Purification, Isolation, and Characterization of Esterase from Rhodococcus sp. LKE-021

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 molecula...

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Bibliographic Details
Published in:Journal of pure & applied microbiology : an international research journal of microbiology 2020-06, Vol.14 (2), p.1387-1395
Main Authors: Singh, Lekha, Sharma, Gaurav, Sharma, Asha, Awasthi, Gyanendra, Kumar, Lokendra, Ali, Mohammad Irfan, Moin, Sarmad
Format: Article
Language:English
Subjects:
Analysis
characterization
Enzymes
Ethylenediaminetetraacetic acid
extremophiles
Hydrolases
isolation & purification
Phenolphthalein
polyacrylamide gel
rhodococcus
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Summary: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[degrees] to 80[degrees]C and the enzyme remained stable when incubated on 60[degrees] 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/[micro]g Proteinase K. Keywords: Rhodococcus, isolation & purification, characterization, Polyacrylamide Gel, Extremophiles
ISSN:0973-7510
2581-690X
DOI:10.22207/JPAM.14.2.36