| 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 |
|