Identification and comparison of N-glycome profiles from common dietary protein sources
The N-glycomes of bovine whey, egg white, pea, and soy protein isolates are described here. N-glycans from four protein isolates were analyzed by HILIC high performance liquid chromatography and quadrupole time-of-flight tandem mass spectrometry (HILIC-FLD-QTOF-MS/MS). In total, 33 N-glycans from bo...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-01-01
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| Series: | Food Chemistry: X |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590157524009131 |
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| author | Matthew Bolino İzzet Avcı Hacı Mehmet Kayili Hatice Duman Bekir Salih Sercan Karav Steven A. Frese |
| author_facet | Matthew Bolino İzzet Avcı Hacı Mehmet Kayili Hatice Duman Bekir Salih Sercan Karav Steven A. Frese |
| author_sort | Matthew Bolino |
| collection | DOAJ |
| description | The N-glycomes of bovine whey, egg white, pea, and soy protein isolates are described here. N-glycans from four protein isolates were analyzed by HILIC high performance liquid chromatography and quadrupole time-of-flight tandem mass spectrometry (HILIC-FLD-QTOF-MS/MS). In total, 33 N-glycans from bovine whey and egg white and 10 N-glycans from soy and pea glycoproteins were identified. The type of N-glycans per glycoprotein source were attributable to differences in biosynthetic glycosylation pathways. Animal glycoprotein sources favored a combination of complex and hybrid glycan configurations, while the plant proteins were dominated by oligomannosidic N-glycans. Bovine whey glycoprotein isolate contained the most diverse N-glycans by monosaccharide composition as well as structure, while plant sources such as pea and soy glycoprotein isolates contained an overlap of oligomannosidic N-glycans. The results suggest N-glycan structure and composition is dependent on the host organism which are driven by the differences in N-glycan biosynthetic pathways. |
| format | Article |
| id | doaj-art-1e21fc32809a429a90401cc9ea943e22 |
| institution | Kabale University |
| issn | 2590-1575 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry: X |
| spelling | doaj-art-1e21fc32809a429a90401cc9ea943e222025-02-12T05:31:46ZengElsevierFood Chemistry: X2590-15752025-01-0125102025Identification and comparison of N-glycome profiles from common dietary protein sourcesMatthew Bolino0İzzet Avcı1Hacı Mehmet Kayili2Hatice Duman3Bekir Salih4Sercan Karav5Steven A. Frese6Department of Nutrition, University of Nevada, Reno, Reno, NV 89557, USADepartment of Chemistry, Faculty of Science, Hacettepe University, 06500 Ankara, TR, Republic of TürkiyeDepartment of Biomedical Engineering, Faculty of Engineering, Karabük University, 78000 Karabük, TR, Republic of TürkiyeDepartment of Molecular Biology and Genetics, Çanakkale Onsekiz Mart University, 17020 Çanakkale, TR, Republic of TürkiyeDepartment of Chemistry, Faculty of Science, Hacettepe University, 06500 Ankara, TR, Republic of TürkiyeDepartment of Molecular Biology and Genetics, Çanakkale Onsekiz Mart University, 17020 Çanakkale, TR, Republic of TürkiyeDepartment of Nutrition, University of Nevada, Reno, Reno, NV 89557, USA; University of Nevada, Reno School of Medicine, Reno, NV 89557, USA; Corresponding author at: Department of Nutrition, University of Nevada, Reno, 1664 N Virginia St, Reno, NV 89557, USA.The N-glycomes of bovine whey, egg white, pea, and soy protein isolates are described here. N-glycans from four protein isolates were analyzed by HILIC high performance liquid chromatography and quadrupole time-of-flight tandem mass spectrometry (HILIC-FLD-QTOF-MS/MS). In total, 33 N-glycans from bovine whey and egg white and 10 N-glycans from soy and pea glycoproteins were identified. The type of N-glycans per glycoprotein source were attributable to differences in biosynthetic glycosylation pathways. Animal glycoprotein sources favored a combination of complex and hybrid glycan configurations, while the plant proteins were dominated by oligomannosidic N-glycans. Bovine whey glycoprotein isolate contained the most diverse N-glycans by monosaccharide composition as well as structure, while plant sources such as pea and soy glycoprotein isolates contained an overlap of oligomannosidic N-glycans. The results suggest N-glycan structure and composition is dependent on the host organism which are driven by the differences in N-glycan biosynthetic pathways.http://www.sciencedirect.com/science/article/pii/S2590157524009131N-glycanProteinMass spectrometryMicrobiomeN-glycomeGlycan |
| spellingShingle | Matthew Bolino İzzet Avcı Hacı Mehmet Kayili Hatice Duman Bekir Salih Sercan Karav Steven A. Frese Identification and comparison of N-glycome profiles from common dietary protein sources Food Chemistry: X N-glycan Protein Mass spectrometry Microbiome N-glycome Glycan |
| title | Identification and comparison of N-glycome profiles from common dietary protein sources |
| title_full | Identification and comparison of N-glycome profiles from common dietary protein sources |
| title_fullStr | Identification and comparison of N-glycome profiles from common dietary protein sources |
| title_full_unstemmed | Identification and comparison of N-glycome profiles from common dietary protein sources |
| title_short | Identification and comparison of N-glycome profiles from common dietary protein sources |
| title_sort | identification and comparison of n glycome profiles from common dietary protein sources |
| topic | N-glycan Protein Mass spectrometry Microbiome N-glycome Glycan |
| url | http://www.sciencedirect.com/science/article/pii/S2590157524009131 |
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