Binding of aroma compounds with myofibrillar proteins modified by a hydroxyl-radical-induced oxidative system.
Binding of aroma compounds with myofibrillar proteins modified by a hydroxyl-radical-induced oxidative system.
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DOI：
10.1021/jf502540p
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发表时间：
2014-09
影响因子：
6.1
通讯作者：
Feibai Zhou;Mouming Zhao;G. Su;Weizheng Sun
中科院分区：
文献类型：
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作者：
Feibai Zhou;Mouming Zhao;G. Su;Weizheng Sun
本研究的目的是研究氧化诱导的肌纤维蛋白结构改变对其与芳香化合物（如2-甲基丁醛、甲基丁醛、2-戊酮、2-庚酮和壬醛）结合能力的影响。采用固相微萃取法（SPME）结合气相色谱/质谱法（GC/MS）测定其结合能力。发现与香气化合物的结合受到蛋白质氧化水平的强烈影响，可能是由于蛋白质结构和表面的不同修饰。与1 mM左右或以下的氧化剂孵育主要引起蛋白质结构的重新折叠，加速蛋白质聚集，从而降低香气化合物的亲和力，从而降低其结合能力。然而，用超过2.5 mM的氧化剂处理会导致蛋白质重新聚集和部分降解，从而导致蛋白质表面性质的后续修饰。荧光猝灭和SPME-GC/MS分析表明，聚集在一起的皱褶表面的蛋白质有利于与芳香化合物的疏水相互作用，形成蛋白质-芳香化合物复合物，从而增强了结合能力。
The objective of this study was to investigate the influence of oxidation-induced structural modifications of myofibrillar protein on its binding ability with aroma compounds such as 2-methyl-butanal, methional, 2-pentanone, 2-heptanone, and nonanal. A method using solid-phase microextraction (SPME) combined with gas chromatography/mass spectrometry (GC/MS) was used to determine the corresponding binding ability. The binding with aroma compounds was found to be strongly affected by the oxidation levels of proteins, probably due to the varying modifications in protein structure and surface. Incubation with oxidants around or below 1 mM mainly caused the refolding of protein structure and accelerated the protein aggregation, which reduced the affinity of the aroma compounds, thus decreasing the binding ability. Nevertheless, treatment with oxidants over 2.5 mM would cause protein reaggregation and partial degradation, and thus, the subsequent modification of protein surface properties. The aggregated protein with wrinkled surfaces favored the hydrophobic interactions with aroma compounds, forming the protein-aroma compound complex, thus enhancing the resultant binding ability as evidenced by fluorescence quenching and SPME-GC/MS analysis.