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Amino Acid Composition and Antioxidant Properties of Pea Seed (Pisum sativum L.) Enzymatic Protein Hydrolysate Fractions
Abstract
The amino acid composition and antioxidant activities of peptide fractions obtained from HPLC separation of a pea protein hydrolysate (PPH) were studied. Thermolysin hydrolysis of pea protein isolate and ultrafiltration (3 kDa molecular weight cutoff membrane) yielded a PPH that was separated into five fractions (F1-F5) on a C(18) reverse phase HPLC column. The fractions that eluted later from the column (F3-F5) contained higher contents hydrophobic and aromatic amino acids when compared to fractions that eluted early or the original PPH. Fractions F3-F5 also exhibited the strongest radical scavenging and metal chelating activities; however, hydrophobic character did not seem to contribute to reducing power of the peptides. In comparison to glutathione, the peptide fractions had significantly higher (p < 0.05) ability to inhibit linoleic acid oxidation and chelate metals. In contrast, glutathione had significantly higher (p < 0.05) free radical scavenging properties than the peptide fractions.
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Cites
The Chemistry behind Antioxidant Capacity Assays
Huang, D., Ou, B., & Prior, R. L. (2005) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf030723c · Cited by 6,162
[1] Role of free radicals and catalytic metal ions in human disease: An overview
Halliwell, B., & Gutteridge, J. M. C. (1990) · Methods in Enzymology · doi:10.1016/0076-6879(90)86093-b · Cited by 4,994
Transition metals as catalysts of “autoxidation” reactions
Miller, D. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90148-c · Cited by 739
Research works printed but not linked: 33
- Agriculture and Agri-Food Canada. Bi-weekly bulletin − dry peas: situation and outlook;http://www.manitobapulse.ca/pdf/market_report-DryPeasBulletin.pdf, viewed Aug 1, 2009.
- Iqbal A., 2006, Food Chem., 97, 331, 10.1016/j.foodchem.2005.05.011 · DOI · Paper page
- Wang T. L., 2003, Plant Physiol., 131, 886, 10.1104/pp.102.017665 · DOI · Paper page
- Aluko R. E., 2008, J. AOAC Int., 91, 947, 10.1093/jaoac/91.4.947 · DOI
- Korhonen H., 2003, Curr. Pharm. Des., 9, 1297, 10.2174/1381612033454892 · DOI · Paper page
- Je J.-Y., 2008, J. Med. Food, 11, 629, 10.1089/jmf.2007.0114 · DOI
- Li Y., 2008, Food Chem., 106, 444, 10.1016/j.foodchem.2007.04.067 · DOI · Paper page
- Bidlingmeyer B., 1984, J. Chromatogr., 336, 93, 10.1016/S0378-4347(00)85133-6 · DOI · Paper page
- Gehrke C., 1985, J. Assoc. Off. Anal. Chem., 68, 811
- Landry J., 1992, J. Agric. Food Chem., 40, 776, 10.1021/jf00017a014 · DOI
- Aluko R. E., 2003, J. Food Sci., 68, 1254, 10.1111/j.1365-2621.2003.tb09635.x · DOI · Paper page
- Zhang S. B., 2008, J. Am. Oil Chem. Soc., 85, 521, 10.1007/s11746-008-1217-y · DOI
- Theodore A. E., 2008, J. Agric. Food Chem., 56, 7459, 10.1021/jf800185f · DOI
- Udenigwe C. C., 2009, Food Chem., 116, 277, 10.1016/j.foodchem.2009.02.046 · DOI
- Guo H., 2009, Food Chem., 113, 238, 10.1016/j.foodchem.2008.06.081 · DOI · Paper page
- Xie Z., 2008, Food Chem., 111, 370, 10.1016/j.foodchem.2008.03.078 · DOI · Paper page
- Antonczak S., 2000, J. Mol. Model., 6, 527, 10.1007/s0089400060527 · doi:10.1007/s0089400060527
- Aluko R. E., 2004, Proteins in Food Processing, 323, 10.1533/9781855738379.2.323 · DOI
- Bougatef A., 2009, Food Chem., 114, 1198, 10.1016/j.foodchem.2008.10.075 · DOI · Paper page
- Prior R. L., 2005, J. Agric. Food Chem., 53, 4290, 10.1021/jf0502698 · DOI · Paper page
- Liu Y.-W., 2003, J. Agric. Food Chem., 51, 4389, 10.1021/jf030016j · doi:10.1021/jf030016j
- Humiski L. M., 2007, J. Food Sci., 72, S605, 10.1111/j.1750-3841.2007.00475.x · DOI
- Tang C. H., 2009, Food Chem., 115, 672, 10.1016/j.foodchem.2008.12.068 · DOI
- Yan X., 1999, J. Agric. Food Chem., 47, 4711, 10.1021/jf981305o · DOI
- Li M., 2003, Biochem. Biophys. Res. Commun., 312, 316, 10.1016/j.bbrc.2003.10.116 · DOI
- Dong S., 2008, Food Chem., 107, 1485, 10.1016/j.foodchem.2007.10.011 · DOI · Paper page
- Megias C., 2008, LWT−Food Sci. Technol., 41, 1973
- Li B., 2007, Food Chem., 102, 1135, 10.1016/j.foodchem.2006.07.002 · DOI · Paper page
- Chang C., 2007, Food Chem., 100, 1537, 10.1016/j.foodchem.2005.12.019 · DOI
- Zhang S. B., 2007, J. Am. Oil Chem. Soc., 84, 693, 10.1007/s11746-007-1080-2 · DOI
- You L., 2009, Innovative Food Sci. Emerg. Technol., 10, 235, 10.1016/j.ifset.2008.08.007 · DOI · Paper page
- Jayaprakasha G. K., 2001, Food Chem., 73, 285, 10.1016/S0308-8146(00)00298-3 · DOI · Paper page
- Chen G., 2007, J. Sci. Food Agric., 87, 357, 10.1002/jsfa.2744 · DOI
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Composition, physicochemical properties of pea protein and its application in functional foods
Lu, Z. X., He, J. F., Zhang, Y. C., & Bing, D. J. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2019.1651248 · Cited by 529
Tong, X., Cao, J., Tian, T., Lyu, B., Miao, L., Lian, Z., Cui, W., Liu, S., Wang, H., & Jiang, L. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.107084 · Cited by 318
Ge, J., Sun, C., Corke, H., Gul, K., Gan, R., & Fang, Y. (2020) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12573 · Cited by 318
Rizzello, C. G., Tagliazucchi, D., Babini, E., Sefora Rutella, G., Taneyo Saa, D. L., & Gianotti, A. (2016) · Journal of Functional Foods · doi:10.1016/j.jff.2016.09.023 · Cited by 250
Bioactive peptides in cereals and legumes: agronomical, biochemical and clinical aspects.
Malaguti, M., Dinelli, G., Leoncini, E., Bregola, V., Bosi, S., Cicero, A., & Hrelia, S. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151121120 · Cited by 180
Metadata
- Authors
- Pownall, T. L., Udenigwe, C. C., & Aluko, R. E.
- Venue
- Journal of Agricultural and Food Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-04-01
- Volume
- 58
- Issue
- 8
- Pages
- 4712-4718
- ISSN
- 0021-8561 (ISSN-L)
- 1520-5118
- OpenAlex
- W1977114185
- Cited by
- 479
- References
- 3
- FWCI
- 6.50
- Type
- journal article
- Language
- en
- Open access
- closed
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