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試験管内酸化が筋原線維蛋白質の電荷、凝集、構造特性に及ぼす影響
Effects of in vitro oxidation on myofibrillar protein charge, aggregation, and structural characteristics.
PMID: 32615386 DOI: 10.1016/j.foodchem.2020.127396.
抄録
ヒドロキシルラジカル酸化装置を用いてインキュベートした抽出MPを用いて、豚筋原始タンパク質（MP）の等電点（pI）、凝集および構造特性に及ぼす酸化度の影響を調べた。過酸化水素濃度は0, 0.5, 1, 3, 5, 10, 20mMとした。酸化度の増加に伴い、α-ヘリックス、イオン結合、水素結合の含有量が有意に減少した（P＜0.05）。また、pI値と総アミノ酸量は減少傾向を示し、βシートと溶解度は最初に上昇し、その後減少した。逆に、ランダムカール、βターン、濁度は有意に上昇した（P<0.05）。そのため、アミノ酸側鎖基が修飾され、タンパク質の架橋や凝集につながる酸化による逆効果が、正味の負電荷などの促進効果よりも大きく、これらがタンパク質溶液系の不安定性につながる主な要因となっていることがわかりました。
The effects of oxidation degree on the isoelectric point (pI), aggregation, and structural characteristics for pork myofibrillar protein (MP) were studied by employing extracted MP, which was incubated by using a hydroxyl radical oxidation system. The concentrations of hydrogen peroxide (HO) were 0, 0.5, 1, 3, 5, 10, and 20 mM. With the increased oxidation degree, the contents of α-helix, ionic bonds, and hydrogen bonds decreased significantly (P < 0.05). Moreover, the pI value and total amino acids showed a declining trend, and the β-sheet as well as solubility rised firstly and then declined. On the contrary, random curl, β-turn, and turbidity increased significantly (P < 0.05). Therefore, amino acid side chain groups were modified, and the opposite effect, caused by oxidation that leads to protein cross-linking and aggregation, was greater than the promotion effect, such as net negative charge, these are the main factors that leads to the instability of protein solution systems.
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