Literature summary for 3.1.3.7 extracted from

Liu, Y.; Sun, M.-H.; Shao, S.-K.; Deng, G.
An affinity-based aqueous two-phase mixed micellar system and its purification of yeast 3',5'-bisphosphate nucleotidase (2017), J. Chromatogr. B, 1060, 215-220 .

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P32179	-	-

Purification (Commentary)

Purification (Comment)	Organism
aqueous two-phase micellar system (ATPMS), as an alternative liquid-liquid extraction technique, is exploited for the precise separation or large-scale concentration of biomolecules. An affinity-based ATPMS composed of mixed micelles is constructed by introducing a copper-chelated Triton X-114 (TX-Cu(II)) into an aqueous solution of hydrophobically modified ethylene oxide polymer (HMEO). The phase diagram of the HM-EO/TX-Cu(II) system is measured, and the partitioning behavior of model proteins (YND, BSA, lysozyme) is studied by using this system. The addition of HM-EO can result in formation of the micellar network in the micelle-rich phase, making the phase separation easier and stabler. In addition, the extractive performance of ATPMS is enhanced due to the existence of the mixed micelles composed by HM-EO and Cu(II)-chelated TX. The recombinant His6-tagged enzyme YND from Escherichia coli strain BL21(DE3) is selectively extracted into the micelle-rich phase, while the histidine-poor proteins (BSA and lysozyme) remain in the micelle-poor phase. Enzyme YND can be recovered from the cell lysate with a recovery yield of 49.23% and purification factor of 2.63, method, overview. And purification of the His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Saccharomyces cerevisiae

Purification (Comment)

Organism

aqueous two-phase micellar system (ATPMS), as an alternative liquid-liquid extraction technique, is exploited for the precise separation or large-scale concentration of biomolecules. An affinity-based ATPMS composed of mixed micelles is constructed by introducing a copper-chelated Triton X-114 (TX-Cu(II)) into an aqueous solution of hydrophobically modified ethylene oxide polymer (HMEO). The phase diagram of the HM-EO/TX-Cu(II) system is measured, and the partitioning behavior of model proteins (YND, BSA, lysozyme) is studied by using this system. The addition of HM-EO can result in formation of the micellar network in the micelle-rich phase, making the phase separation easier and stabler. In addition, the extractive performance of ATPMS is enhanced due to the existence of the mixed micelles composed by HM-EO and Cu(II)-chelated TX. The recombinant His6-tagged enzyme YND from Escherichia coli strain BL21(DE3) is selectively extracted into the micelle-rich phase, while the histidine-poor proteins (BSA and lysozyme) remain in the micelle-poor phase. Enzyme YND can be recovered from the cell lysate with a recovery yield of 49.23% and purification factor of 2.63, method, overview. And purification of the His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography

Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
3',5'-bisphosphate nucleotidase	-	Saccharomyces cerevisiae
Yeast 3',5'-bisphosphate nucleotidase	-	Saccharomyces cerevisiae
YND	-	Saccharomyces cerevisiae