Phase Behavior and Density for Binary and Ternary Solutions of PEG 4000 + Triammonium Citrate + Water Aqueous Two Phase Systems at Different Temperatures

2013 ◽  
Vol 58 (2) ◽  
pp. 315-321 ◽  
Author(s):  
Rajendran Govindarajan ◽  
Kesavan Divya ◽  
Muthiah Perumalsamy
2019 ◽  
Vol 64 (5) ◽  
pp. 2143-2152
Author(s):  
Pedro Lúcio Bonifácio ◽  
Cínthia das Dores Aguiar ◽  
Bruno Giordano Alvarenga ◽  
Nelson Henrique Teixeira Lemes ◽  
Luciano Sindra Virtuoso

1995 ◽  
Vol 28 (10) ◽  
pp. 3597-3603 ◽  
Author(s):  
Maarten Svensson ◽  
Per Linse ◽  
Folke Tjerneld

1999 ◽  
Vol 30 (4) ◽  
pp. 324-331 ◽  
Author(s):  
Maria Estela da Silva ◽  
Telma Teixeira Franco

This work investigated the partitioning of b-galactosidase from Kluyveromyces fragilis in aqueous two-phase systems (ATPS) by bioaffinity. PEG 4000 was chemically activated with thresyl chloride, and the biospecific ligand p-aminophenyl 1-thio-b-D-galactopyranoside (APGP) was attached to the activated PEG 4000. A new two-step method for extraction and purification of the enzyme b-galactosidase from Kluyveromyces fragilis was developed. In the first step, a system composed of 6% PEG 4000-APGP and 8% dextran 505 was used, where b-galactosidase was strongly partitioned to the top phase (K = 2,330). In the second step, a system formed of 13% PEG-APGP and 9% phosphate salt was used to revert the value of the partition coefficient of b-galactosidase (K = 2 x 10-5) in order to provide the purification and recovery of 39% of the enzyme in the bottom salt-rich phase.


2015 ◽  
Vol 60 (6) ◽  
pp. 1722-1726 ◽  
Author(s):  
Diego Nunes Faria ◽  
Angélica Siqueira da Silva ◽  
Luciano Sindra Virtuoso ◽  
Kelany S. Nascimento ◽  
Celso Shiniti Nagano ◽  
...  

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