| dc.creator |
ŞAHİN, Selmihan |
|
| dc.creator |
Demir, Saime Nur |
|
| dc.creator |
ÖZMEN, İsmail |
|
| dc.creator |
BIYIK, HACI HALİL |
|
| dc.date |
2014-12-31T22:00:00Z |
|
| dc.date.accessioned |
2020-10-06T11:38:06Z |
|
| dc.date.available |
2020-10-06T11:38:06Z |
|
| dc.identifier |
e787a657-bdf5-4637-a300-9d11571abaff |
|
| dc.identifier |
https://avesis.sdu.edu.tr/publication/details/e787a657-bdf5-4637-a300-9d11571abaff/oai |
|
| dc.identifier.uri |
http://acikerisim.sdu.edu.tr/xmlui/handle/123456789/74891 |
|
| dc.description |
Enzyme complex contained four CMCases activity from Aspergillus tamari Redpep4 was purified with ammonium sulphate precipitation and gel filtration chromotography. A. tamari Redpep4 produced maximum CMCase when wheat bran was used as carbon source. Four bands on PAGE have CMCase activity according to zymogram activity test. The optimum temperature and pH of CMCase was 60 degrees C and pH 4.0, respectively. The enzymes can sustain 57% of its activity at 60 degrees C for 7 h. Obtained cellulase complex had high substrate specifity toward CMC. Additionally, effects of some metal ions and surfactants on CMCase were determined. BaCl2 activated it, whereas some of other salt ions inhibited. Kinetic studies showed that K-m and V-max value of CMCase were 2.27 mg/mL and 6.61 EU/mL, respectively. |
|
| dc.language |
eng |
|
| dc.rights |
info:eu-repo/semantics/closedAccess |
|
| dc.title |
CHARACTERIZATION OF CMCASES OBTAINED FROM LOCAL ISOLATE Aspergillus tamari Redpep4 AND EFFECT METAL SALTS ON ITS ACTIVITY |
|
| dc.type |
info:eu-repo/semantics/article |
|