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

Lekha Singh | Zendy; Gaurav Sharma | Zendy; Asha Sharma | Zendy; Gyanendra Awasthi | Zendy; Lokendra Kumar | Zendy; Mohammad Irfan Ali | Zendy; Sarmad Moin | Zendy

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

Author(s) -

Lekha Singh,

Gaurav Sharma,

Asha Sharma,

Gyanendra Awasthi,

Lokendra Kumar,

Mohammad Irfan Ali,

Sarmad Moin

Publication year - 2020

Publication title -

journal of pure and applied microbiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.149

H-Index - 16

eISSN - 2581-690X

pISSN - 0973-7510

DOI - 10.22207/jpam.14.2.36

Subject(s) - isolation (microbiology) , esterase , rhodococcus , chemistry , microbiology and biotechnology , rhodococcus equi , chromatography , biology , biochemistry , enzyme , gene , virulence

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.

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