NDLI: Shewanella sp. Ke75 esterase with specificity for p-nitorphenyl butyrate: Gene cloning and characterization

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Shewanella sp. Ke75 esterase with specificity for p-nitorphenyl butyrate: Gene cloning and characterization

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Journal of the Korean Society for Applied Biological Chemistry : Volume 55

Journal of the Korean Society for Applied Biological Chemistry : Volume 54

Journal of the Korean Society for Applied Biological Chemistry : Volume 53

Journal of the Korean Society for Applied Biological Chemistry : Volume 52

Shewanella sp. Ke75 esterase with specificity for p-nitorphenyl butyrate: Gene cloning and characterization

Content Provider	Springer Nature Link
Author	Song, Jung Hun Nam, Bo Hye Park, In Suk Lee, Sang Jun Kim, Woo Jin Kim, Dong Gyun Kim, Young Ok Kong, Hee Jeong Kim, Bong Seok Kim, Hyung Kwoun Jee, Young Ju
Copyright Year	2013
Abstract	A bacterial strain that produces a cold-adapted esterase was isolated from tidal flats and identified as Shewanella sp. Ke75. In the present study, the corresponding gene was cloned using the shotgun method. The amino acid sequence deduced from the nucleotide sequence (957 bp) corresponded to a protein of 318 amino acid residues with a calculated molecular weight of 34875 Da. The esterase showed 68 and 57% identities with the putative esterases of Shewanella amazonensis SB2B and Colwellia psychrerythraea 34H, respectively. The esterase contained a putative leader sequence, as well as the conserved catalytic triad (Ser, His, Asp), consensus pentapeptide GXSXG, and oxyanion hole sequence (HG). The protein Ke75 was produced in both soluble and insoluble forms when Escherichia coli cells harboring the gene were cultured at 30°C. The enzyme showed specificity for C4 (butyrate) as a substrate, with little activity toward the other p-nitrophenyl esters tested. The optimum pH and temperature for enzyme activity were pH 9.0 and 30°C, respectively. Relative activity remained up to 60% even at 5°C with an activation energy of 6.29 kcal/mol, which indicated that it was a cold-adapted enzyme. Enzyme activity was enhanced in the presence of Mn$^{2+}$ ions, but inhibited by Cd$^{2+}$, Cu$^{2+}$, Hg$^{2+}$, and Zn$^{2+}$ ions.
Starting Page	55
Ending Page	62
Page Count	8
File Format	PDF
ISSN	17382203
Journal	Journal of the Korean Society for Applied Biological Chemistry
Volume Number	56
Issue Number	1
e-ISSN	2234344X
Language	English
Publisher	The Korean Society for Applied Biological Chemistry
Publisher Date	2013-02-28
Publisher Place	Seoul
Access Restriction	Subscribed
Subject Keyword	substrate specificity Applied Microbiology Biological Techniques cold-adapted esterase gene expression Bioorganic Chemistry Shewanella sp.
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry, Genetics and Molecular Biology

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Shewanella sp. Ke75 esterase with specificity for p-nitorphenyl butyrate: Gene cloning and characterization

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Shewanella sp. Ke75 esterase with specificity for p-nitorphenyl butyrate: Gene cloning and characterization