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http://purl.uniprot.org/citations/9797302http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9797302http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9797302http://www.w3.org/2000/01/rdf-schema#comment"A DNA genomic library constructed from Bacillus stearothermophilus, a gram-positive, facultative thermophilic aerobe that secretes a thermostable beta-mannanase, was screened for mannan hydrolytic activity. Recombinant beta-mannanase activity was detected on the basis of the clearing of halos around Escherichia coli colonies grown on a dye-labelled substrate, Remazol brilliant blue-locust bean gum. The nucleotide sequence of the mannanase gene, manF, corresponded to an open reading frame of 2,085 bp that codes for a 32-amino-acid signal peptide and a mature protein with a molecular mass of 76,089 Da. From sequence analysis, ManF belongs to glycosyl hydrolase family 5 and exhibits higher similarity to eukaryotic than to bacterial mannanases. The manF coding sequence was subcloned into the pH6EX3 expression plasmid and expressed in E. coli as a recombinant fusion protein containing a hexahistidine N-terminal sequence. The fusion protein has thermostability similar to the native enzyme and was purified by Ni2+ affinity chromatography. The values for the kinetic parameters Vmax and Km were 384 U/mg and 2.4 mg/ml, respectively, for the recombinant mannanase and were comparable to those of the native enzyme."xsd:string
http://purl.uniprot.org/citations/9797302http://purl.org/dc/terms/identifier"doi:10.1128/aem.64.11.4428-4432.1998"xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/author"Talbot G."xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/author"Talbot G."xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/author"Sygusch J."xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/author"Sygusch J."xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/author"Ethier N."xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/author"Ethier N."xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/name"Appl. Environ. Microbiol."xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/name"Appl Environ Microbiol"xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/pages"4428-4432"xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/pages"4428-4432"xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/title"Gene cloning, DNA sequencing, and expression of thermostable beta-mannanase from Bacillus stearothermophilus."xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/title"Gene cloning, DNA sequencing, and expression of thermostable beta-mannanase from Bacillus stearothermophilus."xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/volume"64"xsd:string
http://purl.uniprot.org/citations/9797302http://purl.uniprot.org/core/volume"64"xsd:string
http://purl.uniprot.org/citations/9797302http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9797302
http://purl.uniprot.org/citations/9797302http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9797302
http://purl.uniprot.org/citations/9797302http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9797302
http://purl.uniprot.org/citations/9797302http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9797302
http://purl.uniprot.org/uniprot/Q9JP86http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9797302