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http://dspace.mediu.edu.my:8181/xmlui/handle/2431/73| Title: | Purification and Characterization of Two Different -L-Rhamnosidases,RhaA and RhaB, from Aspergillus aculeatus |
| Keywords: | Aspergillus aculeatus Rhamnosidases |
| Publisher: | American Society for Microbiology |
| 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). EC project AIR3-CT94-2193 |
| URI: | http://dspace.mediu.edu.my:8181/xmlui/handle/2431/73 |
| Other Identifiers: | Applied and Environmental Microbiology 67(5) : 2230-2234 (2001) http://hdl.handle.net/2431/73 http://hdl.handle.net/10261/3070 |
| Appears in Collections: | Digital Csic |
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