Lv Yating, Xu Feifei, Liu Fei, Chen Maoshen
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
Science Center for Future Foods, Jiangnan University, Wuxi 214122, China.
Foods. 2023 Feb 5;12(4):688. doi: 10.3390/foods12040688.
In this study, the possible solubility properties and water-holding capacity mechanism of edible bird nest (EBN) were investigated through a structural analysis of soluble and insoluble fractions. The protein solubility and the water-holding swelling multiple increased from 2.55% to 31.52% and 3.83 to 14.00, respectively, with the heat temperature increase from 40 °C to 100 °C. It was observed that the solubility of high-Mw protein increased through heat treatment; meanwhile, part of the low-Mw fragments was estimated to aggregate to high-Mw protein with the hydrophobic interactions and disulfide bonds. The increased crystallinity of the insoluble fraction from 39.50% to 47.81% also contributed to the higher solubility and stronger water-holding capacity. Furthermore, the hydrophobic interactions, hydrogen bonds, and disulfide bonds in EBN were analyzed and the results showed that hydrogen bonds with burial polar group made a favorable contribution to the protein solubility. Therefore, the crystallization area degradation under high temperature with hydrogen bonds and disulfide bonds may be the main reasons underlying the solubility properties and water-holding capacity of EBN.
在本研究中，通过对可溶和不溶部分的结构分析，研究了食用燕窝（EBN）可能的溶解性和持水能力机制。随着加热温度从40℃升高到100℃，蛋白质溶解度和持水膨胀倍数分别从2.55%增加到31.52%，从3.83增加到14.00。观察到通过热处理，高分子量蛋白质的溶解度增加；同时，估计部分低分子量片段通过疏水相互作用和二硫键聚集形成高分子量蛋白质。不溶部分的结晶度从39.50%增加到47.81%，这也有助于提高溶解度和增强持水能力。此外，对EBN中的疏水相互作用、氢键和二硫键进行了分析，结果表明，具有埋藏极性基团的氢键对蛋白质溶解度有有利贡献。因此，高温下氢键和二硫键导致的结晶区域降解可能是EBN溶解性和持水能力的主要原因。
