Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility
Plant-based proteins are often associated with a range of health benefits. Most research primarily investigates pea and soy proteins, while lentil proteins received minimal attention. This study evaluates the effect of protein complexation (using the pH-shifting technique) coupled with trehalose con...
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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.crstbi.2024.100135 https://www.sciencedirect.com/science/article/pii/S2665928X24000126 http://hdl.handle.net/10576/59333 |
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| _version_ | 1857415086780448768 |
|---|---|
| author | Mohammad, Alrosan |
| author2 | Madi Almajwal, Ali Al-Qaisi, Ali Gammoh, Sana H. Alu'datt, Muhammad R. Al Qudsi, Farah Tan, Thuan-Chew A. Razzak Mahmood, Ammar Maghaydah, Sofyan |
| author2_role | author author author author author author author author |
| author_facet | Mohammad, Alrosan Madi Almajwal, Ali Al-Qaisi, Ali Gammoh, Sana H. Alu'datt, Muhammad R. Al Qudsi, Farah Tan, Thuan-Chew A. Razzak Mahmood, Ammar Maghaydah, Sofyan |
| author_role | author |
| dc.creator.none.fl_str_mv | Mohammad, Alrosan Madi Almajwal, Ali Al-Qaisi, Ali Gammoh, Sana H. Alu'datt, Muhammad R. Al Qudsi, Farah Tan, Thuan-Chew A. Razzak Mahmood, Ammar Maghaydah, Sofyan |
| dc.date.none.fl_str_mv | 2024-09-26T08:47:56Z 2024-11-23 |
| dc.format.none.fl_str_mv | application/pdf |
| dc.identifier.none.fl_str_mv | http://dx.doi.org/10.1016/j.crstbi.2024.100135 Alrosan, M., Almajwal, A. M., Al-Qaisi, A., Gammoh, S., Alu'datt, M. H., Al Qudsi, F. R., ... & Maghaydah, S. (2024). Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility. Current Research in Structural Biology, 7, 100135. https://www.sciencedirect.com/science/article/pii/S2665928X24000126 http://hdl.handle.net/10576/59333 7 2665-928X |
| 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 | Whey proteins Lentil proteins Digestibility Protein structure Disaccharide |
| dc.title.none.fl_str_mv | Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility |
| dc.type.none.fl_str_mv | Article info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/article |
| description | Plant-based proteins are often associated with a range of health benefits. Most research primarily investigates pea and soy proteins, while lentil proteins received minimal attention. This study evaluates the effect of protein complexation (using the pH-shifting technique) coupled with trehalose conjugation on lentil and whey proteins. The protein structures after the modification were analysed using spectroscopic methods: Fourier-transform infrared, ultraviolet spectra, and fluorescence spectra. The amide group I, conformation protein, and tertiary structure of the trehalose-conjugated lentil-whey protein complexes (T-LWPs) showed significant changes (P < 0.05). Moreover, the surface properties (surface hydrophobicity and charges) of T-LWPs were significantly modified (P < 0.05), from 457 to 324 a.u and from 36 to −40 mV, respectively. Due to these modifications on the protein structures, the protein digestibility (80–86%) and water solubility (90–94.5%) of T-LWPs increased significantly (P < 0.05) with the increase in the trehalose concentration, from 0 (control) to 5% (w/w), respectively. This study suggested that coupling protein complexation and trehalose conjugation can enhance the overall properties of lentil-based protein complexes. With this enhancement, more opportunities in the utilisation of lentils are to be expected. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | qu_f63c77b01a12428cb48a7e0f93b0389d |
| identifier_str_mv | Alrosan, M., Almajwal, A. M., Al-Qaisi, A., Gammoh, S., Alu'datt, M. H., Al Qudsi, F. R., ... & Maghaydah, S. (2024). Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility. Current Research in Structural Biology, 7, 100135. 7 2665-928X |
| language_invalid_str_mv | en |
| network_acronym_str | qu |
| network_name_str | Qatar University repository |
| oai_identifier_str | oai:qspace.qu.edu.qa:10576/59333 |
| 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 | Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubilityMohammad, AlrosanMadi Almajwal, AliAl-Qaisi, AliGammoh, SanaH. Alu'datt, MuhammadR. Al Qudsi, FarahTan, Thuan-ChewA. Razzak Mahmood, AmmarMaghaydah, SofyanWhey proteinsLentil proteinsDigestibilityProtein structureDisaccharidePlant-based proteins are often associated with a range of health benefits. Most research primarily investigates pea and soy proteins, while lentil proteins received minimal attention. This study evaluates the effect of protein complexation (using the pH-shifting technique) coupled with trehalose conjugation on lentil and whey proteins. The protein structures after the modification were analysed using spectroscopic methods: Fourier-transform infrared, ultraviolet spectra, and fluorescence spectra. The amide group I, conformation protein, and tertiary structure of the trehalose-conjugated lentil-whey protein complexes (T-LWPs) showed significant changes (P < 0.05). Moreover, the surface properties (surface hydrophobicity and charges) of T-LWPs were significantly modified (P < 0.05), from 457 to 324 a.u and from 36 to −40 mV, respectively. Due to these modifications on the protein structures, the protein digestibility (80–86%) and water solubility (90–94.5%) of T-LWPs increased significantly (P < 0.05) with the increase in the trehalose concentration, from 0 (control) to 5% (w/w), respectively. This study suggested that coupling protein complexation and trehalose conjugation can enhance the overall properties of lentil-based protein complexes. With this enhancement, more opportunities in the utilisation of lentils are to be expected.This research was funded by the Researchers Supporting Project number (019032), Jordan University of Science and Technology Irbid, Jordan. This research was also funded by the Researchers Supporting Project number (RSP2024R502), King Saud University , Riyadh, Saudi Arabia.Elsevier2024-09-26T08:47:56Z2024-11-23Articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://dx.doi.org/10.1016/j.crstbi.2024.100135Alrosan, M., Almajwal, A. M., Al-Qaisi, A., Gammoh, S., Alu'datt, M. H., Al Qudsi, F. R., ... & Maghaydah, S. (2024). Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility. Current Research in Structural Biology, 7, 100135.https://www.sciencedirect.com/science/article/pii/S2665928X24000126http://hdl.handle.net/10576/5933372665-928Xenhttp://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccessoai:qspace.qu.edu.qa:10576/593332024-09-26T19:06:21Z |
| spellingShingle | Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility Mohammad, Alrosan Whey proteins Lentil proteins Digestibility Protein structure Disaccharide |
| status_str | publishedVersion |
| title | Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility |
| title_full | Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility |
| title_fullStr | Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility |
| title_full_unstemmed | Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility |
| title_short | Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility |
| title_sort | Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility |
| topic | Whey proteins Lentil proteins Digestibility Protein structure Disaccharide |
| url | http://dx.doi.org/10.1016/j.crstbi.2024.100135 https://www.sciencedirect.com/science/article/pii/S2665928X24000126 http://hdl.handle.net/10576/59333 |