Self-Assembly of Benzyloxycarbonyl Histidine with Zinc Ions for the Construction of Esterase Mimics

Esterases have been applied in many industrial fields. However, many esterases have inherent defects as natural enzyme, such as low long-term storability, poor operational stability, and difficulty in recovery for reuse. Herein, two histidine derivatives with different structures, L-benzyloxycarbonyl histidine (Z-L-His) and D-benzyloxycarbonyl histidine (Z-D-His), were used to self-assemble with zinc ions to construct esterase mimics (Z-L-His/Zn2+and Z-D-His/Zn2+) based on a minimalist strategy. Two natural enzymes were used for comparison. It was found that the Z-His structure influenced only the stereoselectivity of the enzyme mimic. The kinetics of Z-L-His/Zn2+followed the classical Michaelis–Menten equation, and its catalytic efficiency was comparable to that of natural enzymes. It was verified that Z-L-His/Zn2+had good catalytic stability over a wide range of pH, organic solvent concentrations, ionic strengths, and incubation temperatures. Z-L-His/Zn2+retained high activity after incubation in different environments for 7 d, demonstrating excellent long-term storage stability. Moreover, Z-L-His/Zn2+exhibited good reusability, retaining 93% of its original activity after six cycles, proving its potential for industrial applications in mimicking esterase.