期刊论文详细信息
JOURNAL OF CHEMICAL ENGINEERING OF JAPAN | |
Evaluation of Surface Hydrophobicities during Refolding Process of Carbonic Anhydrase Using Aqueous Two-Phase Partitioning Systems | |
Hisakazu Tanaka1  Isao Komasawa1  Koji Yano1  Ryoichi Kuboi1  | |
[1]Department of Chemical Engineering, Osaka University | |
关键词: Biochemical Engineering; Carbonic Anhydrase; Partition; Aqueous Two Phase; Protein Refolding; Hydrophobic Interaction; Molten Globule; Nonionic Detergent; Triton; | |
DOI : 10.1252/jcej.26.286 | |
来源: Maruzen Company Ltd | |
【 摘 要 】
References(15)Cited-By(14)Changes in conformational and surface properties in refolding processes were quantitatively investigated in aqueous two-phase systems, using bovine carbonic anhydrase (CAB) as a model protein. Surface net hydrophobicity (HFS) of a native CAB was determined as –84 kj·mol–1, showing a moderately hydrophilic surface. By addition of 1.5–2 M guanidine hydrochloride (GuHCl), CAB was denatured and HFS increased drastically up to about 300 kj·mol–1, accompanied by some increment of local hydrophobicity. The fully unfolded state was achieved in 5 M GuHCl. The unsteady change of local hydrophobicity during CAB refolding was also quantified using phase separation of Triton solution. Yield of CAB reactivation was enhanced by the addition of Triton X-405, due to hydrophobic interaction with hydrophobic residues exposed during the refolding process.【 授权许可】
Unknown
【 预 览 】
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RO201912080693587ZK.pdf | 749KB | download |