Site-specific N-glycosylation characterization and allergenicity analysis of globulin-1 S allele from wheat
N-glycans in many proteins are of great concern because of their strong association with food allergies. Triticum aestivum (bread wheat), a major food crop, is known as one of the “Big Eight” allergenic groups. However, little research has been done about N-glycans in wheat glycoproteins. In this st...
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| Language: | English |
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Tsinghua University Press
2023-09-01
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| Series: | Food Science and Human Wellness |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213453023000204 |
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| author | Linglin Fu Rongrong Wang Jinru Zhou Chong Wang Yanbo Wang |
| author_facet | Linglin Fu Rongrong Wang Jinru Zhou Chong Wang Yanbo Wang |
| author_sort | Linglin Fu |
| collection | DOAJ |
| description | N-glycans in many proteins are of great concern because of their strong association with food allergies. Triticum aestivum (bread wheat), a major food crop, is known as one of the “Big Eight” allergenic groups. However, little research has been done about N-glycans in wheat glycoproteins. In this study, a soluble wheat glycoprotein was purified from wheat and further identified as globulin-1 S allele (GSA). The wheat GSA displayed significant IgE-binding activity. Moreover, one N-glycosylation site and 6 kinds of N-glycans were identified by mass spectrometry, including 3 high mannose types and 3 complex types. Furthermore, the IgE-binding activity of wheat GSA is proved to be reduced by the removal of N-glycan, thermal treatment (temperatures > 80 °C), and strong acidic treatment (pH 3.0). These findings would provide a better understanding of the effects of N-glycosylation, thermal treatment, and acidic treatment on the molecular characteristics of GSA, and further provide new insights into the development of hypoallergenic wheat products. |
| format | Article |
| id | doaj-art-1e36ae46c4304c6fa17c74781aa920e2 |
| institution | Kabale University |
| issn | 2213-4530 |
| language | English |
| publishDate | 2023-09-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-1e36ae46c4304c6fa17c74781aa920e22025-02-03T05:40:25ZengTsinghua University PressFood Science and Human Wellness2213-45302023-09-0112516011608Site-specific N-glycosylation characterization and allergenicity analysis of globulin-1 S allele from wheatLinglin Fu0Rongrong Wang1Jinru Zhou2Chong Wang3Yanbo Wang4Food Safety Key Laboratory of Zhejiang Province, School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaFood Safety Key Laboratory of Zhejiang Province, School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaFood Safety Key Laboratory of Zhejiang Province, School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China; Zhejiang Engineering Research Institute of Food & Drug Quality and Safety, School of Management and E-Business, Zhejiang Gongshang University, Hangzhou 310018, ChinaFood Safety Key Laboratory of Zhejiang Province, School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaFood Safety Key Laboratory of Zhejiang Province, School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China; Corresponding author at: School of Food Science and Biotechnology, Zhejiang Gongshang University, 18 Xue Zheng Street, Hangzhou 310018, Zhejiang Province, China.N-glycans in many proteins are of great concern because of their strong association with food allergies. Triticum aestivum (bread wheat), a major food crop, is known as one of the “Big Eight” allergenic groups. However, little research has been done about N-glycans in wheat glycoproteins. In this study, a soluble wheat glycoprotein was purified from wheat and further identified as globulin-1 S allele (GSA). The wheat GSA displayed significant IgE-binding activity. Moreover, one N-glycosylation site and 6 kinds of N-glycans were identified by mass spectrometry, including 3 high mannose types and 3 complex types. Furthermore, the IgE-binding activity of wheat GSA is proved to be reduced by the removal of N-glycan, thermal treatment (temperatures > 80 °C), and strong acidic treatment (pH 3.0). These findings would provide a better understanding of the effects of N-glycosylation, thermal treatment, and acidic treatment on the molecular characteristics of GSA, and further provide new insights into the development of hypoallergenic wheat products.http://www.sciencedirect.com/science/article/pii/S2213453023000204Triticum aestivumAllergenGlycoproteinN-glycansN-glycosylationC18-RPLC-MS/MS |
| spellingShingle | Linglin Fu Rongrong Wang Jinru Zhou Chong Wang Yanbo Wang Site-specific N-glycosylation characterization and allergenicity analysis of globulin-1 S allele from wheat Food Science and Human Wellness Triticum aestivum Allergen Glycoprotein N-glycans N-glycosylation C18-RPLC-MS/MS |
| title | Site-specific N-glycosylation characterization and allergenicity analysis of globulin-1 S allele from wheat |
| title_full | Site-specific N-glycosylation characterization and allergenicity analysis of globulin-1 S allele from wheat |
| title_fullStr | Site-specific N-glycosylation characterization and allergenicity analysis of globulin-1 S allele from wheat |
| title_full_unstemmed | Site-specific N-glycosylation characterization and allergenicity analysis of globulin-1 S allele from wheat |
| title_short | Site-specific N-glycosylation characterization and allergenicity analysis of globulin-1 S allele from wheat |
| title_sort | site specific n glycosylation characterization and allergenicity analysis of globulin 1 s allele from wheat |
| topic | Triticum aestivum Allergen Glycoprotein N-glycans N-glycosylation C18-RPLC-MS/MS |
| url | http://www.sciencedirect.com/science/article/pii/S2213453023000204 |
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