Effect of transglutaminase-catalyzed glycosylation on the allergenicity and conformational structure of shrimp (Metapenaeus ensis) tropomyosin
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- 作者：Fangzhou Yuana ; Liangtao Lva ; Zhenxing Lia ; lizhenxing@ouc.edu.cn" class="auth_mail" title="E-mail the corresponding author ; Nasha Mia ; Hairong Chenb ; Hong Lina
- 关键词：1-Anilino-8-naphthalene-sulfonate (PubChem CID ; 1369) ; 3 ; 3&prime ; 5 ; 5&prime ; -Tetramethylbenzidine (PubChem CID ; 41206) ; o-Phthalaldehyde (PubChem CID ; 4807) ; DL-Dithiothreitol (PubChem CID ; 446094) ; Brilliant Blue R (PubChem CID ; 61365) ; Acrylamide (PubChem CID ; 6579) ; Tween 20 (PubChem CID ; 443314)
- 刊名：Food Chemistry
- 出版年：2017
- 出版时间：15 March 2017
- 年：2017
- 卷：219
- 期：Complete
- 页码：215-222
- 全文大小：1428 K
文摘
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Transglutaminase-catalyzed glycosylation can modulate the IgE binding capacity of tropomyosin.
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The glycosylation rate correlated with reaction temperature.
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Conformational structure of tropomyosin can be modified by transglutaminase-catalyzed glycosylation.
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Transglutaminase-catalyzed glycosylation can be used for allergenicity reduction of tropomyosin.