%0 Journal Article
%T Production and purification of a-amylase from Aspergillus niger 33-19 CNMN FD 02A mutant form
%A Alexandra CILOCI
%A Cezara BIVOL
%A Maria STRATAN
%A Veaceslav REVA
%J Analele Universitatii din Oradea, Fascicula Biologie
%D 2012
%I University of Oradea Publishing House
%X 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. ¦Á-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 ¦Á-amylase resulted in an enzyme specific activity of 199.68U/mg protein with purification fold 8.9. The analyses of purified ¦Á-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 ¦Á-amylaseizoforms.
%K Aspergillus niger
%K ¦Á-amylase
%K enzyme purification
%K ion exchange chromatography
%K SDS-PAGE
%U http://www.bioresearch.ro/bioresearch/2012-1/074-079-AUOFB.19.1.2012-CILOCI.A.-Ins.Micro.Biotech.Acad.Sc.Md.Chis.-Production.and.purification.pdf