An enzymatic approach, based on a transglutaminase-catalyzed coupling reaction, was investigated to modify bovine liver catalase with an end-group aminated dextran derivative. We demonstrated that catalase activity increased after enzymatic glycosidation and that the conjugate was 3.8-fold more stable to thermal inactivation at 55 ◦C and 2-fold more resistant to proteolytic degradation by trypsin. Moreover, the transglutaminase-mediated modification also improved the pharmacokinetics behavior of catalase, increasing 2.5-fold its plasma half-life time and reducing 3-fold the total clearance after its i.v. administration in rats.
Transglutaminase-catalyzed site-specific glycosidation of catalase with aminated dextran / A., Valdivia; R., Villalonga; DI PIERRO, Prospero; Y., Perez; Mariniello, Loredana; L., Gomez; Porta, Raffaele. - In: JOURNAL OF BIOTECHNOLOGY. - ISSN 0168-1656. - STAMPA. - 122:(2006), pp. 326-333. [10.1016/j.jbiotec.2005.12.014]
Transglutaminase-catalyzed site-specific glycosidation of catalase with aminated dextran
DI PIERRO, PROSPERO;MARINIELLO, LOREDANA;PORTA, RAFFAELE
2006
Abstract
An enzymatic approach, based on a transglutaminase-catalyzed coupling reaction, was investigated to modify bovine liver catalase with an end-group aminated dextran derivative. We demonstrated that catalase activity increased after enzymatic glycosidation and that the conjugate was 3.8-fold more stable to thermal inactivation at 55 ◦C and 2-fold more resistant to proteolytic degradation by trypsin. Moreover, the transglutaminase-mediated modification also improved the pharmacokinetics behavior of catalase, increasing 2.5-fold its plasma half-life time and reducing 3-fold the total clearance after its i.v. administration in rats.File | Dimensione | Formato | |
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