A Thermostable Fe/Mn SOD of Geobacillus Sp. PCH100 Isolated from Glacial Soil of Indian Trans-Himalaya Exhibits Activity in the Presence of Common Inhibitors.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES(2021)
Abstract
Superoxide dismutases are the enzymes involved in dismutation of superoxide radicals into oxygen and hydrogen peroxide. The present work reports a thermostable Fe/Mn SOD of Geobacillus sp. strain PCH100 (GsSOD) isolated from glacial soil. Purified recombinant GsSOD is a dimeric protein of similar to 57 kDa that exhibited highest activity at a temperature of 10 degrees C and pH of 7.8. Maximum enzyme velocity and Michaelis constant of the GsSOD were 1098.90 units/mg and 0.62 mu M, respectively. At 80 degrees C, thermal inactivation rate constant and half-life of GsSOD were 3.33 x 10(-3) min(-1) and 208 min, respectively. Interestingly, GsSOD tolerated a temperature of 100 degrees C and 130 degrees C up to 15 min and 5 min, respectively. Circular dichroism and differential scanning calorimetry confirmed thermostable nature of GsSOD. Apoenzyme of GsSOD regained enzymatic activity in the presence of Fe2+ and Mn2+ as metal ion cofactors. GsSOD was stable under varying concentrations of chemicals, namely ethylenediaminetetraacetic acid, potassium cyanide, hydrogen peroxide, chloroform-ethanol, 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate, Tween-20, Triton X-100, urea, and guanidine hydrochloride. The enzyme exhibited >70% activity in presence of 10 mM metal ions. Owing to its thermostable nature and resistance to chemical inhibitors, GsSOD is a potential enzyme for industrial applications. (C) 2021 Elsevier B.V. All rights reserved.
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Key words
Extremophile,Thermostability,Enzyme kinetics,Apoenzyme,Microbes
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