Enhancing enzyme stability against TiO2-UV induced inactivation
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Updated: Aug 20, 2026

Measuring Enzymatic Stability by Isothermal Titration Calorimetry
Published on: March 26, 2019
Bhalchandra S Lele1, Alan J Russell
1McGowan Institute for Regenerative Medicine and Department of Bioengineering, 100, Technology Drive, University of Pittsburgh, Pittsburgh, Pennsylvania 15219, USA.
Abstract:
The use of enzymes in conjunction with inorganic photocatalysts requires stability against photooxidation. In this paper, we describe enhanced stabilization of a model enzyme, chymotrypsin, to photooxidation driven by titanium dioxide exposed to ultraviolet light (TiO(2)-UV). Stabilization is achieved conjugating the enzyme with an oligomeric adduct of UV-absorbing (2-[3-(2H-benzotriazol-2-yl)-4-hydroxyphenyl]ethyl methacrylate) (HBMA) and free radical-absorbing 2-methacryloyloxyethyl-6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylate (Trolox-HEMA). Juxtaposition of the antioxidant Trolox with the UV absorber HBMA within a single chain reduced the rate of deactivation of the former by TiO(2)-UV. This enables modified enzyme, which is adsorbed on TiO(2), to absorb both UV-light and free radicals and locally reduce the rate of photooxidation. Interestingly, Trolox was more readily deactivated by TiO(2)-UV when it was conjugated separately to chymotrypsin that had been pre-modified with HBMA moieties.
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