Cao Jin-Xuan, Zhou Chang-Yu, Wang Ying, Sun Yang-Ying, Pan Dao-Dong
Key Laboratory of Animal Protein Food Processing Technology of Zhejiang Province, Ningbo University, Ningbo 315211, China.
Key Laboratory of Animal Protein Food Processing Technology of Zhejiang Province, Ningbo University, Ningbo 315211, China; Food Science & Nutrition Department of Nanjing Normal University, Nanjing 210097, China.
Food Chem. 2018 Feb 1;240:346-353. doi: 10.1016/j.foodchem.2017.07.068. Epub 2017 Jul 14.
To investigate the influence of oxidative modifications of G-actin on its binding ability with aroma compounds, the influence of HO treatments on G-actin structure and the absorption for alcohols and aldehydes was investigated. Raman spectroscopy and scanning electron microscopy were used to evaluate structural changes of G-actin; GC-MS was used to analyze the binding with alcohols and aldehydes. Results showed that 0-5mM HO enhanced the absorption of G-actin toward alcohols involved in the formation of hydrogen bonds by increasing α-helix and carbonyl values. 0-1mM HO caused the release of aldehydes with decreased sulfhydryl sites. 1-20mM HO increased the retention of aldehydes, due to the increased hydrophobic sites by G-actin rebuilding and aggregating. The aggregated G-actin favoured the hydrophobic interactions with aroma compounds, forming the protein-aroma compound complex, thus enhancing the resultant binding ability, as evidenced by scanning electron microscopy and GC/MS analysis.
为了研究G-肌动蛋白的氧化修饰对其与香气化合物结合能力的影响，研究了羟基自由基（HO）处理对G-肌动蛋白结构以及对醇类和醛类吸收的影响。采用拉曼光谱和扫描电子显微镜评估G-肌动蛋白的结构变化；采用气相色谱-质谱联用仪分析其与醇类和醛类的结合情况。结果表明，0-5mM的HO通过增加α-螺旋和羰基值增强了G-肌动蛋白对参与氢键形成的醇类的吸收。0-1mM的HO导致醛类释放，同时巯基位点减少。1-20mM的HO增加了醛类的保留，这是由于G-肌动蛋白重建和聚集导致疏水位点增加。聚集的G-肌动蛋白有利于与香气化合物的疏水相互作用，形成蛋白质-香气化合物复合物，从而增强了最终的结合能力，扫描电子显微镜和气相色谱/质谱分析证明了这一点。
