Modified huauzontle (Chenopodium nuttalliae Saff.) protein-octenyl succinic anhydride corn starch soluble complexes: structural features and in vitro protein and starch digestibility
Native huauzontle protein (P native ) structure was modified by thermal (P heat ), ultrasound (P US ) and pH shifting (P pH11 ). Soluble complexes (SC) were formed between the huauzontle proteins and a commercial octenyl succinic anhydride modified starch (S). The secondary structure of the native a...
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creator | Herrero-Galindo, Adriana López-Monterrubio, Diana I. Aguirre-Mandujano, Eleazar Hernández-Rodríguez, Blanca E. Lobato-Calleros, Consuelo Vernon-Carter, E. Jaime |
description | Native huauzontle protein (P
native
) structure was modified by thermal (P
heat
), ultrasound (P
US
) and pH shifting (P
pH11
). Soluble complexes (SC) were formed between the huauzontle proteins and a commercial octenyl succinic anhydride modified starch (S). The secondary structure of the native and modified huauzontle proteins differed in terms of abundance of β-sheet, α-helix, and β-turn structures. The pH at which maximum presence of SC was observed varied from 5.1 for P
native
-S to 5.8 for P
us
-S complexes, and being the required protein: polysaccharide weight ratio of 1:1 for P
native
-S and of 1:2 for the modified proteins-S. FT-IR confirmed the formation of SC, as the characteristic carboxylate group in S disappeared from its spectra. Also, the absorption peaks of the proteins in the Amide I and II bands shifted slightly from 1630 to 1635 cm
− 1
and 1520 to 1510 cm
− 1
in the SC, indicating conformational changes due to protein-starch interactions. Aggregation of the biopolymers into relatively large particles was observed by SEM in the SC made with modified proteins. SC showed significant differences in the in vitro protein digestibility values, the lowest (85.1 ± 2.3%) occurring for P
native
-S and the highest (92.7 ± 0.7%) for P
US
-S. P
pH11
-S presented the highest resistant starch content (92.6 ± 0.4%). It is concluded that the modification of P
native
through heat, ultrasound and pH shifting allowed establishing different driving conditions for the formation of SC with S, and in vitro digestibility of protein and starch could also be modified. The improved nutritional properties of SC through modification of the protein structure make them potential ingredients for the formulation of sports drinks or low-calorie dairy products. |
doi_str_mv | 10.1007/s11694-024-02836-9 |
format | Article |
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native
) structure was modified by thermal (P
heat
), ultrasound (P
US
) and pH shifting (P
pH11
). Soluble complexes (SC) were formed between the huauzontle proteins and a commercial octenyl succinic anhydride modified starch (S). The secondary structure of the native and modified huauzontle proteins differed in terms of abundance of β-sheet, α-helix, and β-turn structures. The pH at which maximum presence of SC was observed varied from 5.1 for P
native
-S to 5.8 for P
us
-S complexes, and being the required protein: polysaccharide weight ratio of 1:1 for P
native
-S and of 1:2 for the modified proteins-S. FT-IR confirmed the formation of SC, as the characteristic carboxylate group in S disappeared from its spectra. Also, the absorption peaks of the proteins in the Amide I and II bands shifted slightly from 1630 to 1635 cm
− 1
and 1520 to 1510 cm
− 1
in the SC, indicating conformational changes due to protein-starch interactions. Aggregation of the biopolymers into relatively large particles was observed by SEM in the SC made with modified proteins. SC showed significant differences in the in vitro protein digestibility values, the lowest (85.1 ± 2.3%) occurring for P
native
-S and the highest (92.7 ± 0.7%) for P
US
-S. P
pH11
-S presented the highest resistant starch content (92.6 ± 0.4%). It is concluded that the modification of P
native
through heat, ultrasound and pH shifting allowed establishing different driving conditions for the formation of SC with S, and in vitro digestibility of protein and starch could also be modified. The improved nutritional properties of SC through modification of the protein structure make them potential ingredients for the formulation of sports drinks or low-calorie dairy products.</description><identifier>ISSN: 2193-4126</identifier><identifier>EISSN: 2193-4134</identifier><identifier>DOI: 10.1007/s11694-024-02836-9</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Anhydrides ; Biopolymers ; Chemistry ; Chemistry and Materials Science ; Chemistry/Food Science ; Dairy products ; Digestibility ; Driving conditions ; Engineering ; Food Science ; Original Paper ; pH effects ; Polysaccharides ; Protein structure ; Proteins ; Secondary structure ; Starch ; Ultrasonic imaging ; Ultrasound</subject><ispartof>Journal of food measurement & characterization, 2024-10, Vol.18 (10), p.8702-8719</ispartof><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c200t-5ba397a749028b26c4c9438560dc13dd11fbd82338c60002a9ca964f070185963</cites><orcidid>0000-0001-6668-3332</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/s11694-024-02836-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11694-024-02836-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids></links><search><creatorcontrib>Herrero-Galindo, Adriana</creatorcontrib><creatorcontrib>López-Monterrubio, Diana I.</creatorcontrib><creatorcontrib>Aguirre-Mandujano, Eleazar</creatorcontrib><creatorcontrib>Hernández-Rodríguez, Blanca E.</creatorcontrib><creatorcontrib>Lobato-Calleros, Consuelo</creatorcontrib><creatorcontrib>Vernon-Carter, E. Jaime</creatorcontrib><title>Modified huauzontle (Chenopodium nuttalliae Saff.) protein-octenyl succinic anhydride corn starch soluble complexes: structural features and in vitro protein and starch digestibility</title><title>Journal of food measurement & characterization</title><addtitle>Food Measure</addtitle><description>Native huauzontle protein (P
native
) structure was modified by thermal (P
heat
), ultrasound (P
US
) and pH shifting (P
pH11
). Soluble complexes (SC) were formed between the huauzontle proteins and a commercial octenyl succinic anhydride modified starch (S). The secondary structure of the native and modified huauzontle proteins differed in terms of abundance of β-sheet, α-helix, and β-turn structures. The pH at which maximum presence of SC was observed varied from 5.1 for P
native
-S to 5.8 for P
us
-S complexes, and being the required protein: polysaccharide weight ratio of 1:1 for P
native
-S and of 1:2 for the modified proteins-S. FT-IR confirmed the formation of SC, as the characteristic carboxylate group in S disappeared from its spectra. Also, the absorption peaks of the proteins in the Amide I and II bands shifted slightly from 1630 to 1635 cm
− 1
and 1520 to 1510 cm
− 1
in the SC, indicating conformational changes due to protein-starch interactions. Aggregation of the biopolymers into relatively large particles was observed by SEM in the SC made with modified proteins. SC showed significant differences in the in vitro protein digestibility values, the lowest (85.1 ± 2.3%) occurring for P
native
-S and the highest (92.7 ± 0.7%) for P
US
-S. P
pH11
-S presented the highest resistant starch content (92.6 ± 0.4%). It is concluded that the modification of P
native
through heat, ultrasound and pH shifting allowed establishing different driving conditions for the formation of SC with S, and in vitro digestibility of protein and starch could also be modified. The improved nutritional properties of SC through modification of the protein structure make them potential ingredients for the formulation of sports drinks or low-calorie dairy products.</description><subject>Anhydrides</subject><subject>Biopolymers</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chemistry/Food Science</subject><subject>Dairy products</subject><subject>Digestibility</subject><subject>Driving conditions</subject><subject>Engineering</subject><subject>Food Science</subject><subject>Original Paper</subject><subject>pH effects</subject><subject>Polysaccharides</subject><subject>Protein structure</subject><subject>Proteins</subject><subject>Secondary structure</subject><subject>Starch</subject><subject>Ultrasonic imaging</subject><subject>Ultrasound</subject><issn>2193-4126</issn><issn>2193-4134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><recordid>eNp9UctOGzEUHVVFahTyA11Z6qZdTPBrPOPuqqgUJBALYG15bA8xcuzUj4rwYf0-HJLSHQvLV_eex9U9TfMZwSWCsD9LCDFOW4j3byCs5R-aGUactBQR-vGtxuxTs0jpEUKIUE8pI7Pm73XQdrJGg3WR5Tn47Az4ulobH7Z1UjbAl5ylc1YacCunafkNbGPIxvo2qGz8zoFUlLLeKiD9eqej1QaoED1IWUa1Bim4Mrp9b7N15smk73USi8olSgcmI2thUiVrYD34Y3MM_yxem0cZbR9Myna0zubdaXMySZfM4vjPm_vzn3eri_bq5tfl6sdVqzCEue1GSXgve8rrYUbMFFWckqFjUCtEtEZoGvWACRkUq1fBkivJGZ1gD9HQcUbmzZeDbl3od6n-4jGU6KulIAgj2MEO84rCB5SKIaVoJrGNdiPjTiAo9hGJQ0SiRiReIxJ7EjmQUgX7BxP_S7_DegH3Y5f1</recordid><startdate>20241001</startdate><enddate>20241001</enddate><creator>Herrero-Galindo, Adriana</creator><creator>López-Monterrubio, Diana I.</creator><creator>Aguirre-Mandujano, Eleazar</creator><creator>Hernández-Rodríguez, Blanca E.</creator><creator>Lobato-Calleros, Consuelo</creator><creator>Vernon-Carter, E. Jaime</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>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/0000-0001-6668-3332</orcidid></search><sort><creationdate>20241001</creationdate><title>Modified huauzontle (Chenopodium nuttalliae Saff.) protein-octenyl succinic anhydride corn starch soluble complexes: structural features and in vitro protein and starch digestibility</title><author>Herrero-Galindo, Adriana ; López-Monterrubio, Diana I. ; Aguirre-Mandujano, Eleazar ; Hernández-Rodríguez, Blanca E. ; Lobato-Calleros, Consuelo ; Vernon-Carter, E. Jaime</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c200t-5ba397a749028b26c4c9438560dc13dd11fbd82338c60002a9ca964f070185963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Anhydrides</topic><topic>Biopolymers</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chemistry/Food Science</topic><topic>Dairy products</topic><topic>Digestibility</topic><topic>Driving conditions</topic><topic>Engineering</topic><topic>Food Science</topic><topic>Original Paper</topic><topic>pH effects</topic><topic>Polysaccharides</topic><topic>Protein structure</topic><topic>Proteins</topic><topic>Secondary structure</topic><topic>Starch</topic><topic>Ultrasonic imaging</topic><topic>Ultrasound</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Herrero-Galindo, Adriana</creatorcontrib><creatorcontrib>López-Monterrubio, Diana I.</creatorcontrib><creatorcontrib>Aguirre-Mandujano, Eleazar</creatorcontrib><creatorcontrib>Hernández-Rodríguez, Blanca E.</creatorcontrib><creatorcontrib>Lobato-Calleros, Consuelo</creatorcontrib><creatorcontrib>Vernon-Carter, E. Jaime</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 Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</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>Access via ProQuest (Open Access)</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>Herrero-Galindo, Adriana</au><au>López-Monterrubio, Diana I.</au><au>Aguirre-Mandujano, Eleazar</au><au>Hernández-Rodríguez, Blanca E.</au><au>Lobato-Calleros, Consuelo</au><au>Vernon-Carter, E. Jaime</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Modified huauzontle (Chenopodium nuttalliae Saff.) protein-octenyl succinic anhydride corn starch soluble complexes: structural features and in vitro protein and starch digestibility</atitle><jtitle>Journal of food measurement & characterization</jtitle><stitle>Food Measure</stitle><date>2024-10-01</date><risdate>2024</risdate><volume>18</volume><issue>10</issue><spage>8702</spage><epage>8719</epage><pages>8702-8719</pages><issn>2193-4126</issn><eissn>2193-4134</eissn><abstract>Native huauzontle protein (P
native
) structure was modified by thermal (P
heat
), ultrasound (P
US
) and pH shifting (P
pH11
). Soluble complexes (SC) were formed between the huauzontle proteins and a commercial octenyl succinic anhydride modified starch (S). The secondary structure of the native and modified huauzontle proteins differed in terms of abundance of β-sheet, α-helix, and β-turn structures. The pH at which maximum presence of SC was observed varied from 5.1 for P
native
-S to 5.8 for P
us
-S complexes, and being the required protein: polysaccharide weight ratio of 1:1 for P
native
-S and of 1:2 for the modified proteins-S. FT-IR confirmed the formation of SC, as the characteristic carboxylate group in S disappeared from its spectra. Also, the absorption peaks of the proteins in the Amide I and II bands shifted slightly from 1630 to 1635 cm
− 1
and 1520 to 1510 cm
− 1
in the SC, indicating conformational changes due to protein-starch interactions. Aggregation of the biopolymers into relatively large particles was observed by SEM in the SC made with modified proteins. SC showed significant differences in the in vitro protein digestibility values, the lowest (85.1 ± 2.3%) occurring for P
native
-S and the highest (92.7 ± 0.7%) for P
US
-S. P
pH11
-S presented the highest resistant starch content (92.6 ± 0.4%). It is concluded that the modification of P
native
through heat, ultrasound and pH shifting allowed establishing different driving conditions for the formation of SC with S, and in vitro digestibility of protein and starch could also be modified. The improved nutritional properties of SC through modification of the protein structure make them potential ingredients for the formulation of sports drinks or low-calorie dairy products.</abstract><cop>New York</cop><pub>Springer US</pub><doi>10.1007/s11694-024-02836-9</doi><tpages>18</tpages><orcidid>https://orcid.org/0000-0001-6668-3332</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Anhydrides Biopolymers Chemistry Chemistry and Materials Science Chemistry/Food Science Dairy products Digestibility Driving conditions Engineering Food Science Original Paper pH effects Polysaccharides Protein structure Proteins Secondary structure Starch Ultrasonic imaging Ultrasound |
title | Modified huauzontle (Chenopodium nuttalliae Saff.) protein-octenyl succinic anhydride corn starch soluble complexes: structural features and in vitro protein and starch digestibility |
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