Partition coefficients of α-amylase in aqueous two-phase systems PEG+MgSO4·7H2O+H2O at 298K

Partitioning of caseinomacropeptide in aqueous two-phase systems

“…Thus, Blázquez et al [9] proposed the following simple linear relation to correlate protein partitioning in ATPS:…”

“…In addition, this system is easily scaled-up. ATPS could be a good alternative for a first purification step since such systems allow removal of several contaminants by a simple and low-cost process [4][5][6][7][8][9].…”

Ovomucoid partitioning in aqueous two-phase systems

“…Blázquez et al [25] encountered the same behavior for the TLL when studying the partitioning of ␣-amylase in PEG-magnesium sulfate systems. Babu et al [26] also verified that an increase in potassium phosphate concentration from 14 to 20% (mass basis) resulted in an increase of the partitioning coefficients for polyphenol oxidase and bromelain.…”

Continuous extraction of α- and β-amylases from Zea mays malt in a PEG4000/CaCl2 ATPS

“…The electrical potential effect between the phases is very important for amylase separation, it increased the purification factor (FP) in 130-fold in the salt-rich flux [1][2][3]19,21,29]. This FP value is higher than the FP value obtained by Furuya et al [4,5], Blasquez et al [6] Gu and Glatz [8] and Santana [7], showing that continuous PEG/CaCl 2 ATPS is the best system for amylase recovery. ␣ And ␤-amylases PF values were more than founds by Nirmala and Muralikrishna [22] using CPC, CCC and fractional precipitation methods, by Demirkan et al [30] using gel chromatography and CCC methods and by Aguilar et al [29] and Nguyen et al [31] gel chromatography and fractional precipitation methods.…”

“…The partition coefficients of hydrolytic enzymes, ␣-and ␤-amylases and glucoamylase, of high purity, have been determined in PEG/dextran [4,5], PEG/MgSO 4 [6] and PEG/CaCl 2 [7] batch aqueous two-phase systems (ATPS). The influence of polymer, salt and initial enzyme concentration on partition was investigated in these studies.…”