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|Title:||Efficient and rapid purification of lentil <img src='/image/spc_char/alpha.gif'>-galactosidase by affinity precipitation with alginate|
|Authors:||Çelem, Evran Bıçak|
Bolle, Sharon Sibel
|Abstract:||<smarttagtype namespaceuri="urn:schemas-microsoft-com:office:smarttags" name="metricconverter"> <img src='/image/spc_char/alpha.gif'>-Galactosidase (<img src='/image/spc_char/alpha.gif'>-D-galactoside galactohydrolase, EC 126.96.36.199) was purified (26-fold) from the germinating seeds of lentil (<i style="">Lens culinaris</i>) by affinity precipitation with alginate. The purified enzyme gave a single band corresponding to molecular mass of 40 kDa on SDS-PAGE. The optimum temperature and pH of the enzyme were determined as 40<sup>o</sup>C and 5.5, respectively. The enzyme was very stable at a temperature range of 4-65<sup>o</sup>C and at a pH range of 4-7. The values of kinetic constants <i style="">K</i><sub>m</sub> and <i style="">V</i><sub>max</sub> using p-nitrophenyl-<img src='/image/spc_char/alpha.gif'>-D-galactopyranoside (PNPG) as substrate were 0.191 mM and 0.73 U, respectively. Results suggest that affinity precipitation is an attractive process for the purification of <img src='/image/spc_char/alpha.gif'>-galactosidase. </smarttagtype>|
|ISSN:||0975-0959 (Online); 0301-1208 (Print)|
|Appears in Collections:||IJBB Vol.46(5) [October 2009]|
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