为了弄清热处理时间对肌原纤维蛋白凝胶的风味吸附能力影响，本文建立了肌原纤维蛋白与几类常见的肉类挥发性风味化合物（醇类、醛类、酮类、酯类）相互作用体系，研究了80 ℃ 热处理0~20 min过程中肌原纤维蛋白凝胶表面疏水性、二级结构、风味吸附能力的变化。结果表明，肌原纤维蛋白凝胶风味吸附能力的改变主要集中在加热0~5 min，在该时段内，肌原纤维蛋白凝胶对戊醇、己醇、2-丁酮、2-庚酮及乙酸乙酯的吸附能力显著增强（p<0.05）；其表面疏水性显著升高（p <0.05），α-螺旋结构相对含量从37.48%降至33.44%（p <0.05），β-折叠结构由31.15%增至36.26%（p <0.05），β-转角结构由20.54%降低至15.52%（p <0.05），无规则卷曲16.12%降低至14.78%。热处理导致肌原纤维蛋白凝胶风味吸附能力的改变可能是由于其使得疏水基团暴露、二级结构发生了改变。

In this study, to understand the effect of heat treatment time on the absorption capacity of myofibrillar protein gel on flavor compounds, a myofibrillar protein gel-flavor compound (alcohols, aldehydes, ketones, and esters) interaction system was established, and the changes in the surface hydrophobicity, secondary structure, and absorption capacity of myofibrillar protein gels during the heat treatment at 80?C for 20 min were studied. The results showed that the changes in the absorption capacity of myofibrillar protein gels mainly occurred during the first five minutes of the heat treatment. During this period, the absorption capacities of myofibrillar protein gels on amyl alcohol, hexanol, 2-butanone, 2-heptanone, and ethyl acetate significantly increased (P < 0.05) and the surface hydrophobicity of myofibrillar protein gels markedly increased (P < 0.05). The relative content of α-helix structure decreased significantly (P < 0.05) from 37.48 to 33.44%. The relative content of β- sheet and random coil structure was significantly reduced from 20.54 and 16.12% to 15.52 and 14.78%, respectively (P < 0.05). However, the relative content of β-turn structure increased significantly (P < 0.05) from 31.15 to 36.26% and the content of random coil decreased from 16.12% to 14.78%. The changes in the absorption capacity of myofibrillar protein gels are likely due to the changes in the secondary structures and the exposure of hydrophobic groups by heat treatment.

国家自然科学基金资助项目（31471681）；宁波市创新团队（2012B82017）；国家农业科技成果转化资金项目（2013GB2C200191）；现代农业产业技术体系（CARS-43-17）