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Purification and Characterization of Two Different -L-Rhamnosidases,RhaA and RhaB, from Aspergillus aculeatus

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dc.creator Manzanares, Paloma
dc.creator van den Broeck, Hetty C.
dc.creator Graaff, Leo H. de
dc.creator Visser, Jaap
dc.date 2008-02-25T10:40:31Z
dc.date 2008-02-25T10:40:31Z
dc.date 2001-05
dc.date.accessioned 2017-01-31T01:00:23Z
dc.date.available 2017-01-31T01:00:23Z
dc.identifier Applied and Environmental Microbiology 67(5) : 2230-2234 (2001)
dc.identifier http://hdl.handle.net/2431/73
dc.identifier http://hdl.handle.net/10261/3070
dc.identifier.uri http://dspace.mediu.edu.my:8181/xmlui/handle/2431/73
dc.description Two 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.description EC project AIR3-CT94-2193
dc.format 141808 bytes
dc.format 2459 bytes
dc.format application/pdf
dc.format text/plain
dc.language eng
dc.publisher American Society for Microbiology
dc.rights closedAccess
dc.subject Aspergillus aculeatus
dc.subject Rhamnosidases
dc.title Purification and Characterization of Two Different -L-Rhamnosidases,RhaA and RhaB, from Aspergillus aculeatus
dc.type Artículo


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