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Molecular cloning, expression and characterization of a novel feruloyl esterase enzyme from the symbionts of termite (Coptotermes formosanus) gut.

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Title Molecular cloning, expression and characterization of a novel feruloyl esterase enzyme from the symbionts of termite (Coptotermes formosanus) gut.
Not Available
 
Creator Chandrasekharaiah M
Thulasi A
Bagath M
Prasanna Kumar D
Santosh SS
Palanivel C
Lyju JV
Sampath KT
 
Subject feruloyl esterase
Cloning
Expression
Metagenome
Termite
 
Description Not Available
Termites play an important role in the degradation of dead plant materials and have acquired endogenous and symbiotic cellulose digestion capabilities. The feruloyl esterase enzyme (FAE) gene amplified from the metagenomic DNA of Coptotermes formosanus gut was cloned in the TA cloning vector and subcloned into a pET32a expression vector. The Ft3-7 gene has 84% sequence identity with Clostridium saccharolyticum and shows amino acid sequence identity with predicted xylanase/chitin deacetylase and endo-1,4-beta-xylanase. The sequence analysis reveals that probably Ft3-7 could be a new gene and that its molecular mass was 18.5 kDa. The activity of the recombinant enzyme (Ft3-7) produced in Escherichia coli (E.coli) was 21.4 U with substrate ethyl ferulate and its specific activity was 24.6 U/mg protein. The optimum pH and temperature for enzyme activity were 7.0 and 37∘ C , respectively. The substrate utilization preferences and sequence similarity of the Ft3-7 place it in the type-D sub-class of FAE.
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Date 2021-08-06T06:13:52Z
2021-08-06T06:13:52Z
2011-01-01
 
Type Journal
 
Identifier Chandrasekharaiah M, Thulasi A, Bagath M, Prasanna Kumar D, Santosh SS, Palanivel C, Lyju JV and Sampath KT. 2011. Molecular cloning, expression and characterization of a novel feruloyl esterase enzyme from the symbionts of termite (Coptotermes formosanus) gut. Biochemistry and Molecular Biology Reports, 44: 52-57
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http://krishi.icar.gov.in/jspui/handle/123456789/53357
 
Language English
 
Relation Not Available;
 
Publisher Korean Society for Biochemistry and Molecular Biology