Investigation of Structural Characteristics and Solubility Mechanism of Edible Bird Nest: A Mucin Glycoprotein

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.