dc.contributor.author |
Rashamuse, K
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dc.contributor.author |
Sanyika, W
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dc.contributor.author |
Ronneburg, T
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dc.contributor.author |
Brady, D
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dc.date.accessioned |
2012-07-03T11:02:55Z |
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dc.date.available |
2012-07-03T11:02:55Z |
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dc.date.issued |
2012-01 |
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dc.identifier.citation |
Rashamuse, K, Sanyika, W, Ronneburg, T and Brady, D. 2012. A feruloyl esterase derived from a leachate metagenome library. BMB Reports, vol. 45(1), pp 14-19 |
en_US |
dc.identifier.issn |
1976-6696 |
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dc.identifier.uri |
http://bmbreports.org/jbmb/jbmb_files/%5B45-1%5D1201272127_(014-019)BMB11-165.pdf
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dc.identifier.uri |
http://hdl.handle.net/10204/5970
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dc.description |
Copyright: 2012 Korean Society for Biochemistry and Molecular Biology |
en_US |
dc.description.abstract |
A feruloyl esterase encoding gene (designated fae6), derived from a leachate metagenomic library, was cloned and the nucleotide sequence of the insert DNA determined. Translational analysis revealed that fae6 consists of a 515 amino acid polypeptide, encoding a 55 kDa pre-protein. The Fae6 primary structure contained the G-E-S-A-G sequence, which corresponds well with a typical catalytic serine sequence motif (G-x-S-x-G). The fae6 gene was successfully over-expressed in E. coli and the recombinant protein was purified to 8.4 fold enrichment with 17% recovery. The KM data showed Fae6 has a high affinity to methyl sinapate while thermostability data indicated that Fae6 was thermolabile with a half life (T1/2) < 30 min at 50oC. High affinity for Fae6 against methyl sinapate, methyl ferulate and ethyl ferulate suggest that the enzyme can be useful in hydrolyzing ferulated polysaccharides in a biorefinery process. |
en_US |
dc.language.iso |
en |
en_US |
dc.publisher |
Korean Society for Biochemistry and Molecular Biology |
en_US |
dc.relation.ispartofseries |
Workflow;7184 |
|
dc.subject |
Feruloyl esterase |
en_US |
dc.subject |
Lipolytic enzymes |
en_US |
dc.subject |
Metagenomics |
en_US |
dc.title |
A feruloyl esterase derived from a leachate metagenome library |
en_US |
dc.type |
Article |
en_US |
dc.identifier.apacitation |
Rashamuse, K., Sanyika, W., Ronneburg, T., & Brady, D. (2012). A feruloyl esterase derived from a leachate metagenome library. http://hdl.handle.net/10204/5970 |
en_ZA |
dc.identifier.chicagocitation |
Rashamuse, K, W Sanyika, T Ronneburg, and D Brady "A feruloyl esterase derived from a leachate metagenome library." (2012) http://hdl.handle.net/10204/5970 |
en_ZA |
dc.identifier.vancouvercitation |
Rashamuse K, Sanyika W, Ronneburg T, Brady D. A feruloyl esterase derived from a leachate metagenome library. 2012; http://hdl.handle.net/10204/5970. |
en_ZA |
dc.identifier.ris |
TY - Article
AU - Rashamuse, K
AU - Sanyika, W
AU - Ronneburg, T
AU - Brady, D
AB - A feruloyl esterase encoding gene (designated fae6), derived from a leachate metagenomic library, was cloned and the nucleotide sequence of the insert DNA determined. Translational analysis revealed that fae6 consists of a 515 amino acid polypeptide, encoding a 55 kDa pre-protein. The Fae6 primary structure contained the G-E-S-A-G sequence, which corresponds well with a typical catalytic serine sequence motif (G-x-S-x-G). The fae6 gene was successfully over-expressed in E. coli and the recombinant protein was purified to 8.4 fold enrichment with 17% recovery. The KM data showed Fae6 has a high affinity to methyl sinapate while thermostability data indicated that Fae6 was thermolabile with a half life (T1/2) < 30 min at 50oC. High affinity for Fae6 against methyl sinapate, methyl ferulate and ethyl ferulate suggest that the enzyme can be useful in hydrolyzing ferulated polysaccharides in a biorefinery process.
DA - 2012-01
DB - ResearchSpace
DP - CSIR
KW - Feruloyl esterase
KW - Lipolytic enzymes
KW - Metagenomics
LK - https://researchspace.csir.co.za
PY - 2012
SM - 1976-6696
T1 - A feruloyl esterase derived from a leachate metagenome library
TI - A feruloyl esterase derived from a leachate metagenome library
UR - http://hdl.handle.net/10204/5970
ER -
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en_ZA |