羽毛废弃物降解过程中表观结构与蛋白构象的变化

姚清华; 林香信; 宋永康; 林虬; 胡兵; 黄敏敏

羽毛废弃物降解过程中表观结构与蛋白构象的变化

姚清华^1,2,3,
林香信^1,2,3,
宋永康^1,2,3,,
林虬^1,2,3,
胡兵⁴,
黄敏敏^1,2,3

1.
福建省精密仪器农业测试重点实验室, 福建福州 350003;
2.
农业部农产品质量安全风险评估实验室, 福建福州 350003;
3.
福建省农业科学院中心实验室, 福建福州 350003;
4.
福建天马饲料有限公司, 福建福州 350300

基金项目:

福建省自然科学基金项目(2010J01110);福建省科技计划重大专项(2010NZ0002)

详细信息

通讯作者:
宋永康(1963-),男,高级实验师,主要从事水产动物饲料营养研究

中图分类号: S816
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- 被引次数: 0
出版历程
- 收稿日期: 2012-07-02
- 修回日期: 2012-07-25
- 刊出日期: 2012-09-30

Changes on Apparent Structure and Protein Conformation of Feather Residue in Degradation

YAO Qing-hua^1,2,3,
LIN Xiang-xin^1,2,3,
SONG Yong-kang^{1,2,3
,},
Lin Qiu^1,2,3,
Hu Bing⁴,
Huang Min-min^1,2,3

1.
Fujian Key Laboratory of Precision Measurement of Agriculture, Fuzhou, Fujian 350003, China;
2.
Laboratory of Quality and Safety Risk Assessment for Agro-products, Ministry of Agriculture, Fuzhou, Fujian 350003, China;
3.
Central Laboratory, Fujian Academy of Agricultural Sciences, Fuzhou, Fujian 350003, China;
4.
Fu jian Tianma Feed Co., Ltd., Fuzhou, Fujian 350300, China

摘要

摘要: 为研究羽毛废弃物降解机理,采用SEM和FTIR研究羽毛降解过程中表观结构与蛋白构象的变化。SEM结果表明,羽枝、羽绒与羽轴硬梗虽然表观结构不同,但具有类似的蛋白构象。对羽毛直接进行膨化处理对其表观结构并无明显影响,而先水解处理再膨化处理的羽毛结构更为蓬松、具有大量的空洞结构。FTIR结果表明,水解、膨化处理对羽毛蛋白中的共价键影响并不明显。但碱解、酶解对羽毛蛋白的化学键,尤其是二硫键具有明显的破坏作用,经碱解、酶解后羽毛样品的二硫键断裂后分别生成半胱氨磺酸盐(SO3-)的S-O和胱氨酸氧化产物磺基丙氨酸的S-O。此外,碱解会导致羽毛表面出现大量的盐类结晶。
- 羽毛废弃物 /
- 降解 /
- 表观结构 /
- 蛋白构象 /
- 电子显微镜 /
- 傅里叶红外转换光谱
Abstract: To understand the degrading mechanism of feather, the changes of feather residues on apparent structure and protein conformation in degradation were studied with Scanning Electron Microscope (SEM) and Fourier Transfer Infrared Reflectance (FTIR) techniques. SEM images showed the similarity between feather and feather rod on their protein conformation, although their apparent structures were different. Direct extrusion treatment didn't change the apparent structure of feather but resulted in void structure while treated initially with hydrolysis. The conformations of treated feathers were stable. Alkali degradation and enzymatic degradation could break off the linkage of chemical bonds for feather protein, such as breaking the disulfide bond remarkably into S-O in cysteine sulfonate and cysteic acid, which was indicated by shifting of IR absorption peak at 1075cm-1 towards 1030cm-1 and 1109cm-1. In addition, some salt crystal appeared on the surface of alkali degraded samples.
- feather waste /
- degradation /
- apparent structure /
- protein conformation /
- SEM /
- FTIR

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参考文献(4)

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