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Protein purification by chemo‐selective precipitation using thermoresponsive polymers
Author(s) -
Wu Yuanzi,
Cai Zhen,
Wu Shuigen,
Xiong Wenli,
Ma Shanyun
Publication year - 2018
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.23222
Subject(s) - chemistry , bioconjugation , polymer , protein purification , conjugate , bovine serum albumin , residue (chemistry) , papain , precipitation , cysteine , chromatography , lower critical solution temperature , yield (engineering) , polymer chemistry , biochemistry , organic chemistry , enzyme , copolymer , mathematical analysis , physics , materials science , mathematics , meteorology , metallurgy
A recoverable and thermoresponsive polymer‐protein bioconjugate is synthesized and employed in the purification of protein with free sulfhydryl groups. Initiator with disulphide was modified on the cysteine residue of the target protein. Poly(N‐isopropylacrylamide) exhibiting a lower critical solution temperature was grown from the protein. The resulting protein–polymer conjugate was successfully thermoprecipitated and separated from other proteins. The approach was demonstrated with bovine serum albumin with the recycling yield of 76.4%. Enzyme activity test with papain verified the reversible polymer modification protected protein under extreme environments without affecting the functionality of the protein. This study implies the favorable potential of chemo‐selective enriching and purification of proteins.