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Exploring the Utilization of Bovine Blood as a Source of Antioxidant Peptide: Production, Concentration, Identification, and In Silico Gastrointestinal Digestion
This study delves into the pivotal industrial process of efficiently managing livestock waste. Specifically, the study concentrates on harnessing the potential of bovine blood through enzymatic hydrolysis to produce antioxidant peptides. The whole bovine blood sample, subjected to a 90°C heat treatm...
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Published in: | Food science of animal resources 2024, 44(6), , pp.1283-1304 |
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creator | Boonkong, Saruttiwong Luasiri, Pichitpon Pongsetkul, Jaksuma Suwanandgul, Saranya Chaipayang, Sukanya Molee, Wittawat Sangsawad, Papungkorn |
description | This study delves into the pivotal industrial process of efficiently managing livestock waste. Specifically, the study concentrates on harnessing the potential of bovine blood through enzymatic hydrolysis to produce antioxidant peptides. The whole bovine blood sample, subjected to a 90°C heat treatment for 30 min, underwent hydrolysis utilizing various commercial enzymes, alcalase, neutrase, and papain. Through neutrase hydrolysis (BB-N), we identified optimized conditions crucial for achieving heightened antioxidant activities and 40% protein recovery. Ultrafiltration with a molecular weight cutoff of 3 kDa was employed to concentrate the BB-N peptide, demonstrating the highest antioxidant and protein yield. The gel electrophoresis profile confirmed the denaturation of key proteins like albumin, globulin, and fibrinogen before digestion, while the BB-N derived after digestion contained peptides below 16 kDa. Post-concentration, the permeation of UF-3 kDa underwent purification, and the peptide sequence was discerned using liquid chromatography with tandem mass spectrometry. The exploration identified nine novel peptides- IWAGK, VDLL, MTTPNK, MPLVR, KIII, LPQL, TVIL, DFPGLQ, and VEDVK. Notably, the IWAGK sequence emerged as the most potent antioxidant activity peptide. Subsequent
gastrointestinal digestion predicted structural changes in these peptides. While IWAGK, VDLL, MPLVR, LPQL, TVIL, and DFPGLQ could be fragmented into bioactive dipeptides and tripeptides, MTTPNK, KIII, and VEDVK exhibited resistance, suggesting potential circulation through the bloodstream to reach the target organ. Consequently, our study explores the potential use of BB-N as a novel dietary ingredient with health benefits.
studies are needed to validate and extend our findings. |
doi_str_mv | 10.5851/kosfa.2024.e45 |
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gastrointestinal digestion predicted structural changes in these peptides. While IWAGK, VDLL, MPLVR, LPQL, TVIL, and DFPGLQ could be fragmented into bioactive dipeptides and tripeptides, MTTPNK, KIII, and VEDVK exhibited resistance, suggesting potential circulation through the bloodstream to reach the target organ. Consequently, our study explores the potential use of BB-N as a novel dietary ingredient with health benefits.
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gastrointestinal digestion predicted structural changes in these peptides. While IWAGK, VDLL, MPLVR, LPQL, TVIL, and DFPGLQ could be fragmented into bioactive dipeptides and tripeptides, MTTPNK, KIII, and VEDVK exhibited resistance, suggesting potential circulation through the bloodstream to reach the target organ. Consequently, our study explores the potential use of BB-N as a novel dietary ingredient with health benefits.
studies are needed to validate and extend our findings.</description><subject>축산학</subject><issn>2636-0772</issn><issn>2636-0780</issn><issn>2636-0780</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><recordid>eNpVUk1vEzEQtRCIVmmvHJGPCJHUn_vBBaWhlEiVqGh7try2NzXZ2KntrQr_hn-KNxui1peZ0bx5M-N5ALzDaMYrjs_WPrZyRhBhM8P4K3BMClpMUVmh1we_JEfgNMZfCCGCaV3j4i04ojXnrCLlMfh78bTtfLBuBdO9gXfJdvaPTNY76Ft47h-tM_C8815DGaGEN74Pygy5ucuoJ6ulS_DabJPV5jO8Dl73aij_BBfeKeNSkGO41DmwrVX7WDoNlw7e5IbKw0sZU_DWJROTdbKDX-1qcL07AW9a2UVzurcTcPft4nbxfXr143K5mF9NFSlxmrKmKstCS4KUpIo3WrdEci0VMbgpdIkRyR_TYIy1KinjtawpZ0wXplYNRYhOwMeR14VWrJUVXtqdXXmxDmL-83YpMCoYyS-Dv4zgbd9sjB737MQ22I0Mv3elLzPO3meiR4ExL1i-Q2b4sGcI_qHPq4qNjcp0nXTG91FQTOqiqnk-2gTMRqgKPsZg2kMfjMQgBLETghiEILIQcsH759Md4P_PTv8B8k2y8Q</recordid><startdate>20241101</startdate><enddate>20241101</enddate><creator>Boonkong, Saruttiwong</creator><creator>Luasiri, Pichitpon</creator><creator>Pongsetkul, Jaksuma</creator><creator>Suwanandgul, Saranya</creator><creator>Chaipayang, Sukanya</creator><creator>Molee, Wittawat</creator><creator>Sangsawad, Papungkorn</creator><general>Korean Society for Food Science of Animal Resources</general><general>한국축산식품학회</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><scope>ACYCR</scope><orcidid>https://orcid.org/0009-0007-2332-324X</orcidid><orcidid>https://orcid.org/0000-0002-0880-7031</orcidid><orcidid>https://orcid.org/0000-0003-2420-8634</orcidid><orcidid>https://orcid.org/0009-0005-0256-2773</orcidid><orcidid>https://orcid.org/0009-0004-2079-7034</orcidid><orcidid>https://orcid.org/0000-0003-2346-2980</orcidid><orcidid>https://orcid.org/0000-0003-4096-3285</orcidid></search><sort><creationdate>20241101</creationdate><title>Exploring the Utilization of Bovine Blood as a Source of Antioxidant Peptide: Production, Concentration, Identification, and In Silico Gastrointestinal Digestion</title><author>Boonkong, Saruttiwong ; Luasiri, Pichitpon ; Pongsetkul, Jaksuma ; Suwanandgul, Saranya ; Chaipayang, Sukanya ; Molee, Wittawat ; Sangsawad, Papungkorn</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c271t-4b8776da20ca3c5bddf2a5dac2e1b6d7102078b111dc73459a93544d6e9cb3003</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>축산학</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Boonkong, Saruttiwong</creatorcontrib><creatorcontrib>Luasiri, Pichitpon</creatorcontrib><creatorcontrib>Pongsetkul, Jaksuma</creatorcontrib><creatorcontrib>Suwanandgul, Saranya</creatorcontrib><creatorcontrib>Chaipayang, Sukanya</creatorcontrib><creatorcontrib>Molee, Wittawat</creatorcontrib><creatorcontrib>Sangsawad, Papungkorn</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Korean Citation Index</collection><jtitle>Food science of animal resources</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Boonkong, Saruttiwong</au><au>Luasiri, Pichitpon</au><au>Pongsetkul, Jaksuma</au><au>Suwanandgul, Saranya</au><au>Chaipayang, Sukanya</au><au>Molee, Wittawat</au><au>Sangsawad, Papungkorn</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Exploring the Utilization of Bovine Blood as a Source of Antioxidant Peptide: Production, Concentration, Identification, and In Silico Gastrointestinal Digestion</atitle><jtitle>Food science of animal resources</jtitle><addtitle>Food Sci Anim Resour</addtitle><date>2024-11-01</date><risdate>2024</risdate><volume>44</volume><issue>6</issue><spage>1283</spage><epage>1304</epage><pages>1283-1304</pages><issn>2636-0772</issn><issn>2636-0780</issn><eissn>2636-0780</eissn><abstract>This study delves into the pivotal industrial process of efficiently managing livestock waste. Specifically, the study concentrates on harnessing the potential of bovine blood through enzymatic hydrolysis to produce antioxidant peptides. The whole bovine blood sample, subjected to a 90°C heat treatment for 30 min, underwent hydrolysis utilizing various commercial enzymes, alcalase, neutrase, and papain. Through neutrase hydrolysis (BB-N), we identified optimized conditions crucial for achieving heightened antioxidant activities and 40% protein recovery. Ultrafiltration with a molecular weight cutoff of 3 kDa was employed to concentrate the BB-N peptide, demonstrating the highest antioxidant and protein yield. The gel electrophoresis profile confirmed the denaturation of key proteins like albumin, globulin, and fibrinogen before digestion, while the BB-N derived after digestion contained peptides below 16 kDa. Post-concentration, the permeation of UF-3 kDa underwent purification, and the peptide sequence was discerned using liquid chromatography with tandem mass spectrometry. The exploration identified nine novel peptides- IWAGK, VDLL, MTTPNK, MPLVR, KIII, LPQL, TVIL, DFPGLQ, and VEDVK. Notably, the IWAGK sequence emerged as the most potent antioxidant activity peptide. Subsequent
gastrointestinal digestion predicted structural changes in these peptides. While IWAGK, VDLL, MPLVR, LPQL, TVIL, and DFPGLQ could be fragmented into bioactive dipeptides and tripeptides, MTTPNK, KIII, and VEDVK exhibited resistance, suggesting potential circulation through the bloodstream to reach the target organ. Consequently, our study explores the potential use of BB-N as a novel dietary ingredient with health benefits.
studies are needed to validate and extend our findings.</abstract><cop>Korea (South)</cop><pub>Korean Society for Food Science of Animal Resources</pub><pmid>39554827</pmid><doi>10.5851/kosfa.2024.e45</doi><tpages>22</tpages><orcidid>https://orcid.org/0009-0007-2332-324X</orcidid><orcidid>https://orcid.org/0000-0002-0880-7031</orcidid><orcidid>https://orcid.org/0000-0003-2420-8634</orcidid><orcidid>https://orcid.org/0009-0005-0256-2773</orcidid><orcidid>https://orcid.org/0009-0004-2079-7034</orcidid><orcidid>https://orcid.org/0000-0003-2346-2980</orcidid><orcidid>https://orcid.org/0000-0003-4096-3285</orcidid><oa>free_for_read</oa></addata></record> |
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title | Exploring the Utilization of Bovine Blood as a Source of Antioxidant Peptide: Production, Concentration, Identification, and In Silico Gastrointestinal Digestion |
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