General methods to render macroporous stationary phases nonporous and deformable, exemplified with agarose and silica beads and their use in high-performance ion-exchange and hydrophobic-interaction chromatography of proteins

1991 ◽  
Vol 31 (1-2) ◽  
pp. 85-94 ◽  
Author(s):  
S. Hjertén ◽  
J. Mohammad ◽  
K. -O. Eriksson ◽  
J. -L. Liao
2017 ◽  
Vol 42 (6) ◽  
Author(s):  
Şaban Keskin ◽  
Nagihan Saglam Ertunga

AbstractObjective:In this study, α-amylase from a thermophilic bacterium Geobacillus sp. TF14 was purified and immobilized on two different supports.Methods:Ion exchange and hydrophobic interaction chromatography techniques were employed for the purification.Results:The enzyme was purified as 17.11 fold and determined as a single band of 54 kDa on SDS-PAGE. Purified enzyme showed two pH optimums of pH 5.00 and pH 9.00 and the enzyme is quite stable at these pHs over a period of 48 h. Purified enzyme showed maximal activity at 75°C and stability at this temperature over a period of 72 h. It was observed that CaConclusion:It can be concluded that the purified enzyme may find application in many fields of starch based industries.


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