Studies on Mold Dextranases:
- 1 January 1972
- journal article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 71 (1) , 57-64
- https://doi.org/10.1093/oxfordjournals.jbchem.a129746
Abstract
Aspergillus carneus dextranase [α1, 6-glucan 6-glucanohydrolase, EC 3. 2. 1. 11] was purified about 60-fold by means of ammonium sulfate fractionation, repeated chromatography on a column of DEAE-cellulose and gel filtration on Bio Gel P-150. The enzyme preparation was further fractionated into two fractions, dextranase I (pI4.12) and dextranase II (pI4.35) by isoelectric focusing. The purified dextranase I was homogeneous as examined by ultracentrifugal analysis and by disc electrophoresis. Dextranase II was also homogeneous in disc electrophoresis. Both enzymes were most active at pH values between 5.0 and 5.5 in 10-min reaction and stable over a pH range from 4.5 to 9.0 at 30°C for 24hr. Some heavy metal ions, such as Cu2+, Hg2+, Fe3+ and Ag+, were found to inactivate both the enzymes. Values of 71,000 for the molecular weight and 4.8 S as s20, w were obtained by ultracentrifugal analyses of the dextranase I.Keywords
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