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• W2034387587 abstract "Purification of a recombinant, thermostable α-amylase (MJA1) from the hyperthermophile, Methanococcus jannaschii, was investigated in the ethylene oxide–propylene oxide random copolymer (PEO–PPO)/(NH4)2SO4, and poly(ethylene glycol) (PEG)/(NH4)2SO4 aqueous two-phase systems. MJA1 partitioned in the top polymer-rich phase, while the remainder of proteins partitioned in the bottom salt-rich phase. It was found that enzyme recovery of up to 90% with a purification factor of 3.31 was achieved using a single aqueous two-phase extraction step. In addition, the partition behavior of pure amyloglucosidase in polymer/salt aqueous two-phase systems was also evaluated. All of the studied enzymes partitioned unevenly in these polymer/salt systems. This work is the first reported application of thermoseparating polymer aqueous two-phase systems for the purification of extremophile enzymes." @default.
• W2034387587 created "2016-06-24" @default.
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• W2034387587 date "2004-07-25" @default.
• W2034387587 modified "2023-09-25" @default.
• W2034387587 title "Purification of hyperthermophilic archaeal amylolytic enzyme (MJA1) using thermoseparating aqueous two-phase systems" @default.
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• W2034387587 doi "https://doi.org/10.1016/j.jchromb.2004.03.030" @default.
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