Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting technique
Soluble trehalose-conjugated quinoa proteins (T-QPs) were effectively prepared using the pH-shifting mechanism. The structural properties of the T-QPs were evaluated using a comparative evaluation, which included analyzing the amide I, surface charge and hydrophobicity, protein conformation, thermal...
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| المؤلف الرئيسي: | |
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| مؤلفون آخرون: | , , , , , , , , |
| التنسيق: | article |
| منشور في: |
2024
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| الموضوعات: | |
| الوصول للمادة أونلاين: | http://dx.doi.org/10.1016/j.fochx.2024.101397 https://www.sciencedirect.com/science/article/pii/S2590157524002840 http://hdl.handle.net/10576/59277 |
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| _version_ | 1857415086510964736 |
|---|---|
| author | Mohammad, Alrosan |
| author2 | Almajwal, Ali Madi Al-Qaisi, Ali Gammoh, Sana Alu'datt, Muhammad H. Al Qudsi, Farah R. Tan, Thuan-Chew Razzak Mahmood, Ammar A. Maghaydah, Sofyan Al-Massad, Motasem |
| author2_role | author author author author author author author author author |
| author_facet | Mohammad, Alrosan Almajwal, Ali Madi Al-Qaisi, Ali Gammoh, Sana Alu'datt, Muhammad H. Al Qudsi, Farah R. Tan, Thuan-Chew Razzak Mahmood, Ammar A. Maghaydah, Sofyan Al-Massad, Motasem |
| author_role | author |
| dc.creator.none.fl_str_mv | Mohammad, Alrosan Almajwal, Ali Madi Al-Qaisi, Ali Gammoh, Sana Alu'datt, Muhammad H. Al Qudsi, Farah R. Tan, Thuan-Chew Razzak Mahmood, Ammar A. Maghaydah, Sofyan Al-Massad, Motasem |
| dc.date.none.fl_str_mv | 2024-09-25T10:21:06Z 2024-04-18 |
| dc.format.none.fl_str_mv | application/pdf |
| dc.identifier.none.fl_str_mv | http://dx.doi.org/10.1016/j.fochx.2024.101397 Alrosan, M., Almajwal, A. M., Al-Qaisi, A., Gammoh, S., Alu'datt, M. H., Al Qudsi, F. R., ... & Al-Massad, M. (2024). Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting technique. Food Chemistry: X, 22, 101397. 2590-1575 https://www.sciencedirect.com/science/article/pii/S2590157524002840 http://hdl.handle.net/10576/59277 22 |
| dc.language.none.fl_str_mv | en |
| dc.publisher.none.fl_str_mv | Elsevier |
| dc.rights.none.fl_str_mv | http://creativecommons.org/licenses/by-nc/4.0/ info:eu-repo/semantics/openAccess |
| dc.subject.none.fl_str_mv | Trehalose Structure properties Water solubility Protein digestibility |
| dc.title.none.fl_str_mv | Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting technique |
| dc.type.none.fl_str_mv | Article info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/article |
| description | Soluble trehalose-conjugated quinoa proteins (T-QPs) were effectively prepared using the pH-shifting mechanism. The structural properties of the T-QPs were evaluated using a comparative evaluation, which included analyzing the amide I, surface charge and hydrophobicity, protein conformation, thermal stability, and protein structures. The results suggested that the development of the T-QPs was influenced mainly by no-covalent bonds. These interactions significantly influenced (P < 0.05) the quinoa proteins' conformation and higher-protein structure. T-QP had significant (P < 0.05) surface properties. Furthermore, the T-QPs exhibited improved solubility (79.7 to 88.4%) and digestibility (79.8 to 85.1%). Therefore, quinoa protein proved an excellent plant-based protein for conjugation with disaccharides. These findings provide significant insight into the potential development of modified proteins with enhanced solubility and digestibility by creating trehalose-conjugated plant-based proteins. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | qu_7ff933f63064a38f515b8040d649c809 |
| identifier_str_mv | Alrosan, M., Almajwal, A. M., Al-Qaisi, A., Gammoh, S., Alu'datt, M. H., Al Qudsi, F. R., ... & Al-Massad, M. (2024). Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting technique. Food Chemistry: X, 22, 101397. 2590-1575 22 |
| language_invalid_str_mv | en |
| network_acronym_str | qu |
| network_name_str | Qatar University repository |
| oai_identifier_str | oai:qspace.qu.edu.qa:10576/59277 |
| publishDate | 2024 |
| publisher.none.fl_str_mv | Elsevier |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | http://creativecommons.org/licenses/by-nc/4.0/ |
| spelling | Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting techniqueMohammad, AlrosanAlmajwal, Ali MadiAl-Qaisi, AliGammoh, SanaAlu'datt, Muhammad H.Al Qudsi, Farah R.Tan, Thuan-ChewRazzak Mahmood, Ammar A.Maghaydah, SofyanAl-Massad, MotasemTrehaloseStructure propertiesWater solubilityProtein digestibilitySoluble trehalose-conjugated quinoa proteins (T-QPs) were effectively prepared using the pH-shifting mechanism. The structural properties of the T-QPs were evaluated using a comparative evaluation, which included analyzing the amide I, surface charge and hydrophobicity, protein conformation, thermal stability, and protein structures. The results suggested that the development of the T-QPs was influenced mainly by no-covalent bonds. These interactions significantly influenced (P < 0.05) the quinoa proteins' conformation and higher-protein structure. T-QP had significant (P < 0.05) surface properties. Furthermore, the T-QPs exhibited improved solubility (79.7 to 88.4%) and digestibility (79.8 to 85.1%). Therefore, quinoa protein proved an excellent plant-based protein for conjugation with disaccharides. These findings provide significant insight into the potential development of modified proteins with enhanced solubility and digestibility by creating trehalose-conjugated plant-based proteins.The funding for this research was provided by the Research Supporting Project number ( RSP2024R502 ) at King Saud University in Riyadh, Saudi Arabia.Elsevier2024-09-25T10:21:06Z2024-04-18Articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://dx.doi.org/10.1016/j.fochx.2024.101397Alrosan, M., Almajwal, A. M., Al-Qaisi, A., Gammoh, S., Alu'datt, M. H., Al Qudsi, F. R., ... & Al-Massad, M. (2024). Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting technique. Food Chemistry: X, 22, 101397.2590-1575https://www.sciencedirect.com/science/article/pii/S2590157524002840http://hdl.handle.net/10576/5927722enhttp://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccessoai:qspace.qu.edu.qa:10576/592772024-09-25T19:05:53Z |
| spellingShingle | Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting technique Mohammad, Alrosan Trehalose Structure properties Water solubility Protein digestibility |
| status_str | publishedVersion |
| title | Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting technique |
| title_full | Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting technique |
| title_fullStr | Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting technique |
| title_full_unstemmed | Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting technique |
| title_short | Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting technique |
| title_sort | Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting technique |
| topic | Trehalose Structure properties Water solubility Protein digestibility |
| url | http://dx.doi.org/10.1016/j.fochx.2024.101397 https://www.sciencedirect.com/science/article/pii/S2590157524002840 http://hdl.handle.net/10576/59277 |