探讨肌原纤维蛋白(MP)构象变化和热降解的影响,肌浆蛋白(SP),和胶原蛋白(CO)在加热过程中对香气化合物的结合能力。使用SDS-PAGE,HPLC,和LC-MS/MS,观察到蛋白质热降解形成的肽和游离氨基酸的总浓度持续升高。表面疏水性,总巯基含量,颗粒大小,蛋白质的二级结构含量随时间发生显著变化。此外,通过气相色谱-质谱法测定蛋白质的香气结合能力。结果表明,由于蛋白质的解折叠和降解产物的积累,在加热5或10分钟的过程中结合能力增加。然而,随着长时间的加热,由于蛋白质聚集,结合能力降低。值得注意的是,所有蛋白质对(E)-2-辛烯,(E,E)-2,4-decadienal,2-甲基-3-呋喃硫醇,和二甲基三硫醚。MP和SP的结合能力相似,但与CO有显著差异,对己醛的结合能力较低,(E)-2-octenal,(E,E)-2,4-decadienal,和二甲基三硫醚与MP和SP相比。
To investigate the effects of conformational changes and thermal degradation of myofibrillar protein (MP), sarcoplasmic protein (SP), and collagen (CO) on the binding ability for aroma compounds during heating. Using SDS-PAGE, HPLC, and LC-MS/MS, a consistent rise in the total concentration of peptides and free amino acids formed by the thermal degradation of proteins was observed. The surface hydrophobicity, total sulfhydryl content, particle size, and secondary structure content of proteins changed significantly over time. Furthermore, the aroma binding ability of proteins was determined by gas chromatography-mass spectrometry. The results revealed an increase in binding ability during 5 or 10 min of heating due to protein unfolding and the accumulation of degradation products. However, the binding ability decreased due to protein aggregation with prolonged heating. Notably, all proteins exhibited strong affinity toward (E)-2-octenal, (E,E)-2,4-decadienal, 2-methyl-3-furanthiol, and dimethyl trisulfide. The binding ability of MP and SP was similar but differed significantly from that of CO, which had lower binding ability for hexanal, (E)-2-octenal, (E,E)-2,4-decadienal, and dimethyl trisulfide compared to MP and SP.