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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 1
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pubmed:dateCreated |
2002-2-6
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pubmed:databankReference |
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pubmed:abstractText |
Extracellular exo-inulinase has been isolated from a solid-phase culture of the filamentous fungus Aspergillus awamori var. 2250. The apparent molecular mass of the monomer enzyme was 69 +/- kDa, with a pI of 4.4 and a pH optimum of 4.5. The enzyme hydrolysed the beta-(2-->1)-fructan (inulin) and beta-(2-->6)-fructan (levan) via exo-cleavage, releasing fructose. The values for the Michaelis constants K(m) and V(max) in the hydrolysis of inulin were 0.003 +/- 0.0001 mM and 175 +/- 5 micromol.min(-1).mg(-1). The same parameters in the hydrolysis of levan were 2.08 +/- 0.04 mg/ml and 1.2 +/- 0.02 micromol/min per mg, respectively. The gene and cDNA encoding the A. awamori exo-inulinase were cloned and sequenced. The amino acid sequence indicated that the protein belongs to glycoside hydrolase family 32. A surprisingly high similarity was found to fructosyltransferase from Aspergillus foetidus (90.7% on the level of the amino acid sequence), despite the fact that the latter enzyme is unable to hydrolyse inulin and levan. Crystals of the native exo-inulinase were obtained and found to belong to the orthorhombic space group P2(1)2(1)2(1) with cell parameters a=64.726 A (1A=0.1 nm), b=82.041 A and c=136.075 A. Crystals diffracted beyond 1.54 A, and useful X-ray data were collected to a resolution of 1.73 A.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-10052135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-10432595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-10533713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-10548559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-10548561,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-10949149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-11115126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-11305239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-1398976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-14938350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-15299862,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-1747104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-2113524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-2254250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-2440339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-343633,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-4204552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-5838092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-6650261,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-8481000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-8580088,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-8662946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-9486422,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-9495772,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-9805373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11829749-9895294
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0264-6021
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pubmed:author |
pubmed-author:ArandMichaelM,
pubmed-author:ChepurnayaOlga VOV,
pubmed-author:EneyskayaElena VEV,
pubmed-author:GolubevAlexander MAM,
pubmed-author:KorneevaOlga SOS,
pubmed-author:KulminskayaAnna AAA,
pubmed-author:NetoJ R BrandaoJR,
pubmed-author:NeustroevKirill NKN,
pubmed-author:PolikarpovIgorI,
pubmed-author:ShabalinKonstantin AKA,
pubmed-author:ShishliannikovSergei MSM,
pubmed-author:WattiezRR
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
362
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
131-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11829749-Amino Acid Sequence,
pubmed-meshheading:11829749-Aspergillus,
pubmed-meshheading:11829749-Base Sequence,
pubmed-meshheading:11829749-Crystallography, X-Ray,
pubmed-meshheading:11829749-DNA, Complementary,
pubmed-meshheading:11829749-DNA Primers,
pubmed-meshheading:11829749-Glycoside Hydrolases,
pubmed-meshheading:11829749-Molecular Sequence Data,
pubmed-meshheading:11829749-Reverse Transcriptase Polymerase Chain Reaction
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pubmed:year |
2002
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pubmed:articleTitle |
Purification, characterization, gene cloning and preliminary X-ray data of the exo-inulinase from Aspergillus awamori.
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pubmed:affiliation |
Institute of Toxicology, University of Mainz, Mainz, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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