Chia (Salvia hispanica) protein fractions: characterization and emulsifying properties
A material with a high content of fibers and proteins is generated as a by-product of the chia oil extraction process. A strategy to add value to this by-product is to evaluate its possible use as a food ingredient. Thus, using a chia protein-rich fraction (CPRF) of chia seeds as starting material,...
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| Veröffentlicht in: | Journal of food measurement & characterization 2019-12, Vol.13 (4), p.3318-3328 |
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| creator | Julio, Luciana M. Ruiz-Ruiz, Jorge C. Tomás, Mabel C. Segura-Campos, Maira R. |
| description | A material with a high content of fibers and proteins is generated as a by-product of the chia oil extraction process. A strategy to add value to this by-product is to evaluate its possible use as a food ingredient. Thus, using a chia protein-rich fraction (CPRF) of chia seeds as starting material, albumins, globulins, glutelins, and prolamins fractions were obtained, characterized, and their emulsifying properties investigated. CPRF covers the essential amino acid requirements suggested by FAO; protein fractions only cover the requirements for Tre, Tyr and Val. Protein solubility profile for CPRF, globulins and prolamins was similar, with maximum solubility at pH 9. In contrast, glutelin and albumin fractions showed highest solubility at pH 5. Oil/Water (O/W) emulsions, using the chia protein fractions as emulsifying agent, were obtained at different pH (3, 5, 7, and 9) in their native and denatured state. The global stability and the destabilization kinetics of these systems were evaluated by their backscattering profiles. Additionally, the particle size distributions and their D
4.3
diameter were determined. The emulsions destabilization occurred mainly by creaming process, with globulins as the fraction that led to most stable systems. Besides, high pH values improved the stability of emulsions prepared with globulins, glutelins, and the protein-rich fraction. The heat treatment application only slightly improved the emulsifying activity of the CPRF. These results indicate that chia protein fractions could be used as food ingredient to improve the amino acid content and the techno-functional properties of the functional foods. |
| doi_str_mv | 10.1007/s11694-019-00254-w |
| format | Article |
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4.3
diameter were determined. The emulsions destabilization occurred mainly by creaming process, with globulins as the fraction that led to most stable systems. Besides, high pH values improved the stability of emulsions prepared with globulins, glutelins, and the protein-rich fraction. The heat treatment application only slightly improved the emulsifying activity of the CPRF. These results indicate that chia protein fractions could be used as food ingredient to improve the amino acid content and the techno-functional properties of the functional foods.</description><identifier>ISSN: 2193-4126</identifier><identifier>EISSN: 2193-4134</identifier><identifier>DOI: 10.1007/s11694-019-00254-w</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Acids ; Albumin ; Albumins ; Amino acids ; Backscattering ; Byproducts ; Chemistry ; Chemistry and Materials Science ; Chemistry/Food Science ; ChiA protein ; Destabilization ; Emulsifying agents ; Emulsions ; Engineering ; Fibers ; Food Science ; Functional foods & nutraceuticals ; Globulins ; Glutelin ; Heat treatment ; Kinetics ; Original Paper ; pH effects ; Prolamines ; Properties (attributes) ; Proteins ; Salvia columbariae ; Seeds ; Solubility ; Stability analysis ; Systems analysis</subject><ispartof>Journal of food measurement & characterization, 2019-12, Vol.13 (4), p.3318-3328</ispartof><rights>Springer Science+Business Media, LLC, part of Springer Nature 2019</rights><rights>Journal of Food Measurement and Characterization is a copyright of Springer, (2019). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c319t-7d8e312a7c0e41b1358443640a382377e4416f983638ed5430162a5b155ca2c3</citedby><cites>FETCH-LOGICAL-c319t-7d8e312a7c0e41b1358443640a382377e4416f983638ed5430162a5b155ca2c3</cites><orcidid>0000-0002-7664-6647</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/s11694-019-00254-w$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11694-019-00254-w$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids></links><search><creatorcontrib>Julio, Luciana M.</creatorcontrib><creatorcontrib>Ruiz-Ruiz, Jorge C.</creatorcontrib><creatorcontrib>Tomás, Mabel C.</creatorcontrib><creatorcontrib>Segura-Campos, Maira R.</creatorcontrib><title>Chia (Salvia hispanica) protein fractions: characterization and emulsifying properties</title><title>Journal of food measurement & characterization</title><addtitle>Food Measure</addtitle><description>A material with a high content of fibers and proteins is generated as a by-product of the chia oil extraction process. A strategy to add value to this by-product is to evaluate its possible use as a food ingredient. Thus, using a chia protein-rich fraction (CPRF) of chia seeds as starting material, albumins, globulins, glutelins, and prolamins fractions were obtained, characterized, and their emulsifying properties investigated. CPRF covers the essential amino acid requirements suggested by FAO; protein fractions only cover the requirements for Tre, Tyr and Val. Protein solubility profile for CPRF, globulins and prolamins was similar, with maximum solubility at pH 9. In contrast, glutelin and albumin fractions showed highest solubility at pH 5. Oil/Water (O/W) emulsions, using the chia protein fractions as emulsifying agent, were obtained at different pH (3, 5, 7, and 9) in their native and denatured state. The global stability and the destabilization kinetics of these systems were evaluated by their backscattering profiles. Additionally, the particle size distributions and their D
4.3
diameter were determined. The emulsions destabilization occurred mainly by creaming process, with globulins as the fraction that led to most stable systems. Besides, high pH values improved the stability of emulsions prepared with globulins, glutelins, and the protein-rich fraction. The heat treatment application only slightly improved the emulsifying activity of the CPRF. These results indicate that chia protein fractions could be used as food ingredient to improve the amino acid content and the techno-functional properties of the functional foods.</description><subject>Acids</subject><subject>Albumin</subject><subject>Albumins</subject><subject>Amino acids</subject><subject>Backscattering</subject><subject>Byproducts</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chemistry/Food Science</subject><subject>ChiA protein</subject><subject>Destabilization</subject><subject>Emulsifying agents</subject><subject>Emulsions</subject><subject>Engineering</subject><subject>Fibers</subject><subject>Food Science</subject><subject>Functional foods & nutraceuticals</subject><subject>Globulins</subject><subject>Glutelin</subject><subject>Heat treatment</subject><subject>Kinetics</subject><subject>Original Paper</subject><subject>pH effects</subject><subject>Prolamines</subject><subject>Properties (attributes)</subject><subject>Proteins</subject><subject>Salvia columbariae</subject><subject>Seeds</subject><subject>Solubility</subject><subject>Stability analysis</subject><subject>Systems analysis</subject><issn>2193-4126</issn><issn>2193-4134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><recordid>eNp9kE1LwzAYx4MoOOa-gKeCFz1U8yRPk9abDN9g4MHhNWRZumVsaU1ax_z0tlb05ul54f8CP0LOgV4DpfImAogCUwpFSinLMN0fkRGDgqcIHI9_dyZOySTGDaUUQCIKPiJv07XTyeWr3n50c-1irb0z-iqpQ9VY55MyaNO4ysfbxKx1f9jgPnX_SrRfJnbXbqMrD86vek9tQ-NsPCMnpd5GO_mZYzJ_uJ9Pn9LZy-Pz9G6WGg5Fk8plbjkwLQ21CAvgWY7IBVLNc8altIggyiLngud2mSGnIJjOFpBlRjPDx-RiiO2a31sbG7Wp2uC7RsVYLihiLotOxQaVCVWMwZaqDm6nw0EBVT1BNRBUHUH1TVDtOxMfTLET-5UNf9H_uL4AhpFzSQ</recordid><startdate>20191201</startdate><enddate>20191201</enddate><creator>Julio, Luciana M.</creator><creator>Ruiz-Ruiz, Jorge C.</creator><creator>Tomás, Mabel C.</creator><creator>Segura-Campos, Maira R.</creator><general>Springer US</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X2</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>HCIFZ</scope><scope>L6V</scope><scope>M0K</scope><scope>M7S</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><orcidid>https://orcid.org/0000-0002-7664-6647</orcidid></search><sort><creationdate>20191201</creationdate><title>Chia (Salvia hispanica) protein fractions: characterization and emulsifying properties</title><author>Julio, Luciana M. ; Ruiz-Ruiz, Jorge C. ; Tomás, Mabel C. ; Segura-Campos, Maira R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c319t-7d8e312a7c0e41b1358443640a382377e4416f983638ed5430162a5b155ca2c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Acids</topic><topic>Albumin</topic><topic>Albumins</topic><topic>Amino acids</topic><topic>Backscattering</topic><topic>Byproducts</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chemistry/Food Science</topic><topic>ChiA protein</topic><topic>Destabilization</topic><topic>Emulsifying agents</topic><topic>Emulsions</topic><topic>Engineering</topic><topic>Fibers</topic><topic>Food Science</topic><topic>Functional foods & nutraceuticals</topic><topic>Globulins</topic><topic>Glutelin</topic><topic>Heat treatment</topic><topic>Kinetics</topic><topic>Original Paper</topic><topic>pH effects</topic><topic>Prolamines</topic><topic>Properties (attributes)</topic><topic>Proteins</topic><topic>Salvia columbariae</topic><topic>Seeds</topic><topic>Solubility</topic><topic>Stability analysis</topic><topic>Systems analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Julio, Luciana M.</creatorcontrib><creatorcontrib>Ruiz-Ruiz, Jorge C.</creatorcontrib><creatorcontrib>Tomás, Mabel C.</creatorcontrib><creatorcontrib>Segura-Campos, Maira R.</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Agricultural Science Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</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>ProQuest Central</collection><collection>Technology Collection (ProQuest)</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Engineering Collection</collection><collection>Agricultural Science Database</collection><collection>Engineering Database</collection><collection>Publicly Available Content Database</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 China</collection><collection>Engineering Collection</collection><jtitle>Journal of food measurement & characterization</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Julio, Luciana M.</au><au>Ruiz-Ruiz, Jorge C.</au><au>Tomás, Mabel C.</au><au>Segura-Campos, Maira R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chia (Salvia hispanica) protein fractions: characterization and emulsifying properties</atitle><jtitle>Journal of food measurement & characterization</jtitle><stitle>Food Measure</stitle><date>2019-12-01</date><risdate>2019</risdate><volume>13</volume><issue>4</issue><spage>3318</spage><epage>3328</epage><pages>3318-3328</pages><issn>2193-4126</issn><eissn>2193-4134</eissn><abstract>A material with a high content of fibers and proteins is generated as a by-product of the chia oil extraction process. A strategy to add value to this by-product is to evaluate its possible use as a food ingredient. Thus, using a chia protein-rich fraction (CPRF) of chia seeds as starting material, albumins, globulins, glutelins, and prolamins fractions were obtained, characterized, and their emulsifying properties investigated. CPRF covers the essential amino acid requirements suggested by FAO; protein fractions only cover the requirements for Tre, Tyr and Val. Protein solubility profile for CPRF, globulins and prolamins was similar, with maximum solubility at pH 9. In contrast, glutelin and albumin fractions showed highest solubility at pH 5. Oil/Water (O/W) emulsions, using the chia protein fractions as emulsifying agent, were obtained at different pH (3, 5, 7, and 9) in their native and denatured state. The global stability and the destabilization kinetics of these systems were evaluated by their backscattering profiles. Additionally, the particle size distributions and their D
4.3
diameter were determined. The emulsions destabilization occurred mainly by creaming process, with globulins as the fraction that led to most stable systems. Besides, high pH values improved the stability of emulsions prepared with globulins, glutelins, and the protein-rich fraction. The heat treatment application only slightly improved the emulsifying activity of the CPRF. These results indicate that chia protein fractions could be used as food ingredient to improve the amino acid content and the techno-functional properties of the functional foods.</abstract><cop>New York</cop><pub>Springer US</pub><doi>10.1007/s11694-019-00254-w</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0002-7664-6647</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Acids Albumin Albumins Amino acids Backscattering Byproducts Chemistry Chemistry and Materials Science Chemistry/Food Science ChiA protein Destabilization Emulsifying agents Emulsions Engineering Fibers Food Science Functional foods & nutraceuticals Globulins Glutelin Heat treatment Kinetics Original Paper pH effects Prolamines Properties (attributes) Proteins Salvia columbariae Seeds Solubility Stability analysis Systems analysis |
| title | Chia (Salvia hispanica) protein fractions: characterization and emulsifying properties |
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