97-105 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2024. Published by Science Publishing Group |
Roselle-Seeds, Protein- Hydrolysates, Identification, Antioxidative-Peptides
| [1] | Wong, F C, Xiao, J, Wang, S, Ee, K Y, & Chai, TT. (2020). Advances on the antioxidant peptides from edible plant sources. Trends in Food Science & Technology, 99: 44–57. doi: 10.1016/j.tifs.2020.02.012. |
| [2] | Chen, Z, Tian, R, She, Z, Cai, J & Li, H. (2020). Role of oxidative stress in the pathogenesis of nonalcoholic fatty liver disease. Free Rdical Biology and Medecine, 152: 116-141. doi: 10.1016/j.freeradbiomed.2020.06.011. |
| [3] | Yang, X R, Zhang, L, Zhao, Y Q, Chi, C F & Wang, B. (2019). Preparation and characterization of antioxidant peptides from protein hydrolysate of blood cockle (Tegillarca granosa) digested by neutrase and alcalase. Marine Drugs, 17: 251. doi: 10.3390/md17050251. |
| [4] | Cho, H R & Lee, S O. (2020). Novel hepatoprotective peptides derived from protein hydrolysates of mealworm (Tenebrio molitor). Food Research International, 133: 109194. doi: 10.1016/j.foodres.2020.109194. |
| [5] | Botterweck, A A, Verhagen, H, Goldbohm, R A, Kleinjans, J & van den Brandt, P A. (2000). Intake of butylated hydroxyanisole and butylated hydroxytoluene and stomach cancer risk: results from analyses in the Netherlands Cohort Study. Food Chemistry and Toxicology, 38, 599-605. doi: 10.1016/S0278-6915(00)00042-9. |
| [6] | Peng, X., Xiong, YL, & Kong, B. (2009). Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance. Food Chemistry, 113 (1), 196-201. doi: 10.1016/j.foodchem.2008.07.068. |
| [7] | Reuter, S, Gupta, S C, Chaturvedi, M M & Aggarwal, B B. (2010). Oxidative stress, inflammation, and cancer: how are they linked? Free Radic. Biol. Med. 49, 1603–1616. doi: 10.1016/j.freeradbiomed.2010.09.006. |
| [8] | Liu, C, Ren, D, Li, J, Fang, L, Wang, J, Liu, J & Min, W. (2018). Cytoprotective effect and purification of novel antioxidant peptides from hazelnut (C. heterophylla Fisch) protein hydrolysates. Journal of Functional Foods, 42: 203-215. doi: 10.1016/j.jff.2017.12.003. |
| [9] | Pihlanto-Leppälä, A. (2001). Bioactive peptides derived from bovine whey proteins:opioid and ace-inhibitory peptides. Trends in Food Science and Technology, 11 (9-10), 347-356. Doi: 10.1016/S0924-2244(01)00003-6. |
| [10] | Tsuruki, T, Kishi, K, Takahashi, M, Tanaka, M, Matsukawa, T & Yoshikawa, M. (2003). Soymetide an immunostimulating peptide derived from soybean ß-conglycinin, is an fMLP agonist. FEBS Letters, 540 (1-3), 206-210. doi: 10.1016/s0014-5793(03)00265-5. |
| [11] | Mendis, E, Rajapakse, N & Kim, S. 2005. Antioxidant properties of a radical scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate. Journal of Agricicultural and Food Chemistry, 53 (3), 581-587. doi: 10.1021/jf048877v. |
| [12] | Suetsuna, K., Maekawa, K & Chen, J R. (2004). Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats. Journal of Nutritional Biochemistry. 15 (5), 267- 272. doi: 10.1016/j.jnutbio.2003.11.004. |
| [13] | Suetsuna, K. (1998). Isolation and characterization of angiotensin I-converting enzyme inhibitor dipeptides derived from Allium sativum L (garlic). Journal of Nutritional Biochemistry, 9 (7), 415-419. doi: 10.1016/S0955-2863(98)00036-9. |
| [14] | Kim, SY, Je, JY & Kim, SK. (2007). Purification and characterization of antioxidant peptide from hoki (Johnius belengerii) frame protein by gastrointestinal digestion. Journal of Nutritional Biochemistry. 18 (1), 31- 38. doi: 10.1016/j.jnutbio.2006.02.006. |
| [15] | Zhang, J, Zhang, H, Wang, L, Guo, X. N, Wang X & Yao, H. (2010). Isolation and identification of antioxidative peptides from rice endosperm protein enzymatic hydrolysate by consecutive chromatography and MALDI-TOF/TOF MS/MS. Food Chemistry, 119 (1), 226–234. doi: 10.1016/J.FOODCHEM.2009.06.015. |
| [16] | Chen, GT, Zhao, L, Zhao, LY, Cong T & Bao, S F. (2007). In vitro study on antioxidant activities of peanut protein hydrolysate. Journal of the Science of Food and Agriculture, 87 (2), 357–362. doi: 10.1002/jsfa.2744. |
| [17] | Moure, A, Domínguez, H & Parajó, JC. (2005). Fractionation and enzymatic hydrolysis of soluble protein present in waste liquors from soy processing. Journal of Agricicultural and Food Chemistry. 53 (19), 7600-8. doi: 10.1021/jf0505325. |
| [18] | Li, XX, Han, LJ & Chen, LJ. (2008). In vitro antioxidant activity of proteinhydrolysates prepared from corn gluten meal. Journal of the Science of Food and Agriculture, 88 (9), 1660-1666. doi: 10.1002/jsfa.3264. |
| [19] | Vioque, J, Weinbrenner, T, Castello, A, Asensio L & Garcia de la, HM. (2008). Intake of fruits and vegetables in relation to 10-year weight gain among Spanish adults. Obesity, 16 (3), 664-670. doi: 10.1038/oby.2007.121. |
| [20] | Tounkara, F., Bashari, M, Le. GW & Shi, YH. (2014). Antioxidant Activities of Roselle (Hibiscus sabdariffa L.) Seed Protein Hydrolysate and its Derived peptide Fractions. International Journal of Food Properties, 17 (9), 1998-2011. doi: 10.1080/10942912.2013.779700. |
| [21] | El-Tinay, AH, Nour, AM, Abdel-Karim, SH & Mahgoub SO. (1988). Aqueous protein and gossypol extraction from glanded cottonseed flour: Factors affecting protein extraction. Food Chemistry, 29 (1), 57-63. doi: 10.1016/0308-8146(88)90076-3. |
| [22] | AOAC., 1990. Official Method of Analysis. 15th edn.; Association of official Analytical chemistry. Washington, D.C., USA. pp: 805-845. |
| [23] | Shahidi, F, Liyana-Pathirana, CM & Wall, DS. (2006). Antioxidant activity of white and black sesame seeds and their hull fractions. Food Chemistry, 99 (3), 478-483. Doi: 10.1016/j.foodchem.2005.08.009. |
| [24] | You, L, Zhao, M, Regenstein, JM & Ren, J. (2010). Purification and identification of antioxidative peptides from loach (Misgurnus anguillicaudatus) protein hydrolysate by consecutive chromatography and electrospray ionization–mass spectrometry. Food Research International, 43 (4), 1167-117. doi: 10.1016/j.foodres.2010.02.009. |
| [25] | Nagai, T, Inoue, R, Inoue, H & Suzuki. N. (2002). Scavenging capacities of pollen extracts from cistus ladaniferus on autoxidation, superoxide radicals, hydroxyl radicals, and DPPH radicals. Nutrition Research, 22 (4), 519-526. doi: 10.1016/S0271-5317(01)00400-6. |
| [26] | Nazeer, RA &. Deeptha, R. (2013). Antioxidant Activity and Amino Acid Profiling of Protein Hydrolysates from the Skin of Sphyraena barracuda and Lepturacanthus savala. International Journal of Food Properties, 16 (3), 500-511. doi: 10.1080/10942912.2011.553757. |
| [27] | Roberts, PR, Burney, JD, Black, KW & Zaloga, GP. (1999). Effect of chain length on absorption of biologically active peptides from the gastrointestinal tract. Digestion, 60 (4), 332-337. doi: 10.1159/000007679. |
| [28] | Rajapakse, N, Mendis, E, Jung, WK, Je JY & Kim, SK. 2005. Purification of a radical scavenging peptide from fermented mussel sauce and its antioxidant properties. Food Research International, 38 (2), 175-182. doi: 10.1016/j.foodres.2004.10.002. |
| [29] | Kumar, NSS, Nazeer, RA & Jaiganesh, R. (2011). Purification and biochemical characterization of antioxidant peptide from horse mackerel (Magalaspis cordyla) viscera protein. Peptides, 32 (7), 1496–501. doi: 10.1016/j.peptides.2011.05.020. |
| [30] | Zhu, K., Zhou H & Qian, H. (2006). Antioxidant and free radical scavenging activities of wheat germ protein hydrolysates (WGPH) prepared with alcalase. Process Biochemistry, 41 (6), 1296-1302. doi: 10.1016/j.procbio.2005.12.029. |
| [31] | Zhu, L, Chen, J, Tang, X & Xiong, YL. (2008). Reducing, radical scavenging and chelation properties of in vitro digests of Alcalase-treated zein hydrolysate. Journal of Agriculture and Food Chemistry, 56 (8), 2714- 2721. doi: 10.1021/jf703697e. |
| [32] | Hancock, JT, Desikan, R & Neill, S J. (2001). Role of reactive oxygen species in cell signaling pathways. Biochemical Society Transactions 29 (Pt2), 345-350. doi: 10.1042/BST0290345. |
| [33] | Saiga, Ai., Tanabe, S, Nishimura, T. (2003). Antioxidant activity of peptides from porcine myofibrillar proteins by protease treatment. Journal of Agriculture and Food Chemistry. 51 (12), 3661-3667. doi: 10.1021/jf021156g. |
| [34] | Rajapakse, N, Mendis, E, Byun, HG & Kim, SK. (2005). Purification and in vitro antioxidative effects of giant squid muscle peptides on free radical mediated oxidative systems. Journal of Nutritional Biochemistry, 16 (9), 562-569. doi: 10.1016/j.jnutbio.2005.02.005. |
| [35] | Je, JY, Park, PJ & Kim, SK. 2005. Antioxidant activity of peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate. Food Research International 38 (1), 45-50. doi: 10.1016/j.foodres.2004.07.005. |
| [36] | Yu, L, Haley, S, Perret, J, Harris, M, Wilson J & Qian M. (2002). Free radical scavenging properties of wheat extracts. Journal of Agriculture and Food Chemistry, 50 (6), 1619-1624. doi: 10.1021/jf010964p. |
APA Style
Fatoumata Tounkara, Issiaka Togola, Mamadou Abdoulaye Konare, Mah Moutaga Fane. (2022). Identification of Antioxidative Peptides from Roselle (Hibiscus Sabdariffa Linn) Seeds Protein Hydrolysates. Journal of Food and Nutrition Sciences, 10(4), 97-105. https://doi.org/10.11648/j.jfns.20221004.11
ACS Style
Fatoumata Tounkara; Issiaka Togola; Mamadou Abdoulaye Konare; Mah Moutaga Fane. Identification of Antioxidative Peptides from Roselle (Hibiscus Sabdariffa Linn) Seeds Protein Hydrolysates. J. Food Nutr. Sci. 2022, 10(4), 97-105. doi: 10.11648/j.jfns.20221004.11
Share This Article
Twitter
Linked In
Facebook
Copy
Download@article{10.11648/j.jfns.20221004.11,
author = {Fatoumata Tounkara and Issiaka Togola and Mamadou Abdoulaye Konare and Mah Moutaga Fane},
title = {Identification of Antioxidative Peptides from Roselle (Hibiscus Sabdariffa Linn) Seeds Protein Hydrolysates},
journal = {Journal of Food and Nutrition Sciences},
volume = {10},
number = {4},
pages = {97-105},
doi = {10.11648/j.jfns.20221004.11},
url = {https://doi.org/10.11648/j.jfns.20221004.11},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.jfns.20221004.11},
abstract = {In this study Roselle seed protein isolates were digested using pepsin followed by pancreatin at different time in order to produce hydrolysate with good antioxidant. The prepared hydrolysates were as effective as antioxidants in model systems, in scavenging of free radicals. This effect was concentration-dependent and was also influenced by the hydrolysis time. Among all the hydrolysates, the 3 hours Roselle seed protein hydrolysate showed the highest antioxidant activity. Then it was separated into four fractions (I, II, III and IV) by filtration on Sephadex G-15. The antioxidant activities of the fractions were investigated using different in vitro methods. All fractions were effective antioxidants, with fraction III showing the highest antioxidant activity. The Reverse phase high performance liquid chromatography purification was then performed to the fraction (FIII). From the resultant, five isolated peptides from the active peak (FIII-3), were identified by liquid chromatography/ tandem mass spectrometry (LC-MS/MS), to contain Thr-Val-Glu-Asn-Leu/ Ala-Leu-Gly-Ala-Asp-Cys-Asp-Val/ Tyr-Thr-Met-Phe-Ser-Thr-Ser-Trp-Phe/ His-Asn-Asp-Pro-Glu-Phe/ Thr-Pro-Glu-Cys-Asn-Val amino acid structural sequences. The study confirmed that peptides with strong antioxidant activities from Roselle seed protein can be successfully provided through enzymatic digestion. In addition, five purified peptides are mainly responsible for the potent free radical scavenging of the fraction and the hydrolysate. Thus, they could be included as antioxidant constituents in the food industry due to their role in food quality preservation and would be expected to protect against oxidative damage in living systems. For the first time, antioxidant peptides were purified and identified from prepared Roselle seed protein hydrolysates.},
year = {2022}
}
TY - JOUR T1 - Identification of Antioxidative Peptides from Roselle (Hibiscus Sabdariffa Linn) Seeds Protein Hydrolysates AU - Fatoumata Tounkara AU - Issiaka Togola AU - Mamadou Abdoulaye Konare AU - Mah Moutaga Fane Y1 - 2022/07/12 PY - 2022 N1 - https://doi.org/10.11648/j.jfns.20221004.11 DO - 10.11648/j.jfns.20221004.11 T2 - Journal of Food and Nutrition Sciences JF - Journal of Food and Nutrition Sciences JO - Journal of Food and Nutrition Sciences SP - 97 EP - 105 PB - Science Publishing Group SN - 2330-7293 UR - https://doi.org/10.11648/j.jfns.20221004.11 AB - In this study Roselle seed protein isolates were digested using pepsin followed by pancreatin at different time in order to produce hydrolysate with good antioxidant. The prepared hydrolysates were as effective as antioxidants in model systems, in scavenging of free radicals. This effect was concentration-dependent and was also influenced by the hydrolysis time. Among all the hydrolysates, the 3 hours Roselle seed protein hydrolysate showed the highest antioxidant activity. Then it was separated into four fractions (I, II, III and IV) by filtration on Sephadex G-15. The antioxidant activities of the fractions were investigated using different in vitro methods. All fractions were effective antioxidants, with fraction III showing the highest antioxidant activity. The Reverse phase high performance liquid chromatography purification was then performed to the fraction (FIII). From the resultant, five isolated peptides from the active peak (FIII-3), were identified by liquid chromatography/ tandem mass spectrometry (LC-MS/MS), to contain Thr-Val-Glu-Asn-Leu/ Ala-Leu-Gly-Ala-Asp-Cys-Asp-Val/ Tyr-Thr-Met-Phe-Ser-Thr-Ser-Trp-Phe/ His-Asn-Asp-Pro-Glu-Phe/ Thr-Pro-Glu-Cys-Asn-Val amino acid structural sequences. The study confirmed that peptides with strong antioxidant activities from Roselle seed protein can be successfully provided through enzymatic digestion. In addition, five purified peptides are mainly responsible for the potent free radical scavenging of the fraction and the hydrolysate. Thus, they could be included as antioxidant constituents in the food industry due to their role in food quality preservation and would be expected to protect against oxidative damage in living systems. For the first time, antioxidant peptides were purified and identified from prepared Roselle seed protein hydrolysates. VL - 10 IS - 4 ER -
Information
Email: