Preparation and antioxidant properties of crayfish (Procambarus clarkii) By-products protein hydrolysates and ultra filtration fractions
Protein isolate from crayfish by-products (CBPI) were hydrolyzed using Alcalase, neutrase, pancreatin and bromelain. Hydrolysis by Alcalase had more remarkable digesting efficiency on crayfish by-products protein than that by the other enzymes. Therefore, protein hydrolysate from Alcalase digestion...
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| Veröffentlicht in: | Pakistan journal of pharmaceutical sciences 2019-09, Vol.32 (5(Special)), p.2391-2397 |
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| container_title | Pakistan journal of pharmaceutical sciences |
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| creator | Tang, Zhihong Yu, Liang Wen, Shaohong Zhang, Kaiqi Sun, Yongrong Lv, Jiasen BaoJu, - Hu, Zhongliang |
| description | Protein isolate from crayfish by-products (CBPI) were hydrolyzed using Alcalase, neutrase, pancreatin and bromelain. Hydrolysis by Alcalase had more remarkable digesting efficiency on crayfish by-products protein than that by the other enzymes. Therefore, protein hydrolysate from Alcalase digestion (CBPHa) was selected to be fractionated by ultrafiltration according to molecular weight into three fractions F1 (MW |
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Hydrolysis by Alcalase had more remarkable digesting efficiency on crayfish by-products protein than that by the other enzymes. Therefore, protein hydrolysate from Alcalase digestion (CBPHa) was selected to be fractionated by ultrafiltration according to molecular weight into three fractions F1 (MW <1kDa), F2 (MW 1-3kDa) and F3 (MW 3-10kDa). The amino acid determination revealed that CBPI had essential amino acid (EAA) close to that required for human protein synthesis. In vitro activity experiments showed that CBPHa and its fractions possessed considerable antioxidant activity. F1 exhibited the highest DPPH, superoxide radicals scavenging activities and Fe2+ chelating ability, whereas F2 showed the best hydroxyl radicals scavenging capacity and reducing power. In addition, all the fractions showed higher super oxide radical scavenging activity than the crude hydrolysates. Our findings suggest that CBPHa and their ultra filtration fractions have the potential for use in nutraceutical and functional food industries to maximize the use of crayfish processing by-products.</description><identifier>ISSN: 1011-601X</identifier><identifier>PMID: 31894023</identifier><language>eng</language><publisher>Pakistan: Pakistan Journal of Pharmaceutical Sciences</publisher><subject>Amino acids ; Antioxidants (Nutrients) ; Backup software ; Biological products ; EDTA ; Enzymes ; Fishes ; Hydrolysis ; Protein hydrolysates ; Protein synthesis</subject><ispartof>Pakistan journal of pharmaceutical sciences, 2019-09, Vol.32 (5(Special)), p.2391-2397</ispartof><rights>COPYRIGHT 2019 Pakistan Journal of Pharmaceutical Sciences</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31894023$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tang, Zhihong</creatorcontrib><creatorcontrib>Yu, Liang</creatorcontrib><creatorcontrib>Wen, Shaohong</creatorcontrib><creatorcontrib>Zhang, Kaiqi</creatorcontrib><creatorcontrib>Sun, Yongrong</creatorcontrib><creatorcontrib>Lv, Jiasen</creatorcontrib><creatorcontrib>BaoJu, -</creatorcontrib><creatorcontrib>Hu, Zhongliang</creatorcontrib><title>Preparation and antioxidant properties of crayfish (Procambarus clarkii) By-products protein hydrolysates and ultra filtration fractions</title><title>Pakistan journal of pharmaceutical sciences</title><addtitle>Pak J Pharm Sci</addtitle><description>Protein isolate from crayfish by-products (CBPI) were hydrolyzed using Alcalase, neutrase, pancreatin and bromelain. Hydrolysis by Alcalase had more remarkable digesting efficiency on crayfish by-products protein than that by the other enzymes. Therefore, protein hydrolysate from Alcalase digestion (CBPHa) was selected to be fractionated by ultrafiltration according to molecular weight into three fractions F1 (MW <1kDa), F2 (MW 1-3kDa) and F3 (MW 3-10kDa). The amino acid determination revealed that CBPI had essential amino acid (EAA) close to that required for human protein synthesis. In vitro activity experiments showed that CBPHa and its fractions possessed considerable antioxidant activity. F1 exhibited the highest DPPH, superoxide radicals scavenging activities and Fe2+ chelating ability, whereas F2 showed the best hydroxyl radicals scavenging capacity and reducing power. In addition, all the fractions showed higher super oxide radical scavenging activity than the crude hydrolysates. Our findings suggest that CBPHa and their ultra filtration fractions have the potential for use in nutraceutical and functional food industries to maximize the use of crayfish processing by-products.</description><subject>Amino acids</subject><subject>Antioxidants (Nutrients)</subject><subject>Backup software</subject><subject>Biological products</subject><subject>EDTA</subject><subject>Enzymes</subject><subject>Fishes</subject><subject>Hydrolysis</subject><subject>Protein hydrolysates</subject><subject>Protein synthesis</subject><issn>1011-601X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNo1UMtOwzAQzAFES-EXkI_lEORHXj6WipdUiR5A4hZt7HVryAs7kcgf8Nm4ULRazRxmZ2f3JJozylicUfY2i869f6c0S6SUZ9FMsEImlIt59L112IODwXYtgVaHDvTL6oCkd12PbrDoSWeIcjAZ6_dkuXWdgqYCN3qianAf1l6T2ykOej2qwR8GB7Qt2U_adfXkYQgWB_exHhwQYw_wu9I4UAfiL6JTA7XHyyMuotf7u5f1Y7x5fnharzbxjqd0iFEnPDc8ZaygNBUMVYVSKl1JKnIwRiUFJFqmxjDBoaBM5wmmlFbUVEh1IRbR8s83ZPwc0Q9lY73CuoYWu9GXXAhOCy5yGaQ3f9Id1Fja1nQhtQqlsbGqazHcgeUqo0XGEpmmYeDq6D1WDeqyd7YBN5X_7xY_MJh-jg</recordid><startdate>20190901</startdate><enddate>20190901</enddate><creator>Tang, Zhihong</creator><creator>Yu, Liang</creator><creator>Wen, Shaohong</creator><creator>Zhang, Kaiqi</creator><creator>Sun, Yongrong</creator><creator>Lv, Jiasen</creator><creator>BaoJu, -</creator><creator>Hu, Zhongliang</creator><general>Pakistan Journal of Pharmaceutical Sciences</general><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20190901</creationdate><title>Preparation and antioxidant properties of crayfish (Procambarus clarkii) By-products protein hydrolysates and ultra filtration fractions</title><author>Tang, Zhihong ; Yu, Liang ; Wen, Shaohong ; Zhang, Kaiqi ; Sun, Yongrong ; Lv, Jiasen ; BaoJu, - ; Hu, Zhongliang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-g250t-ed427f2511800531ecbe99cdb9037affc48a4d95ff132a801d74e500b0fbe0d83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Amino acids</topic><topic>Antioxidants (Nutrients)</topic><topic>Backup software</topic><topic>Biological products</topic><topic>EDTA</topic><topic>Enzymes</topic><topic>Fishes</topic><topic>Hydrolysis</topic><topic>Protein hydrolysates</topic><topic>Protein synthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tang, Zhihong</creatorcontrib><creatorcontrib>Yu, Liang</creatorcontrib><creatorcontrib>Wen, Shaohong</creatorcontrib><creatorcontrib>Zhang, Kaiqi</creatorcontrib><creatorcontrib>Sun, Yongrong</creatorcontrib><creatorcontrib>Lv, Jiasen</creatorcontrib><creatorcontrib>BaoJu, -</creatorcontrib><creatorcontrib>Hu, Zhongliang</creatorcontrib><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Pakistan journal of pharmaceutical sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tang, Zhihong</au><au>Yu, Liang</au><au>Wen, Shaohong</au><au>Zhang, Kaiqi</au><au>Sun, Yongrong</au><au>Lv, Jiasen</au><au>BaoJu, -</au><au>Hu, Zhongliang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preparation and antioxidant properties of crayfish (Procambarus clarkii) By-products protein hydrolysates and ultra filtration fractions</atitle><jtitle>Pakistan journal of pharmaceutical sciences</jtitle><addtitle>Pak J Pharm Sci</addtitle><date>2019-09-01</date><risdate>2019</risdate><volume>32</volume><issue>5(Special)</issue><spage>2391</spage><epage>2397</epage><pages>2391-2397</pages><issn>1011-601X</issn><abstract>Protein isolate from crayfish by-products (CBPI) were hydrolyzed using Alcalase, neutrase, pancreatin and bromelain. Hydrolysis by Alcalase had more remarkable digesting efficiency on crayfish by-products protein than that by the other enzymes. Therefore, protein hydrolysate from Alcalase digestion (CBPHa) was selected to be fractionated by ultrafiltration according to molecular weight into three fractions F1 (MW <1kDa), F2 (MW 1-3kDa) and F3 (MW 3-10kDa). The amino acid determination revealed that CBPI had essential amino acid (EAA) close to that required for human protein synthesis. In vitro activity experiments showed that CBPHa and its fractions possessed considerable antioxidant activity. F1 exhibited the highest DPPH, superoxide radicals scavenging activities and Fe2+ chelating ability, whereas F2 showed the best hydroxyl radicals scavenging capacity and reducing power. In addition, all the fractions showed higher super oxide radical scavenging activity than the crude hydrolysates. Our findings suggest that CBPHa and their ultra filtration fractions have the potential for use in nutraceutical and functional food industries to maximize the use of crayfish processing by-products.</abstract><cop>Pakistan</cop><pub>Pakistan Journal of Pharmaceutical Sciences</pub><pmid>31894023</pmid><tpages>7</tpages></addata></record> |
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| subjects | Amino acids Antioxidants (Nutrients) Backup software Biological products EDTA Enzymes Fishes Hydrolysis Protein hydrolysates Protein synthesis |
| title | Preparation and antioxidant properties of crayfish (Procambarus clarkii) By-products protein hydrolysates and ultra filtration fractions |
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