热处理对Ⅰ型胶原蛋白与肉汤香气物质结合能力的影响

doi:10.12441/spyswjs.20230128001

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热处理对Ⅰ型胶原蛋白与肉汤香气物质结合能力的影响
DOI:
                        10.12441/spyswjs.20230128001
                    
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作者单位:1.福州大学生物科学与工程学院，福建 福州350002;2.福州大学至诚学院，福建 福州 350002
作者简介:
通讯作者:刘树滔（1970—），男，博士，教授，博士研究生导师，主要从事食品营养与健康、中餐的标准化与工业化研究。E-mail： stliu@fzu.edu.cn
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基金项目:福建省科技厅引导性项目（2023N0001）；福建省大学生创新创业项目（S202213470032）。

Effects of Thermal Treatment on the Binding Ability of Type I Collagen to Aroma Compounds of Broth

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1.College of Biological Science and Engineering, Fuzhou University, Fuzhou 350002, China;2.College of Zhicheng, Fuzhou University, Fuzhou 350002, China

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目的研究胶原蛋白在煮制过程中与挥发性物质间的相互作用。方法对加热后胶原蛋白的相对分子质量、粒径、溶解度、二级结构、表面疏水性以及形成的胶原蛋白乳液的粒径进行分析，并分别探究胶原蛋白水溶液和乳液与挥发性物质的结合能力。结果随着加热时间的延长，胶原蛋白的三螺旋结构被破坏且多肽链发生降解，同时伴随着胶原蛋白表面疏水性的降低、溶解度的升高以及热聚集。胶原蛋白与挥发性物质的结合能力随着加热时间的延长而逐渐降低，并且在水溶液体系中，胶原蛋白加热4 h后反而促进挥发性物质的释放。而在乳液体系中，胶原蛋白展现出更强的结合能力，即使加热时间达到4 h后也未表现出促进挥发性物质释放的作用。结论完整的胶原蛋白三螺旋结构有利于保留更多的挥发性物质，加热时间与胶原蛋白结合挥发性物质的能力呈负相关，胶原蛋白在短时加热以及与油脂共存的情况下结合挥发性物质的能力最强。

Abstract:

Objective This study aims to reveal the interactions between collagen and volatile compounds during the cooking process.Method The relative molecular weight, particle size, solubility, secondary structure, and surface hydrophobicity of collagen and the droplet size of the collagen emulsion were studied. Furthermore, the binding ability of collagen to volatile compounds of the aqueous and emulsion systems of collagen was measured.Result As the heating time was extended, the triple-helix structure of collagen was destroyed and the polypeptide chains were degraded, which were accompanied with the decrease in surface hydrophobicity, increase in solubility, and heat-induced aggregation. The binding ability of collagen to volatile compounds gradually decreased with the extension of heating time. In the aqueous system, the release of volatile compounds was promoted after heating for 4 h. In the emulsion system, collagen exhibited a higher binding ability to volatile compounds and did not exhibit the effect of promoting release of volatile compounds even after heating for 4 h.Conclusion The triple-helix structure of collagen is beneficial to the binding to volatile compounds and the heating time has a negative correlation with the binding ability of collagen to volatile compounds. Collagen exhibits the strongest binding ability to volatile compounds in the case of short-term heating and the coexistence with lipids.

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骆晓林,袁毅,陈祥仪,刘树滔.热处理对Ⅰ型胶原蛋白与肉汤香气物质结合能力的影响[J].食品与生物技术学报,2025,(5):127-136.

LUO Xiaolin, YUAN Yi, CHEN Xiangyi, LIU Shutao. Effects of Thermal Treatment on the Binding Ability of Type I Collagen to Aroma Compounds of Broth[J]. Journal of Food Science and Biotechnology,2025,(5):127-136.

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收稿日期:2023-01-28
最后修改日期:2023-02-02
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在线发布日期: 2025-09-02
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