ISSN: 0973-7510
E-ISSN: 2581-690X
, Gaurav Sharma1 , Asha Sharma3, Gyanendra Awasthi2, Lokendra Kumar2,4, Mohammad Irfan Ali1 and Sarmad Moin1A thermophilic esterase isolated from Rhodococcus sp. LKE-021. This enzyme was purified with purification fold 60 from the crude extracts of enzyme and recovery of enzyme obtained approximately 21%. The specific activity of the LKE-021 esteraseis 795.1 U/mg. SDS-PAGE analysis determined the molecular weight of LKE-21 esteraseis around 32,000Da/32KDa. The enzyme activity of LKE-021 esterase exhibited over a wide range of temperature i.e. 30° to 80°C and the enzyme remained stable when incubated on 60° for 2h. This indicates that the isolated LKE-021 esterase is thermostable. The isolated enzyme exhibits activity on various pH ranges from 2.0 to 12.0 and the highest activity observed on 11.0 pH.The LKE-021 esterase was active after proteinase K treatment and shows over 75 % specific activity i.e. 50 U/µg Proteinase K.
Rhodococcus, isolation & purification,characterization, Polyacrylamide Gel, Extremophiles
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