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dc.creatorManzanares, Paloma-
dc.creatorvan den Broeck, Hetty C.-
dc.creatorGraaff, Leo H. de-
dc.creatorVisser, Jaap-
dc.date2008-02-25T10:40:31Z-
dc.date2008-02-25T10:40:31Z-
dc.date2001-05-
dc.date.accessioned2017-01-31T01:00:23Z-
dc.date.available2017-01-31T01:00:23Z-
dc.identifierApplied and Environmental Microbiology 67(5) : 2230-2234 (2001)-
dc.identifierhttp://hdl.handle.net/2431/73-
dc.identifierhttp://hdl.handle.net/10261/3070-
dc.identifier.urihttp://dspace.mediu.edu.my:8181/xmlui/handle/2431/73-
dc.descriptionTwo proteins exhibiting -L-rhamnosidase activity, RhaA and RhaB, were identified upon fractionation and purification of a culture filtrate from Aspergillus aculeatus grown on hesperidin. Both proteins were shown to be N glycosylated and had molecular masses of 92 and 85 kDa, of which approximately 24 and 15%, respectively, were contributed by carbohydrate. RhaA and RhaB, optimally active at pH 4.5 to 5, showed Km and Vmax values of 2.8 mM and 24 U/mg (RhaA) and 0.30 mM and 14 U/mg (RhaB) when tested for p-nitrophenyl--L-rhamnopyranoside. Both enzymes were able to hydrolyze -1,2 and -1,6 linkages to -D-glucosides. Using polyclonal antibodies, the corresponding cDNA of both -L-rhamnosidases, rhaA and rhaB, was cloned. On the basis of the amino acid sequences derived from the cDNA clones, both proteins are highly homologous (60% identity).-
dc.descriptionEC project AIR3-CT94-2193-
dc.format141808 bytes-
dc.format2459 bytes-
dc.formatapplication/pdf-
dc.formattext/plain-
dc.languageeng-
dc.publisherAmerican Society for Microbiology-
dc.rightsclosedAccess-
dc.subjectAspergillus aculeatus-
dc.subjectRhamnosidases-
dc.titlePurification and Characterization of Two Different -L-Rhamnosidases,RhaA and RhaB, from Aspergillus aculeatus-
dc.typeArtículo-
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