Evaluation of the surface hydrophobicities of proteins using aqueous two-phase partitioning systems and application to the separation process.

YANO Koji, WAKAYAMA Akihiro, KUBOI Ryoichi, KOMASAWA Isao

doi:10.2116/bunsekikagaku.42.11_673

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Other Title

水性二相分配法によるタンパク質の表面疎水性の評価と疎水性差に基づく分離
スイセイ 2ソウブンパイホウニヨルタンパクシツノヒョウメンソスイ
水性二相分配法によるタンパク質の表面疎水性の評価と疎水性差に基づく分離(<特集>:分離(その1))(抽出・吸着分離)

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A systematic investigation of the surface hydrophobicity of proteins was carried out. Hydrophobicity can be classified into at least two groups: one is the surface net hydrophobicity, which can be quantified by examining the partition behavior of various proteins with differing properties in polyethylene glycol (PEG)/dextran (Dex) systems; the other is the local hydrophobicity originating from the hydrophobic binding site on the surface, and can be evaluated from the increment in the partition coefficient of proteins in PEG/Dex caused by a nonionic surfactant, Triton. Some of the proteins examined were lipase, α-chymotrypsin and cytochrome c. Each protein has its own characteristic hydrophobic nature depending on both its conformational change and the interaction with its environment. These hydrophobicity differences can be systematically exploited in order to achieve an effective separation. As a case study, the separation of α-lactalbumin and β-lactoglobulin, the major proteins in cheese whey, was examined. A highly effective separation was achieved by an enlarged difference in the local hydrophobicities of the apo-proteins formed by removing calcium ion using EDTA.

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BUNSEKI KAGAKU

BUNSEKI KAGAKU 42 (11), 673-679, 1993

The Japan Society for Analytical Chemistry

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