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Production and purification of a-amylase from Aspergillus niger 33-19 CNMN FD 02A mutant form

Author(s): Alexandra CILOCI | Cezara BIVOL | Maria STRATAN | Veaceslav REVA | Steliana CLAPCO | Janeta TIURIN | Svetlana LABLIUC

Journal: Analele Universitatii din Oradea, Fascicula Biologie
ISSN 1224-5119

Volume: TOM XIX;
Issue: 1;
Start page: 74;
Date: 2012;
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Keywords: Aspergillus niger | α-amylase | enzyme purification | ion exchange chromatography | SDS-PAGE

From mutant micelial strain Aspergillus niger 33-19 CNMN FD 02A, through alcohol ethylic precipitation of cultural liquid, amylolytic preparation Amilonigrin AS was isolated with 10x degree of purity and a specific activity of 138.3U/mg proteins. α-Amylase from 20mM Tris-HCl extract of Amilonigrin AS was purified to homogeneity by PD-10 column gel filtration and HiTrap TM Q column ion exchange chromatography. A trial for the purification of α-amylase resulted in an enzyme specific activity of 199.68U/mg protein with purification fold 8.9. The analyses of purified α-amylase for molecular weight was carried out by SDSPAGE electrophoresis, with revealed two polypeptide bands estimated to be 66 and 40.5kDa, probably being two α-amylaseizoforms.
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