Isolation of monoclonal antibody from a Chinese hamster ovary supernatant. II: Dynamics of the integrated separation on ion exchange and hydrophobic interaction chromatography media

2013 ◽  
Vol 1305 ◽  
pp. 64-75 ◽  
Author(s):  
Wojciech Marek ◽  
Renata Muca ◽  
Sylwia Woś ◽  
Wojciech Piątkowski ◽  
Dorota Antos
Author(s):  
Sai Rashmika Velugula-Yellela ◽  
David N. Powers ◽  
Phillip Angart ◽  
Anneliese Faustino ◽  
Talia Faison ◽  
...  

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.


2020 ◽  
Vol 36 (4) ◽  
Author(s):  
Luis Toronjo‐Urquiza ◽  
Adelina E. Acosta‐Martin ◽  
David C. James ◽  
Tibor Nagy ◽  
Robert J. Falconer

2015 ◽  
Vol 120 (3) ◽  
pp. 340-346 ◽  
Author(s):  
Takeshi Okumura ◽  
Kenji Masuda ◽  
Kazuhiko Watanabe ◽  
Kenji Miyadai ◽  
Koichi Nonaka ◽  
...  

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