Effect of aging treatment on the physicochemical properties of collagen films

被引:65
|
作者
Shi, Donghui [1 ,2 ]
Liu, Fei [1 ,2 ]
Yu, Zhe [1 ,2 ]
Chang, Bingyu [1 ,2 ]
Goff, H. Douglas [3 ]
Zhong, Fang [1 ,2 ]
机构
[1] Jiangnan Univ, State Key Lab Food Sci & Technol, Wuxi 214122, Peoples R China
[2] Jiangnan Univ, Sch Food Sci & Technol, Wuxi 214122, Peoples R China
[3] Univ Guelph, Dept Food Sci, Guelph, ON N1G 2W1, Canada
基金
国家重点研发计划; 中国博士后科学基金; 中国国家自然科学基金;
关键词
Collagen films; Aging treatment; Mechanical properties; Thermal properties; Triple helix structures; HEAT-MOISTURE TREATMENT; MECHANICAL-PROPERTIES; GELATIN FILMS; CROSS-LINKING; PHYSICAL-PROPERTIES; DRYING TEMPERATURE; YOUNGS MODULUS; EDIBLE FILMS; STABILITY; PROTEIN;
D O I
10.1016/j.foodhyd.2018.08.016
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Aging treatment was used as a safe and green physical crosslinking method to successfully improve the physicochemical properties of collagen casing films. The aging treatment increased the Young's modulus (YM) of dry, wet, and boiled collagen films, as well as the tensile strength (TS) of wet and boiled collagen films to some extent. However, the highest aging temperature (80 degrees C) together with the higher relative humidity (RH) values (70% and 80%) led to the decreases in YM and TS and increases in elongation at break (EB). The aging treatment also improved the cooking performance of collagen films, like water absorption and shrinkage in boiling water, where the water absorption decreased to the range of 185%-102% and the shrinkage decreased to the range of 41.5%-21.5%. Collagen films after aging treatment had higher moisture contents than that of control film, and their moisture contents increased with increasing aging time and RH value. The thermal properties of collagen films was improved only at lower temperatures (< 130 degrees C) by aging treatment as shown from the thermogravimetric analysis results. Furthermore, the aging treatment did not significantly affect the chemical composition of collagen films but caused the denaturation of collagen triple helix structures at different degrees according to fourier transformation infrared spectroscopy, x-ray diffraction pattern, and differential scanning calorimetry analyses.
引用
收藏
页码:436 / 447
页数:12
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