Characterization of a Novel Low Molecular Weight Sucrase From Filamentous Fungus Termitomyces Clypeatus
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
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Title |
Characterization of a Novel Low Molecular Weight Sucrase From Filamentous Fungus Termitomyces Clypeatus
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Creator |
Choudhury, Sudeshna
Ghorai, Shakuntala Banik, Samudra Prasad Pal, Sagata Basak, Soumen Khowala, Suman |
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Subject |
Drug Development/Diagnostics & Biotechnology
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Description |
An extracellular sucrase from the culture filtrate of filamentous basidiomycota Termitomyces clypeatus
grown on high sucrose (5%, w/v) was purified by gel filtration chromatography, ion exchange
chromatography and HPGPLC. The biochemical properties, molecular weight and conformation of
sucrase produced were significantly different from the sucrase earlier purified from sucrose (1%, w/v)
mediumin the fungus. Purified sucrase was characterized as a low molecular weight protein of 13.5 kDa
as approximated by SDS-PAGE and HPGPLC and exhibited predominantly random coil conformation in
far-UV CD spectra. The enzyme was optimally active at 47 8C and pH 5.0. Km and catalytic activity of the
enzyme for sucrose were found to be 3.5 mM and 1.06 U/mg/mM, respectively. The enzyme was
maximally active towards sucrose than to raffinose and sucrase activity was significantly inhibited by
bivalent metal ions and reducing group agents. The results indicated that due to changes in aggregation
pattern, molecular organization of purified sucrase, produced in high sucrose medium, was altered and
was different from the previously reported enzyme. This is the first report of a sucrase of such low size
showing activity.
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Date |
2009
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Type |
Article
PeerReviewed |
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Format |
application/pdf
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Identifier |
http://www.eprints.iicb.res.in/977/1/10_PB_2009.pdf
Choudhury, Sudeshna and Ghorai, Shakuntala and Banik, Samudra Prasad and Pal, Sagata and Basak, Soumen and Khowala, Suman (2009) Characterization of a Novel Low Molecular Weight Sucrase From Filamentous Fungus Termitomyces Clypeatus. Process Biochemistry, 44 (10). pp. 1075-1082. |
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Relation |
http://dx.doi.org/10.1016/j.procbio.2009.05.009
http://www.eprints.iicb.res.in/977/ |
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