Peptide profiles and antioxidant capacity of extensive hydrolysates of milk protein concentrate
ABSTRACT: Milk protein concentrate was hydrolyzed using one-step enzymatic hydrolysis. Both the peptide profiles and antioxidant activities of the resulting extensive hydrolysates of milk protein concentrate (EMPH) were analyzed using a peptidomics approach based on liquid chromatography–tandem mass...
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Elsevier
2022-10-01
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Series: | Journal of Dairy Science |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S0022030222004702 |
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author | Qiang Cui Yuqing Duan Mengjie Zhang Shuxia Liang Yuxue Sun Jianjun Cheng Mingruo Guo |
author_facet | Qiang Cui Yuqing Duan Mengjie Zhang Shuxia Liang Yuxue Sun Jianjun Cheng Mingruo Guo |
author_sort | Qiang Cui |
collection | DOAJ |
description | ABSTRACT: Milk protein concentrate was hydrolyzed using one-step enzymatic hydrolysis. Both the peptide profiles and antioxidant activities of the resulting extensive hydrolysates of milk protein concentrate (EMPH) were analyzed using a peptidomics approach based on liquid chromatography–tandem mass spectrometry. The results demonstrated that the degrees of hydrolysis of the 4 EMPH by Alcalase-Protamex, Alcalase-Protease A 2SD, Alcalase-Flavorzyme, and Alcalase-ProteAXH were 12.02%, 16.85%, 15.87%, and 15.77%, respectively. Using size exclusion chromatography, 99.85% of the peptides in the Alcalase-Protease A 2SD hydrolysate were shown to have a molecular weight of <3 kDa. A total of 33 common peptides were identified in the EMPH by liquid chromatography–tandem mass spectrometry, 16 of which were identified as bioactive peptides using bioinformatics. The peptide profiles and the coverage of master proteins of the 4 EMPH were different. The EMPH also exhibited strong free radical scavenging capacity, as indicated by the results of the 1,1-diphenyl-2-picrylhydrazyl radical, 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid), hydroxyl radical, and reducing power assays. The results of this study provided useful information on the peptide profiles and antioxidant activity of EMPH. |
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issn | 0022-0302 |
language | English |
last_indexed | 2024-04-11T20:32:31Z |
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publisher | Elsevier |
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series | Journal of Dairy Science |
spelling | doaj.art-93fbf05f8d32482bbf432ecfb2c127ee2022-12-22T04:04:27ZengElsevierJournal of Dairy Science0022-03022022-10-011051079727985Peptide profiles and antioxidant capacity of extensive hydrolysates of milk protein concentrateQiang Cui0Yuqing Duan1Mengjie Zhang2Shuxia Liang3Yuxue Sun4Jianjun Cheng5Mingruo Guo6College of Food Science, Northeast Agricultural University, Harbin 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, China; Jiangsu Daisy FSMP Co. Ltd., Nantong 226133, ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, China; Corresponding authorsCollege of Food Science, Northeast Agricultural University, Harbin 150030, China; Department of Nutrition and Food Sciences, College of Agriculture and Life Sciences, University of Vermont, Burlington 05405; Corresponding authorsABSTRACT: Milk protein concentrate was hydrolyzed using one-step enzymatic hydrolysis. Both the peptide profiles and antioxidant activities of the resulting extensive hydrolysates of milk protein concentrate (EMPH) were analyzed using a peptidomics approach based on liquid chromatography–tandem mass spectrometry. The results demonstrated that the degrees of hydrolysis of the 4 EMPH by Alcalase-Protamex, Alcalase-Protease A 2SD, Alcalase-Flavorzyme, and Alcalase-ProteAXH were 12.02%, 16.85%, 15.87%, and 15.77%, respectively. Using size exclusion chromatography, 99.85% of the peptides in the Alcalase-Protease A 2SD hydrolysate were shown to have a molecular weight of <3 kDa. A total of 33 common peptides were identified in the EMPH by liquid chromatography–tandem mass spectrometry, 16 of which were identified as bioactive peptides using bioinformatics. The peptide profiles and the coverage of master proteins of the 4 EMPH were different. The EMPH also exhibited strong free radical scavenging capacity, as indicated by the results of the 1,1-diphenyl-2-picrylhydrazyl radical, 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid), hydroxyl radical, and reducing power assays. The results of this study provided useful information on the peptide profiles and antioxidant activity of EMPH.http://www.sciencedirect.com/science/article/pii/S0022030222004702peptide profileantioxidant capacityliquid chromatography–tandem mass spectrometrymilk protein concentrate |
spellingShingle | Qiang Cui Yuqing Duan Mengjie Zhang Shuxia Liang Yuxue Sun Jianjun Cheng Mingruo Guo Peptide profiles and antioxidant capacity of extensive hydrolysates of milk protein concentrate Journal of Dairy Science peptide profile antioxidant capacity liquid chromatography–tandem mass spectrometry milk protein concentrate |
title | Peptide profiles and antioxidant capacity of extensive hydrolysates of milk protein concentrate |
title_full | Peptide profiles and antioxidant capacity of extensive hydrolysates of milk protein concentrate |
title_fullStr | Peptide profiles and antioxidant capacity of extensive hydrolysates of milk protein concentrate |
title_full_unstemmed | Peptide profiles and antioxidant capacity of extensive hydrolysates of milk protein concentrate |
title_short | Peptide profiles and antioxidant capacity of extensive hydrolysates of milk protein concentrate |
title_sort | peptide profiles and antioxidant capacity of extensive hydrolysates of milk protein concentrate |
topic | peptide profile antioxidant capacity liquid chromatography–tandem mass spectrometry milk protein concentrate |
url | http://www.sciencedirect.com/science/article/pii/S0022030222004702 |
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