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二维红外相关光谱研究熟度对肌原纤维蛋白构象的影响
引用本文:万红兵,李海鹏,雷元华,谢鹏,张松山,丰永红,刘璇,王欢,孙宝忠. 二维红外相关光谱研究熟度对肌原纤维蛋白构象的影响[J]. 光谱学与光谱分析, 2021, 41(7): 2082-2086. DOI: 10.3964/j.issn.1000-0593(2021)07-2082-05
作者姓名:万红兵  李海鹏  雷元华  谢鹏  张松山  丰永红  刘璇  王欢  孙宝忠
作者单位:中国农业科学院北京畜牧兽医研究所/畜产品质量安全研究室,北京 100193
基金项目:国家肉牛牦牛产业技术体系项目(CARS-37),新疆自治区重点研发专项(2017B01001),河北省现代农业产业技术体系肉牛产业创新团队建设项目(HBCT2018130204)资助
摘    要:熟度是指牛排烹煮到可食用的程度,是影响牛排的适口性和消费者满意度的重要因素.肌原纤维蛋白是肌肉中一类重要的盐溶性结构蛋白群,其热凝胶特性与肉品品质密切相关.加热是使生肉变熟的关键工艺,近年来,国内外在加热过程对肌原纤维蛋白凝胶特性及其结构变化影响方面开展了广泛的研究,但在熟度对牛肉蛋白结构影响研究方面却鲜有报道.为了探...

关 键 词:熟度  肌原纤维蛋白  衰减全反射傅里叶变换红外光谱  二维红外相关光谱
收稿时间:2020-06-28

Effect of Degree of Doneness on Conformation of Myofibrillar Proteins by Two-Dimensional Infrared Correlation Spectroscopy
WAN Hong-bing,LI Hai-peng,LEI Yuan-hua,XIE Peng,ZHANG Song-shan,FENG Yong-hong,LIU Xuan,WANG Huan,SUN Bao-zhong. Effect of Degree of Doneness on Conformation of Myofibrillar Proteins by Two-Dimensional Infrared Correlation Spectroscopy[J]. Spectroscopy and Spectral Analysis, 2021, 41(7): 2082-2086. DOI: 10.3964/j.issn.1000-0593(2021)07-2082-05
Authors:WAN Hong-bing  LI Hai-peng  LEI Yuan-hua  XIE Peng  ZHANG Song-shan  FENG Yong-hong  LIU Xuan  WANG Huan  SUN Bao-zhong
Affiliation:Animal Product Quality and Safety Laboratory, Institute of Animal Science, Chinese Academy of Agricultural Sciences,Beijing 100193, China
Abstract:Degree of doneness(DOD)is an important factor affecting the palatability and consumer satisfaction of steak. Myofibrillar proteins are important structural proteins, which are closely related to meat quality. Heating is the key technology of meat processing. In recent years, there were lots of articles that reported the effects of thermal treatment on the structural properties of myofibrillar proteins, but few reports on the effects of DOD on its structure. Based on modern infrared spectroscopy, the attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR)was combined with two-dimensional correlation spectroscopy, using infrared spectroscopy, second derivative spectroscopy and two-dimensional correlation spectroscopy to track the cooking process of myofibrillar proteins dynamically. The main changes in the protein cooking process were explained by analyzing the trend and regularity of characteristic peaks. The results showed that in the range of 1 700~1 500 cm-1, DOD had a significant effect on myofibrillar proteins’ characteristic absorption peak. As the DOD increased, the intensity change of myofibrillar proteins characteristic peak was divided into three stages: the first stage was the initial stage of heating, and the intensity decreased from control to rare; the second stage was the middle stage of heating, from rare to medium. There was no significant change in peak intensity; the third stage was the late stage, from medium to over-cooked, and the peak intensity decreased significantly. The synchronous spectrum analysis results showed four autopeaks near 1 650, 1 640, 1 556, 1 540 cm-1, and the cross peaks between the two autopeaks were all positive. The autopeaks intensity analysis results showed that the medium was the turning point of the change of the protein’s temperature sensitive region. When proteins were cooked from control to medium, the amide II band was the sensitive region of myofibrillar proteins, while the sensitive region was the α-helix of amide I banded when proteins were cooked from medium to over-cooked. The information of the dynamic changes of myofibrillar proteins molecular structure caused by cooking provided a theoretical basis for the control and optimization of Western steak cooking.
Keywords:Degree of doneness  Myofibrillar proteins  Attenuated total reflectance Fourier transform infrared spectroscopy  Two-dimensional infrared correlation spectroscopy  
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