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Preserving enzymatic activity and enhancing biochemical stability of glutathione transferase by soluble additives under free and tethered conditions
Author(s) -
Karamitros Christos S.,
Labrou Nikolaos E.
Publication year - 2017
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1535
Subject(s) - sucrose , chemistry , enzyme , glutathione , dextran , glutathione transferase , transferase , enzyme assay , biochemistry , chromatography
Abstract In the present study, we report the effect of four different soluble additives (sucrose, lactitol, superfloc c577, and dextran sulfate) on the stability of glutathione transferase 1 enzyme from Zea mays ( Zm GSTF1‐1) under free and tethered conditions at 4 and 25 °C. Among all additives, the best stabilizing effects were observed in the case of superfloc c577 and sucrose at both tested temperatures, yet at distinct concentrations at each condition. Those two stabilizing agents were further combined and potential positive synergistic effects were investigated. In addition, we assessed the long‐term storage and operational stability of Zm GSTF1‐1 under tethered conditions in the presence of additives, which provided the most conducive effects on its stability under free conditions. Our results strongly suggest that the presence of additives may be beneficial to the stability of the enzyme under both free and tethered conditions. Thermodynamic analysis of the free enzyme in the presence of sucrose, which exhibited the best stabilizing effect at both temperatures, shed light on the possible mechanism of action. Given the considerable importance of the development of GST‐based biosensors with prolonged stability, the present work may be of general interest to researchers in the field of applied enzymology.