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Membrane affinity chromatography used for the separation of trypsin inhibitor
Author(s) -
Guo Wei,
Shang Zhenhua,
Yu Yinian,
Guan Yafeng,
Zhou Liangmo
Publication year - 1992
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/bmc.1130060211
Subject(s) - chemistry , trypsin , ultrafiltration (renal) , chromatography , membrane , amination , affinity chromatography , covalent bond , phase inversion , trypsin inhibitor , kunitz sti protease inhibitor , enzyme , biochemistry , organic chemistry , catalysis
Polysulphone (PS) was chemically modified by acrylation–amination and by chloromethylation‐amination, respectively. An ultrafiltration membrane of chemically modified polysulphone (CMPS) was prepared by the phase inversion method. Trypsin was then covalently bonded onto the CMPS membrane by diazotization. The activity of immobilized trypsin reaches up to 10200 U/g; 15 mg trypsin was immobilized on 1 g CMPS membrane. Separation of soybean trypsin inhibitor was carried out on the affinity membrane, yielding 6.5 mg pure trypsin inhibitor in one run. The enzyme membrane has good activity and stability.