Scientia Agricultura Sinica ›› 2013, Vol. 46 ›› Issue (18): 3871-3877.doi: 10.3864/j.issn.0578-1752.2013.18.017

• STORAGE·FRESH-KEEPING·PROCESSING • Previous Articles     Next Articles

Changes of the Construction of Myofibrillar Proteins in Chinese Traditional Bacon During Processing

 CAO  Jin-Xuan-1, ZHANG  Yu-Lin-1, HAN  Min-Yi-2, JIANG  Ya-Ting-1, PAN  Dao-Dong-1, 欧Chang-Rong-1   

  1. 1.Department of Food Science and Engineering, Ningbo University, Ningbo 315211, Zhejiang
    2.College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095
  • Received:2013-04-10 Online:2013-09-15 Published:2013-05-16

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Abstract: 【Objective】The objective of the study was to analyze the configuration and microenvironment changes of the myofibrillar proteins in Chinese traditional bacon at different processing points. 【Method】 Raman spectroscopy was used to analyze the changes of amide I, III belt and S-S, C-C and C-N stretching vibration bands and compare the intensity changes of I760, I850/I830, respectively. 【Result】 The content of α-helix decreased significantly accompanied by an final increase in β-sheet during the processing period, while the β-turns and random coil had no obvious change. The intensity of main chains of C-C（α-helix）and C-N stretching vibration was weaken. The intensity of native conformation of disulfide bond decreased during the processing. The normalized intensity of I760 decreased significantly after 2 days when samples were dry-cured, and then increased significantly during the drying process, while the I850/I830 ratio was a significantly decreased.【Conclusion】The main chain and secondary structure of myofibrillar proteins changed during the whole process period, but the hydrophobicity of amino acid residues was enhanced just in the drying process.

Key words: Raman spectroscopy , myo?brillar proteins , structure , Chinese traditional bacon

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