Effect of Degree of Doneness on Conformation of Myofibrillar Proteins by Two-Dimensional Infrared Correlation Spectroscopy

Hong-bing WAN; Hai-peng LI; Yuan-hua LEI; Peng XIE; Song-shan ZHANG; Yong-hong FENG; Xuan LIU; Huan WANG; Bao-zhong SUN

doi:10.3964/j.issn.1000-0593(2021)07-2082-05

Journals >Spectroscopy and Spectral Analysis >Volume 41 >Issue 7 >Page 2082 > Article

Spectroscopy and Spectral Analysis
Vol. 41, Issue 7, 2082 (2021)

Effect of Degree of Doneness on Conformation of Myofibrillar Proteins by Two-Dimensional Infrared Correlation Spectroscopy

Hong-bing WAN^*, Hai-peng LI, Yuan-hua LEI, Peng XIE, Song-shan ZHANG, Yong-hong FENG, Xuan LIU, Huan WANG, and Bao-zhong SUN^*;

Author Affiliations

Animal Product Quality and Safety Laboratory, Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, China

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DOI: 10.3964/j.issn.1000-0593(2021)07-2082-05 Cite this Article

Hong-bing WAN, Hai-peng LI, Yuan-hua LEI, Peng XIE, Song-shan ZHANG, Yong-hong FENG, Xuan LIU, Huan WANG, Bao-zhong SUN. 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 Copy Citation Text

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Fig. 1. ATR-FTIR spectra of beef myofibrillar proteins recorded at room temperature (25 ℃)

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Fig. 2. ATR-FTIR spectra of beef myofibrillar proteins with different degrees of doneness

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Fig. 3. Second derivative spectra of myofibrillar proteins with different degrees of doneness in 1 700~1 500 cm^-1

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Fig. 4. Synchronous spectra of beef myofibrillar proteins with different degrees of doneness in the range of 1 700~1 500 cm^-1

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