ISSN: 0973-7510

E-ISSN: 2581-690X

Research Article | Open Access
Lekha Singh1,2, Gaurav Sharma1 , Asha Sharma3, Gyanendra Awasthi2, Lokendra Kumar2,4, Mohammad Irfan Ali1 and Sarmad Moin1
1School of Applied Sciences, Suresh Gyan Vihar University, Jaipur, Rajasthan – 302 017, India.
2Department of Biochemistry, Dolphin PG Institute of Biomedical and Natural Science, Dehradun, Uttarakhand – 248 007, India.
3SW.P.N.K.S. Govt. P.G. College, Dausa – 303303, Rajasthan, India.
4Department of Microbiology, PM College of Education, Karsua, Aligarh, Uttar Pradesh – 202 001, India.
J Pure Appl Microbiol. 2020;14(2):1387-1395 | Article Number: 6058 | © The Author(s). 2020
Received: 24/01/2020 | Accepted: 21/05/2020 | Published: 25/06/2020

A 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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