dc.contributor.author |
Şener, Aysun |
|
dc.date.accessioned |
2022-07-22T11:24:49Z |
|
dc.date.available |
2022-07-22T11:24:49Z |
|
dc.date.issued |
2015 |
|
dc.identifier.issn |
0022-1155 |
|
dc.identifier.uri |
http://dspace.adiyaman.edu.tr:8080/xmlui/handle/20.500.12414/3412 |
|
dc.description.abstract |
This research was carried out to determine biochemical properties of beta-glucosidase (beta-D-glucoside glucohydrolase, EC 3.2.1.21) isolated from Turkish tea leaves. Two protein peaks containing beta-glucosidase activity were recovered and characterized, which were denoted as isoenzyme A and isoenzyme B. Their pH optimum, thermal resistances, affinity towards p-nitrophenyl-beta-D-glucopyranoside differed markedly. They both displayed maximal activity at pH 5.0. The effects of the inhibitors tested varied in a dose dependent manner. |
tr |
dc.language.iso |
en |
tr |
dc.publisher |
Springer India |
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dc.subject |
Beta-glucosidase |
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dc.subject |
Purification |
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dc.subject |
Tea leaves |
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dc.subject |
Kinetics |
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dc.subject |
Thermal inactivation |
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dc.subject |
Thermal stability |
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dc.title |
Extraction, partial purification and determination of some biochemical properties of beta-glucosidase from Tea Leaves (Camellia sinensis L.) |
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dc.type |
Article |
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dc.identifier.endpage |
8328 |
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dc.identifier.issue |
12 |
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dc.identifier.startpage |
8322 |
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dc.identifier.volume |
52 |
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dc.source.title |
Journal Of Food Science And Technology-Mysore |
tr |