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中国精品科技期刊2020
黄丹丹, 马良, 周梦柔, 刘轶, 张宇昊. 超高压时间对胶原明胶化及成品明胶品质的影响[J]. 华体会体育, 2014, (16): 109-114. DOI: 10.13386/j.issn1002-0306.2014.16.015
引用本文: 黄丹丹, 马良, 周梦柔, 刘轶, 张宇昊. 超高压时间对胶原明胶化及成品明胶品质的影响[J]. 华体会体育, 2014, (16): 109-114. DOI: 10.13386/j.issn1002-0306.2014.16.015
HUANG Dan-dan, MA Liang, ZHOU Meng-rou, LIU Yi, ZHANG Yu-hao. Effects of pressure level on collagen gelatinizing and properties of extracted gelains[J]. Science and Technology of Food Industry, 2014, (16): 109-114. DOI: 10.13386/j.issn1002-0306.2014.16.015
Citation: HUANG Dan-dan, MA Liang, ZHOU Meng-rou, LIU Yi, ZHANG Yu-hao. Effects of pressure level on collagen gelatinizing and properties of extracted gelains[J]. Science and Technology of Food Industry, 2014, (16): 109-114. DOI: 10.13386/j.issn1002-0306.2014.16.015

超高压时间对胶原明胶化及成品明胶品质的影响

Effects of pressure level on collagen gelatinizing and properties of extracted gelains

  • 摘要: 以1%(w/v)HCl溶液为传压介质,研究不同时间(0~45min)的超高压(300MPa)处理对胶原的热稳定性及成品明胶的分子量分布、凝胶强度、流变学特性等的影响,以分析超高压时间在胶原明胶化过程中的作用及其对明胶品质的影响。结果显示:经5~45min的超高压处理的明胶化胶原的热稳定性高于传统酸处理组,但是低于未处理组(超高压时间为0min);结合前期工艺研究结果,可以发现超高压处理组胶原的热稳定性较低、明胶提取率较高,说明超高压处理能够破坏链间氢键、松散胶原三螺旋结构,有利于胶原明胶化;且超高压组明胶的亚基组分(α、β)得到很好的保留,而传统酸法明胶亚基组分相对含量很低(小于10%),超高压明胶中高分子量组分(亚基组分)使超高压明胶组明胶具有较好的胶凝特性和粘弹性能。 

     

    Abstract: The effects of ultra-high pressure (UHP) (300MPa) pretreatment on collagen gelatinizing and the quality of resultant gelatin was investigated in different times (from 0 to 45 minutes) with 1% (w/v) hydrochloric acid as transmission medium. With the study of collagen thermal stability and the finished gelatin's molecular weight distribution, viscoelastic properties and rheological properties. The results showed that the pressurized collagens were more thermostable than the one pretreated at ordinary pressure, but less than the untreated (the UHP time was 0) . While in the foregoing study, the UHP pretreatment found lower thermal stability, high extraction rate of gelatin, which showed ultra-high pressure could disrupt hydrogen bonds between chains, loose collagen triple helix collagen gelatin and contribute to gelatinizing. The pressurized collagens gelatin preserved subunit component (α, β) than the traditional method (less than 10%) , and the well-preserved subunit made the pressurized collagens owned good high pressure gelling properties and viscoelastic properties.

     

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