研究报告

热处理对燕窝蛋白凝胶-溶胶转变及即食燕窝品质的影响

  • 陈榕芬 ,
  • 张文斌
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  • (江南大学 食品科学学院,江苏 无锡,214122)
第一作者:硕士研究生(张文斌教授为通信作者,E-mail:wbzhang@jiangnan.edu.cn)

收稿日期: 2026-04-20

  修回日期: 2026-05-06

  网络出版日期: 2026-09-21

基金资助

新疆维吾尔自治区重大科技专项课题(2022A02009-4)

Effects of thermal treatment on gel-to-sol transition of edible bird’s nest proteins and quality of its instant product

  • CHEN Rongfen ,
  • ZHANG Wenbin
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  • (School of Food Science and Technology, Jiangnan University, Wuxi 214122, China)

Received date: 2026-04-20

  Revised date: 2026-05-06

  Online published: 2026-09-21

摘要

燕窝食用前需经炖煮处理,其形态结构与质地受热加工的影响显著。该研究以炖煮时间(0~120 min)为变量,探究加热过程中燕窝蛋白质的凝胶-溶胶转变与即食产品的消化特性。结果表明,炖煮至25 min时涨发率达到峰值241.38%,燕窝蛋白质受热后充分展开,β-折叠含量由48.36%增加至52.48%,丝氨酸、苏氨酸等亲水氨基酸残基结合位点暴露,通过氢键与疏水相互作用形成水合凝胶网络结构。扫描电镜显示即食燕窝表面形成均匀、密集的孔洞,使产品复水比达最大值31.37倍,质地最软。热处理30 min后凝胶电泳结果显示溶出蛋白开始聚集,40~120 min的持续加热导致肽键断裂与结构蛋白降解,从水凝胶态向液态溶胶转变,涨发率降低、即食产品复水比与硬度显著劣变。模拟胃消化证实,25 min处理组蛋白质释放量(2.62 mg/mL)及固形物残留率(10.53%)最为均衡,而长时间炖煮制备的即食燕窝消化后蛋白亚基仍维持较大分子质量,消化利用率低。该研究揭示了燕窝蛋白凝胶网络形成向多肽链热降解的溶胶化转变过程,为即食燕窝产品开发及蛋白凝胶热加工工艺提供了理论依据。

本文引用格式

陈榕芬 , 张文斌 . 热处理对燕窝蛋白凝胶-溶胶转变及即食燕窝品质的影响[J]. 食品与发酵工业, 2026 , 52(17) : 243 -252 . DOI: 10.13995/j.cnki.11-1802/ts.047012

Abstract

Edible bird's nest (EBN) requires boiling prior to consumption, and its morphology, structure and texture are significantly influenced by thermal processing.This study investigated the gel-to-sol transition of EBN proteins and the digestive properties of instant EBN as a function of boiling duration (0-120 min).The results showed that the swelling ratio reached a peak of 241.38% at 25 minutes of boiling.During this period, EBN proteins were fully unfolded, with the β-sheet content increasing from 48.36% to 52.48%.Hydrophilic binding sites (e.g., serine and threonine residues) were exposed, leading to the formation of a hydrated gel network through hydrogen bonding and hydrophobic interactions.Scanning electron microscopy revealed that the surface of instant EBN exhibited uniform and dense pores, resulting in a maximum rehydration ratio of 31.37-fold and the softest texture.After 30 minutes of heating, electrophoresis indicated the onset of protein aggregation.Continued heating from 40 to 120 minutes caused peptide bond cleavage and degradation of structural proteins, inducing a transition from a hydrogel to a liquid sol, accompanied by a decrease in the swelling ratio and significant deterioration in rehydration ratio and hardness of the instant product.Simulated gastric digestion confirmed that the 25 min treatment group exhibited the most balanced protein release (2.62 mg/mL) and solid retention (10.53%).In contrast, instant EBN prepared with prolonged boiling still maintained larger molecular weight protein subunits after digestion, indicating low digestive utilization.This study elucidates the solation process of EBN proteins from gel network formation to thermal degradation of peptide chains, providing a theoretical basis for the development of instant EBN products and the thermal processing of protein-rich gel foods.

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