Influence of Transglutaminase (TGase) Enzyme on Mechanical and Bioactive Properties of Crayfish Protein Gels
Functional and bioactive properties of crayfish meat convert their surpluses in an excellent alternative for the development of food products. Thus, protein dispersions were subjected to a thermal treatment, obtaining a protein-based gel. Rheological and antioxidant properties were studied at three...
Gespeichert in:
Veröffentlicht in: | Food biophysics 2017-09, Vol.12 (3), p.348-355 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 355 |
---|---|
container_issue | 3 |
container_start_page | 348 |
container_title | Food biophysics |
container_volume | 12 |
creator | Felix, M. Romero, A. Rustad, T. Guerrero, A. |
description | Functional and bioactive properties of crayfish meat convert their surpluses in an excellent alternative for the development of food products. Thus, protein dispersions were subjected to a thermal treatment, obtaining a protein-based gel. Rheological and antioxidant properties were studied at three different pH values (2.0, 6.5 and 8.0) when the TGase enzyme was used. The pH value exerted a strong influence on the gelation behaviour, as well as on the functional properties and the antioxidant activity of the final gels. The activity of the TGase enzyme is highly influenced by the pH of the protein dispersions. The highest antioxidant activity was obtained against ABTS and the lowest when FC reagent was used, whereas the activity against DPPH was also remarkable. TGase enzyme can be used during the thermal treatment to increase the mechanical properties, which were lost when hydrolysate systems were used. |
doi_str_mv | 10.1007/s11483-017-9490-7 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_1926998909</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1926998909</sourcerecordid><originalsourceid>FETCH-LOGICAL-c316t-d7913b0a56e53ffc7dc406cacf135687a1131f939286b482ffd0368243b553aa3</originalsourceid><addsrcrecordid>eNp1kM1KAzEURoMoWKsP4C7gRhejyeR_qaXWgqKLug5pmrQp00xNZoT69M4wIm5c3cvlfN-FA8AlRrcYIXGXMaaSFAiLQlGFCnEERpgxUWDJ-fHvzuQpOMt5ixCllKMRqObRV62L1sHaw0UyMa-rtjG7EE128Hox68YNnMavw65DInxxdmNisKaCJq7gQ6iNbcKng2-p3rvUBJf7pkkyBx_ypj83LkQ4c1U-ByfeVNld_MwxeH-cLiZPxfPrbD65fy4swbwpVkJhskSGcceI91asLEXcGusxYVwKgzHBXhFVSr6ksvR-hQiXJSVLxogxZAyuht59qj9alxu9rdsUu5caq5IrJRVSHYUHyqY65-S83qewM-mgMdK9VD1I1Z1U3UvVosuUQyZ3bFy79Kf539A3KpN5zw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1926998909</pqid></control><display><type>article</type><title>Influence of Transglutaminase (TGase) Enzyme on Mechanical and Bioactive Properties of Crayfish Protein Gels</title><source>Springer Nature - Complete Springer Journals</source><creator>Felix, M. ; Romero, A. ; Rustad, T. ; Guerrero, A.</creator><creatorcontrib>Felix, M. ; Romero, A. ; Rustad, T. ; Guerrero, A.</creatorcontrib><description>Functional and bioactive properties of crayfish meat convert their surpluses in an excellent alternative for the development of food products. Thus, protein dispersions were subjected to a thermal treatment, obtaining a protein-based gel. Rheological and antioxidant properties were studied at three different pH values (2.0, 6.5 and 8.0) when the TGase enzyme was used. The pH value exerted a strong influence on the gelation behaviour, as well as on the functional properties and the antioxidant activity of the final gels. The activity of the TGase enzyme is highly influenced by the pH of the protein dispersions. The highest antioxidant activity was obtained against ABTS and the lowest when FC reagent was used, whereas the activity against DPPH was also remarkable. TGase enzyme can be used during the thermal treatment to increase the mechanical properties, which were lost when hydrolysate systems were used.</description><identifier>ISSN: 1557-1858</identifier><identifier>EISSN: 1557-1866</identifier><identifier>DOI: 10.1007/s11483-017-9490-7</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Analytical Chemistry ; Antioxidants ; Biocompatibility ; Biological and Medical Physics ; Biophysics ; Chemistry ; Chemistry and Materials Science ; Crayfish ; Dispersions ; Enzymes ; Fish ; Food ; Food Science ; Gelation ; Gels ; Heat treatment ; Meat ; Mechanical properties ; Original Article ; pH effects ; Proteins ; Rheological properties</subject><ispartof>Food biophysics, 2017-09, Vol.12 (3), p.348-355</ispartof><rights>Springer Science+Business Media New York 2017</rights><rights>Food Biophysics is a copyright of Springer, 2017.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c316t-d7913b0a56e53ffc7dc406cacf135687a1131f939286b482ffd0368243b553aa3</citedby><cites>FETCH-LOGICAL-c316t-d7913b0a56e53ffc7dc406cacf135687a1131f939286b482ffd0368243b553aa3</cites><orcidid>0000-0002-3608-7035</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11483-017-9490-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11483-017-9490-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids></links><search><creatorcontrib>Felix, M.</creatorcontrib><creatorcontrib>Romero, A.</creatorcontrib><creatorcontrib>Rustad, T.</creatorcontrib><creatorcontrib>Guerrero, A.</creatorcontrib><title>Influence of Transglutaminase (TGase) Enzyme on Mechanical and Bioactive Properties of Crayfish Protein Gels</title><title>Food biophysics</title><addtitle>Food Biophysics</addtitle><description>Functional and bioactive properties of crayfish meat convert their surpluses in an excellent alternative for the development of food products. Thus, protein dispersions were subjected to a thermal treatment, obtaining a protein-based gel. Rheological and antioxidant properties were studied at three different pH values (2.0, 6.5 and 8.0) when the TGase enzyme was used. The pH value exerted a strong influence on the gelation behaviour, as well as on the functional properties and the antioxidant activity of the final gels. The activity of the TGase enzyme is highly influenced by the pH of the protein dispersions. The highest antioxidant activity was obtained against ABTS and the lowest when FC reagent was used, whereas the activity against DPPH was also remarkable. TGase enzyme can be used during the thermal treatment to increase the mechanical properties, which were lost when hydrolysate systems were used.</description><subject>Analytical Chemistry</subject><subject>Antioxidants</subject><subject>Biocompatibility</subject><subject>Biological and Medical Physics</subject><subject>Biophysics</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Crayfish</subject><subject>Dispersions</subject><subject>Enzymes</subject><subject>Fish</subject><subject>Food</subject><subject>Food Science</subject><subject>Gelation</subject><subject>Gels</subject><subject>Heat treatment</subject><subject>Meat</subject><subject>Mechanical properties</subject><subject>Original Article</subject><subject>pH effects</subject><subject>Proteins</subject><subject>Rheological properties</subject><issn>1557-1858</issn><issn>1557-1866</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kM1KAzEURoMoWKsP4C7gRhejyeR_qaXWgqKLug5pmrQp00xNZoT69M4wIm5c3cvlfN-FA8AlRrcYIXGXMaaSFAiLQlGFCnEERpgxUWDJ-fHvzuQpOMt5ixCllKMRqObRV62L1sHaw0UyMa-rtjG7EE128Hox68YNnMavw65DInxxdmNisKaCJq7gQ6iNbcKng2-p3rvUBJf7pkkyBx_ypj83LkQ4c1U-ByfeVNld_MwxeH-cLiZPxfPrbD65fy4swbwpVkJhskSGcceI91asLEXcGusxYVwKgzHBXhFVSr6ksvR-hQiXJSVLxogxZAyuht59qj9alxu9rdsUu5caq5IrJRVSHYUHyqY65-S83qewM-mgMdK9VD1I1Z1U3UvVosuUQyZ3bFy79Kf539A3KpN5zw</recordid><startdate>20170901</startdate><enddate>20170901</enddate><creator>Felix, M.</creator><creator>Romero, A.</creator><creator>Rustad, T.</creator><creator>Guerrero, A.</creator><general>Springer US</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7RQ</scope><scope>7T7</scope><scope>7X2</scope><scope>7XB</scope><scope>88A</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M0K</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><orcidid>https://orcid.org/0000-0002-3608-7035</orcidid></search><sort><creationdate>20170901</creationdate><title>Influence of Transglutaminase (TGase) Enzyme on Mechanical and Bioactive Properties of Crayfish Protein Gels</title><author>Felix, M. ; Romero, A. ; Rustad, T. ; Guerrero, A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c316t-d7913b0a56e53ffc7dc406cacf135687a1131f939286b482ffd0368243b553aa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Analytical Chemistry</topic><topic>Antioxidants</topic><topic>Biocompatibility</topic><topic>Biological and Medical Physics</topic><topic>Biophysics</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Crayfish</topic><topic>Dispersions</topic><topic>Enzymes</topic><topic>Fish</topic><topic>Food</topic><topic>Food Science</topic><topic>Gelation</topic><topic>Gels</topic><topic>Heat treatment</topic><topic>Meat</topic><topic>Mechanical properties</topic><topic>Original Article</topic><topic>pH effects</topic><topic>Proteins</topic><topic>Rheological properties</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Felix, M.</creatorcontrib><creatorcontrib>Romero, A.</creatorcontrib><creatorcontrib>Rustad, T.</creatorcontrib><creatorcontrib>Guerrero, A.</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Career & Technical Education Database</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Agricultural Science Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><jtitle>Food biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Felix, M.</au><au>Romero, A.</au><au>Rustad, T.</au><au>Guerrero, A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Influence of Transglutaminase (TGase) Enzyme on Mechanical and Bioactive Properties of Crayfish Protein Gels</atitle><jtitle>Food biophysics</jtitle><stitle>Food Biophysics</stitle><date>2017-09-01</date><risdate>2017</risdate><volume>12</volume><issue>3</issue><spage>348</spage><epage>355</epage><pages>348-355</pages><issn>1557-1858</issn><eissn>1557-1866</eissn><abstract>Functional and bioactive properties of crayfish meat convert their surpluses in an excellent alternative for the development of food products. Thus, protein dispersions were subjected to a thermal treatment, obtaining a protein-based gel. Rheological and antioxidant properties were studied at three different pH values (2.0, 6.5 and 8.0) when the TGase enzyme was used. The pH value exerted a strong influence on the gelation behaviour, as well as on the functional properties and the antioxidant activity of the final gels. The activity of the TGase enzyme is highly influenced by the pH of the protein dispersions. The highest antioxidant activity was obtained against ABTS and the lowest when FC reagent was used, whereas the activity against DPPH was also remarkable. TGase enzyme can be used during the thermal treatment to increase the mechanical properties, which were lost when hydrolysate systems were used.</abstract><cop>New York</cop><pub>Springer US</pub><doi>10.1007/s11483-017-9490-7</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-3608-7035</orcidid></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1557-1858 |
ispartof | Food biophysics, 2017-09, Vol.12 (3), p.348-355 |
issn | 1557-1858 1557-1866 |
language | eng |
recordid | cdi_proquest_journals_1926998909 |
source | Springer Nature - Complete Springer Journals |
subjects | Analytical Chemistry Antioxidants Biocompatibility Biological and Medical Physics Biophysics Chemistry Chemistry and Materials Science Crayfish Dispersions Enzymes Fish Food Food Science Gelation Gels Heat treatment Meat Mechanical properties Original Article pH effects Proteins Rheological properties |
title | Influence of Transglutaminase (TGase) Enzyme on Mechanical and Bioactive Properties of Crayfish Protein Gels |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-20T17%3A08%3A50IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Influence%20of%20Transglutaminase%20(TGase)%20Enzyme%20on%20Mechanical%20and%20Bioactive%20Properties%20of%20Crayfish%20Protein%20Gels&rft.jtitle=Food%20biophysics&rft.au=Felix,%20M.&rft.date=2017-09-01&rft.volume=12&rft.issue=3&rft.spage=348&rft.epage=355&rft.pages=348-355&rft.issn=1557-1858&rft.eissn=1557-1866&rft_id=info:doi/10.1007/s11483-017-9490-7&rft_dat=%3Cproquest_cross%3E1926998909%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1926998909&rft_id=info:pmid/&rfr_iscdi=true |