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Updated: Aug 13, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Transglutaminase-catalyzed site-specific glycosidation of catalase with aminated dextran
Aymara Valdivia1, Reynaldo Villalonga, Prospero Di Pierro
1Center for Enzyme Technology, University of Matanzas, Autopista a Varadero Km 3 1/2, Matanzas, C.P. 44740, Cuba.
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 degrees 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.
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