AI Article Synopsis
- This study investigated how heat affects the enzyme β-glucosidase from Hypocrea orientalis, revealing that its inactivation is irreversible and follows a first-order reaction.
- It found that certain substrates can effectively protect the enzyme from thermal damage, especially glucose at a concentration of 20mM, which kept the enzyme's activity intact up to 70°C.
- Additionally, glucose not only reduces the inactivation rate of the enzyme but also stabilizes its structure against heat, as shown through intrinsic fluorescence and docking simulations.
Article Abstract
Thermal inactivation kinetics of Hypocrea orientalis β-glucosidase and effect of glucose on thermostability of the enzyme have been determined in this paper. Kinetic studies showed that the thermal inactivation was irreversible and first-order reaction. The microscopic rate constants for inactivation of free enzyme and substrate-enzyme complex were both determined, which suggested that substrates can protect β-glucosidase against thermal deactivation effectively. On the other hand, glucose was found to protect β-glucosidase from heat inactivation to remain almost whole activity below 70°C at 20mM concentration, whereas the apparent inactivation rate of BG decreased to be 0.3×10(-3)s(-1) in the presence of 5mM glucose, smaller than that of sugar-free enzyme (1.91×10(-3)s(-1)). The intrinsic fluorescence spectra results showed that glucose also had stabilizing effect on the conformation of BG against thermal denaturation. Docking simulation depicted the interaction mode between glucose and active residues of the enzyme to produce stabilizing effect.
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| http://dx.doi.org/10.1016/j.ijbiomac.2015.09.022 | DOI Listing |
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