Scientists studied how to attach an enzyme called L-lactate oxidase (LOx) to tiny beads (carriers) so it can be reused, for example, in sensors or chemical production. They tested different types of beads (made of agarose, polyurethane, or polymethacrylate) with different chemical hooks (amine, NiNTA, or epoxide) on their surfaces. They tried sticking the enzyme on permanently (covalent binding) or just letting it attach loosely (adsorption). They measured how active the enzyme was on the beads. The best results came from using beads made of agarose (a seaweed-based gel) with amine hooks, especially when attached covalently.
However, they found that simply letting the enzyme adsorb to these agarose-amine beads worked almost as well and even made the enzyme more resistant to heat. Surprisingly, the enzyme also stuck well to NiNTA beads, even without the special ‘His-tag’ handle NiNTA usually grabs. This suggests that simple electrical attraction (ionic interaction) is very important for sticking the enzyme to the beads. Adding a His-tag handle did help the enzyme work more efficiently once attached. Washing with salt solution removed some enzyme from the amine beads but almost none from the NiNTA beads, confirming the strong attachment. The study shows that agarose-amine beads are good carriers for LOx, and simple adsorption is an effective and stabilizing method.
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