Antioxidant activity of protein hydrolysates derived from threadfin bream surimi byproducts
► Threadfin bream surimi byproducts are a potential source for production of protein hydrolysate. ► Pepsin-hydrolysed FBS showed the highest antioxidant activity based on free radical assays. ► FBS and RD hydrolysates protected HepG2 cells against oxidative damage. ► Virgibacillus sp. SK33 proteinas...
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| Veröffentlicht in: | Food chemistry 2012-05, Vol.132 (1), p.104-111 |
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| creator | Wiriyaphan, Chompoonuch Chitsomboon, Benjamart Yongsawadigul, Jirawat |
| description | ► Threadfin bream surimi byproducts are a potential source for production of protein hydrolysate. ► Pepsin-hydrolysed FBS showed the highest antioxidant activity based on free radical assays. ► FBS and RD hydrolysates protected HepG2 cells against oxidative damage. ► Virgibacillus sp. SK33 proteinase is a promising processing-aid for functional protein hydrolysate production.
Antioxidant activities of protein hydrolysates from threadfin bream surimi wastes, including frame, bone and skin (FBS) and refiner discharge (RD), were investigated. FBS and RD were rich in Lys, Glu, Gly, Pro, Asp, Leu, His, Tyr and Phe. FBS was hydrolysed to a greater extent than RD regardless of proteinases tested (Virgibacillus sp. SK33 proteinase, Alcalase, pepsin and trypsin). Pepsin-hydrolysed FBS, at a 5% degree of hydrolysis (DH), showed the highest antioxidant activity based on 2,2′-azinobis (3-ethyl-benzothiazoline-6-sulphonate) (ABTS) radical (0.455±0.054mg Trolox equivalents/mg leucine equivalents), ferric reducing antioxidant power (FRAP) (0.221±0.005mM Trolox equivalents) and inhibition of β-carotene bleaching assays. FBS hydrolysates showed higher antioxidant activity based on chemical assays than their RD counterparts. However, FBS and RD hydrolysates protected HepG2 cells against tert-butyl hydroperoxide-induced oxidative damage to a similar extent. Therefore, FBS and RD hydrolysates have a potential as antioxidative neutraceutical ingredients. |
| doi_str_mv | 10.1016/j.foodchem.2011.10.040 |
| format | Article |
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Antioxidant activities of protein hydrolysates from threadfin bream surimi wastes, including frame, bone and skin (FBS) and refiner discharge (RD), were investigated. FBS and RD were rich in Lys, Glu, Gly, Pro, Asp, Leu, His, Tyr and Phe. FBS was hydrolysed to a greater extent than RD regardless of proteinases tested (Virgibacillus sp. SK33 proteinase, Alcalase, pepsin and trypsin). Pepsin-hydrolysed FBS, at a 5% degree of hydrolysis (DH), showed the highest antioxidant activity based on 2,2′-azinobis (3-ethyl-benzothiazoline-6-sulphonate) (ABTS) radical (0.455±0.054mg Trolox equivalents/mg leucine equivalents), ferric reducing antioxidant power (FRAP) (0.221±0.005mM Trolox equivalents) and inhibition of β-carotene bleaching assays. FBS hydrolysates showed higher antioxidant activity based on chemical assays than their RD counterparts. However, FBS and RD hydrolysates protected HepG2 cells against tert-butyl hydroperoxide-induced oxidative damage to a similar extent. Therefore, FBS and RD hydrolysates have a potential as antioxidative neutraceutical ingredients.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2011.10.040</identifier><identifier>PMID: 26434269</identifier><identifier>CODEN: FOCHDJ</identifier><language>eng</language><publisher>Kidlington: Elsevier Ltd</publisher><subject>Animals ; Antioxidant activity ; Antioxidants ; Biological and medical sciences ; bones ; bream ; byproducts ; Fishes - metabolism ; Food industries ; Fundamental and applied biological sciences. Psychology ; General aspects ; Hep G2 Cells ; HepG2 cell line ; Humans ; hydrolysates ; hydrolysis ; ingredients ; leucine ; Oxidation-Reduction ; pepsin ; Pollution and sludges ; Protein hydrolysates ; Protein Hydrolysates - chemistry ; Protein Hydrolysates - pharmacology ; Seafood - analysis ; subtilisin ; surimi ; Surimi wastes ; trypsin ; Trypsin - metabolism ; Virgibacillus ; wastes</subject><ispartof>Food chemistry, 2012-05, Vol.132 (1), p.104-111</ispartof><rights>2011 Elsevier Ltd</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2011 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c455t-77fb4d2c84893f39ca39fa21b1817bd67e0fd64788c75670f6281316bccde1113</citedby><cites>FETCH-LOGICAL-c455t-77fb4d2c84893f39ca39fa21b1817bd67e0fd64788c75670f6281316bccde1113</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.foodchem.2011.10.040$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25929054$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26434269$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wiriyaphan, Chompoonuch</creatorcontrib><creatorcontrib>Chitsomboon, Benjamart</creatorcontrib><creatorcontrib>Yongsawadigul, Jirawat</creatorcontrib><title>Antioxidant activity of protein hydrolysates derived from threadfin bream surimi byproducts</title><title>Food chemistry</title><addtitle>Food Chem</addtitle><description>► Threadfin bream surimi byproducts are a potential source for production of protein hydrolysate. ► Pepsin-hydrolysed FBS showed the highest antioxidant activity based on free radical assays. ► FBS and RD hydrolysates protected HepG2 cells against oxidative damage. ► Virgibacillus sp. SK33 proteinase is a promising processing-aid for functional protein hydrolysate production.
Antioxidant activities of protein hydrolysates from threadfin bream surimi wastes, including frame, bone and skin (FBS) and refiner discharge (RD), were investigated. FBS and RD were rich in Lys, Glu, Gly, Pro, Asp, Leu, His, Tyr and Phe. FBS was hydrolysed to a greater extent than RD regardless of proteinases tested (Virgibacillus sp. SK33 proteinase, Alcalase, pepsin and trypsin). Pepsin-hydrolysed FBS, at a 5% degree of hydrolysis (DH), showed the highest antioxidant activity based on 2,2′-azinobis (3-ethyl-benzothiazoline-6-sulphonate) (ABTS) radical (0.455±0.054mg Trolox equivalents/mg leucine equivalents), ferric reducing antioxidant power (FRAP) (0.221±0.005mM Trolox equivalents) and inhibition of β-carotene bleaching assays. FBS hydrolysates showed higher antioxidant activity based on chemical assays than their RD counterparts. However, FBS and RD hydrolysates protected HepG2 cells against tert-butyl hydroperoxide-induced oxidative damage to a similar extent. Therefore, FBS and RD hydrolysates have a potential as antioxidative neutraceutical ingredients.</description><subject>Animals</subject><subject>Antioxidant activity</subject><subject>Antioxidants</subject><subject>Biological and medical sciences</subject><subject>bones</subject><subject>bream</subject><subject>byproducts</subject><subject>Fishes - metabolism</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects</subject><subject>Hep G2 Cells</subject><subject>HepG2 cell line</subject><subject>Humans</subject><subject>hydrolysates</subject><subject>hydrolysis</subject><subject>ingredients</subject><subject>leucine</subject><subject>Oxidation-Reduction</subject><subject>pepsin</subject><subject>Pollution and sludges</subject><subject>Protein hydrolysates</subject><subject>Protein Hydrolysates - chemistry</subject><subject>Protein Hydrolysates - pharmacology</subject><subject>Seafood - analysis</subject><subject>subtilisin</subject><subject>surimi</subject><subject>Surimi wastes</subject><subject>trypsin</subject><subject>Trypsin - metabolism</subject><subject>Virgibacillus</subject><subject>wastes</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqN0UuPFCEQAGBiNO64-hfWvph46REamsfNzWZ9JJt40D15IDQUDpPuZgV6Yv97mcysHvUEqXxFUVUIXRG8JZjwd_utj9HZHUzbDhNSg1vM8BO0IVLQVmDRPUUbTLFsJWH8Ar3IeY8xrlY-RxcdZ5R1XG3Q9-u5hPgrODOXxtgSDqGsTfTNQ4oFwtzsVpfiuGZTIDcOUjiAa3yKU1N2CYzz1Qz1MjV5SWEKzbDWVLfYkl-iZ96MGV6dz0t0_-H2282n9u7Lx88313etZX1fWiH8wFxnJZOKeqqsocqbjgxEEjE4LgB7x5mQ0oqeC-x5JwklfLDWASGEXqK3p3dr4Z8L5KKnkC2Mo5khLlkTQRQjSsj_oFwxxbnoaKX8RG2KOSfw-qH2Z9KqCdbHHei9ftyBPu7gGK87qIlX5xrLMIH7k_Y49ArenIHJ1ow-mdmG_Nf1qlO4Z9W9PjlvojY_UjX3X2slhnFtiTJexfuTgDreQ4Cksw0wW3AhgS3axfCv3_4GgJKyIw</recordid><startdate>20120501</startdate><enddate>20120501</enddate><creator>Wiriyaphan, Chompoonuch</creator><creator>Chitsomboon, Benjamart</creator><creator>Yongsawadigul, Jirawat</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TN</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>20120501</creationdate><title>Antioxidant activity of protein hydrolysates derived from threadfin bream surimi byproducts</title><author>Wiriyaphan, Chompoonuch ; Chitsomboon, Benjamart ; Yongsawadigul, Jirawat</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c455t-77fb4d2c84893f39ca39fa21b1817bd67e0fd64788c75670f6281316bccde1113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Animals</topic><topic>Antioxidant activity</topic><topic>Antioxidants</topic><topic>Biological and medical sciences</topic><topic>bones</topic><topic>bream</topic><topic>byproducts</topic><topic>Fishes - metabolism</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects</topic><topic>Hep G2 Cells</topic><topic>HepG2 cell line</topic><topic>Humans</topic><topic>hydrolysates</topic><topic>hydrolysis</topic><topic>ingredients</topic><topic>leucine</topic><topic>Oxidation-Reduction</topic><topic>pepsin</topic><topic>Pollution and sludges</topic><topic>Protein hydrolysates</topic><topic>Protein Hydrolysates - chemistry</topic><topic>Protein Hydrolysates - pharmacology</topic><topic>Seafood - analysis</topic><topic>subtilisin</topic><topic>surimi</topic><topic>Surimi wastes</topic><topic>trypsin</topic><topic>Trypsin - metabolism</topic><topic>Virgibacillus</topic><topic>wastes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wiriyaphan, Chompoonuch</creatorcontrib><creatorcontrib>Chitsomboon, Benjamart</creatorcontrib><creatorcontrib>Yongsawadigul, Jirawat</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Oceanic Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wiriyaphan, Chompoonuch</au><au>Chitsomboon, Benjamart</au><au>Yongsawadigul, Jirawat</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antioxidant activity of protein hydrolysates derived from threadfin bream surimi byproducts</atitle><jtitle>Food chemistry</jtitle><addtitle>Food Chem</addtitle><date>2012-05-01</date><risdate>2012</risdate><volume>132</volume><issue>1</issue><spage>104</spage><epage>111</epage><pages>104-111</pages><issn>0308-8146</issn><eissn>1873-7072</eissn><coden>FOCHDJ</coden><abstract>► Threadfin bream surimi byproducts are a potential source for production of protein hydrolysate. ► Pepsin-hydrolysed FBS showed the highest antioxidant activity based on free radical assays. ► FBS and RD hydrolysates protected HepG2 cells against oxidative damage. ► Virgibacillus sp. SK33 proteinase is a promising processing-aid for functional protein hydrolysate production.
Antioxidant activities of protein hydrolysates from threadfin bream surimi wastes, including frame, bone and skin (FBS) and refiner discharge (RD), were investigated. FBS and RD were rich in Lys, Glu, Gly, Pro, Asp, Leu, His, Tyr and Phe. FBS was hydrolysed to a greater extent than RD regardless of proteinases tested (Virgibacillus sp. SK33 proteinase, Alcalase, pepsin and trypsin). Pepsin-hydrolysed FBS, at a 5% degree of hydrolysis (DH), showed the highest antioxidant activity based on 2,2′-azinobis (3-ethyl-benzothiazoline-6-sulphonate) (ABTS) radical (0.455±0.054mg Trolox equivalents/mg leucine equivalents), ferric reducing antioxidant power (FRAP) (0.221±0.005mM Trolox equivalents) and inhibition of β-carotene bleaching assays. FBS hydrolysates showed higher antioxidant activity based on chemical assays than their RD counterparts. However, FBS and RD hydrolysates protected HepG2 cells against tert-butyl hydroperoxide-induced oxidative damage to a similar extent. Therefore, FBS and RD hydrolysates have a potential as antioxidative neutraceutical ingredients.</abstract><cop>Kidlington</cop><pub>Elsevier Ltd</pub><pmid>26434269</pmid><doi>10.1016/j.foodchem.2011.10.040</doi><tpages>8</tpages></addata></record> |
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| identifier | ISSN: 0308-8146 |
| ispartof | Food chemistry, 2012-05, Vol.132 (1), p.104-111 |
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| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Animals Antioxidant activity Antioxidants Biological and medical sciences bones bream byproducts Fishes - metabolism Food industries Fundamental and applied biological sciences. Psychology General aspects Hep G2 Cells HepG2 cell line Humans hydrolysates hydrolysis ingredients leucine Oxidation-Reduction pepsin Pollution and sludges Protein hydrolysates Protein Hydrolysates - chemistry Protein Hydrolysates - pharmacology Seafood - analysis subtilisin surimi Surimi wastes trypsin Trypsin - metabolism Virgibacillus wastes |
| title | Antioxidant activity of protein hydrolysates derived from threadfin bream surimi byproducts |
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