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Paper Information

Journal:   JOURNAL OF SCIENCES ISLAMIC REPUBLIC OF IRAN   FALL 2009 , Volume 20 , Number 4; Page(s) 311 To 317.
 
Paper: 

COMPARISON BETWEEN POLYVINYL PYRROLIDONE/ NA2SO4 AQUEOUS TWO-PHASE SYSTEMS AND CHROMATOGRAPHIC METHODS FOR PURIFICATION OF RECOMBINANT PHENYLALANINE DEHYDROGENASE

 
 
Author(s):  SHAHBAZ MOHAMMADI H., OMIDINIA E.*
 
* DEPARTMENT OF BIOCHEMISTRY, PASTEUR INSTITUTE OF IRAN, TEHRAN, ISLAMIC REPUBLIC OF IRAN
 
Abstract: 

Phenylalanine dehydrogenase (PheDH; EC 1.4.1.20) is an important enzyme of amino acid dehydrogenases family that increasingly used as a valuable biocatalyst in neonatal screening kits and synthesis of L-phenylalanine. The goal of this literature was to find a suitable purification method for recombinant Bacillus badius PheDH by practical comparison between chromatographic and polyvinyl pyrrolidone (PVP)/Na2SO4 aqueous two-phase systems (ATPS) techniques. The partitioning behavior of target enzyme in PVP/Na2SO4 ATPS was examined and compared with the obtained results from a chromatographic protocol. Direct comparison of chromatography and ATPS procedures clearly revealed that the ATPS consisting of 8.0% (w/w) PVP, 17.0% (w/w) Na2SO4 with pH of 8.0, VR=0.25 and temperature of 25oC was the most desirable process for PheDH purification. A specific activity of 1231.42 U/mg, a purification factor of 36.61, a ield of 95.5% and a recovery of 138.9% were achieved. Altogether, we presented a two-phase methodology as a scalable and economically alternative for the production of PheDH enzyme.

 
Keyword(s): COMPARISON, NA2SO4, PURIFICATION, PHENYLALANINE DEHYDROGENASE (PHEDH), POLYVINYL PYRROLIDONE (PVP)
 
References: 
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