腊肉加工过程中肌原纤维蛋白结构的变化

doi:10.3864/j.issn.0578-1752.2013.18.017

摘要/Abstract

摘要： 【目的】解析肌原纤维蛋白在腊肉加工过程中主链构象及微环境的变化。【方法】运用拉曼光谱，对酰胺Ⅰ、Ⅲ带及S-S、C-C、C-N伸缩振动谱带进行分析，比较I760、 I850/I830的强度变化。【结果】在加工过程中，肌原纤维蛋白α-螺旋的含量显著下降，β-折叠的最终含量显著增加，β-转角及无规则卷曲含量无明显变化，主链C-C的α-螺旋及C-N伸缩振动强度减弱，二硫键天然构象的谱带强度也显著下降；I760归一化强度在干腌2 d后显著降低，而后在风干过程中又显著上升，I850/I830的比值在同时期显著下降。【结论】肌原纤维蛋白的主链及二级结构在整个加工过程中发生了变化，氨基酸残基的疏水性在风干过程中得到了增强。

关键词: 拉曼光谱 , 肌原纤维蛋白 , 构型 , 腊肉

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

曹锦轩1, 张玉林1, 韩敏义2, 蒋亚婷1, 潘道东1, 欧昌荣1. 腊肉加工过程中肌原纤维蛋白结构的变化[J]. 中国农业科学, 2013, 46(18): 3871-3877.

CAO Jin-Xuan-1, ZHANG Yu-Lin-1, HAN Min-Yi-2, JIANG Ya-Ting-1, PAN Dao-Dong-1, 欧Chang-Rong-1 . Changes of the Construction of Myofibrillar Proteins in Chinese Traditional Bacon During Processing[J]. Scientia Agricultura Sinica, 2013, 46(18): 3871-3877.

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