Hen egg can cause food hypersensitivity in infants and young children, and ovomucoid is the most allergenic factor among proteins contained in egg white. Since proteinase treatment, a well-recognized strategy in reducing food allergenicity, is ineffective when applied to ovomucoid because of its ability to act as trypsin inhibitor, we investigated the possibility of reducing the ovomucoid antiprotease activity and antigenic properties by covalently modifying its structure. The present paper reports data showing the ability of the Gln115 residue of ovomucoid to act as an acyl donor substrate for the enzyme transglutaminase and, as a consequence, to give rise to a covalent monodansylcadaverine conjugate of the protein in the presence of both enzyme and the diamine dansylated derivative. Moreover, we demonstrated that the obtained structural modification of ovomucoid significantly reduced the capability of the protein to inhibit trypsin activity, also having impact on its anti-ovomucoid serum-binding properties.

Transglutaminase-mediated modification of ovomucoid. Effect on its trypsin inhibitory activity and antigenic properties / Porta, Raffaele; Giosafatto, CONCETTA VALERIA LUCIA; DI PIERRO, Prospero; Sorrentino, Angela; Mariniello, Loredana. - In: AMINO ACIDS. - ISSN 0939-4451. - 44:1(2013), pp. 285-292. [10.1007/s00726-011-1155-0]

Transglutaminase-mediated modification of ovomucoid. Effect on its trypsin inhibitory activity and antigenic properties

PORTA, RAFFAELE;GIOSAFATTO, CONCETTA VALERIA LUCIA;DI PIERRO, PROSPERO;SORRENTINO, ANGELA;MARINIELLO, LOREDANA
2013

Abstract

Hen egg can cause food hypersensitivity in infants and young children, and ovomucoid is the most allergenic factor among proteins contained in egg white. Since proteinase treatment, a well-recognized strategy in reducing food allergenicity, is ineffective when applied to ovomucoid because of its ability to act as trypsin inhibitor, we investigated the possibility of reducing the ovomucoid antiprotease activity and antigenic properties by covalently modifying its structure. The present paper reports data showing the ability of the Gln115 residue of ovomucoid to act as an acyl donor substrate for the enzyme transglutaminase and, as a consequence, to give rise to a covalent monodansylcadaverine conjugate of the protein in the presence of both enzyme and the diamine dansylated derivative. Moreover, we demonstrated that the obtained structural modification of ovomucoid significantly reduced the capability of the protein to inhibit trypsin activity, also having impact on its anti-ovomucoid serum-binding properties.
2013
Transglutaminase-mediated modification of ovomucoid. Effect on its trypsin inhibitory activity and antigenic properties / Porta, Raffaele; Giosafatto, CONCETTA VALERIA LUCIA; DI PIERRO, Prospero; Sorrentino, Angela; Mariniello, Loredana. - In: AMINO ACIDS. - ISSN 0939-4451. - 44:1(2013), pp. 285-292. [10.1007/s00726-011-1155-0]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/562045
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