The use of Fourier transform-infrared (FTIR) and Raman spectroscopy (FTR) for the investigation of structural changes in wool fibre keratin after enzymatic treatment
The use of Fourier transform-infrared (FTIR) and Raman spectroscopy (FTR) for the investigation of structural changes in wool fibre keratin after enzymatic treatment
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DOI：
10.1016/j.molstruc.2004.03.044
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发表时间：
2004-10-18
影响因子：
3.8
通讯作者：
Weselucha-Birczynska, A
中科院分区：
文献类型：
--
作者：
Wojciechowska, E;Rom, M;Weselucha-Birczynska, A
在缓冲条件下用蛋白水解酶处理从波兰美利奴羊获得的羊毛纤维的角蛋白。在酶促攻击之前，使用原硅酸作为预处理。研究表明，缓冲环境对羊毛纤维角蛋白结构的变化有显着影响。根据所用缓冲液的类型，观察到不同的构象变化。使用氨和四硼酸盐缓冲液（pH = 8.2 内）。所使用的每种缓冲剂对羊毛纤维角蛋白结构的变化都有不同的影响。氨缓冲液引起二硫键区域更大的构象变化，而四硼酸盐缓冲液破坏了酰胺组分的稳定性。采用红外光谱和拉曼光谱来评估羊毛角蛋白结构的变化。 (C) 2004 Elsevier B.V. 保留所有权利。
Keratin of wool fibres obtained from Polish Merino Sheep was treated with proteolytic enzyme in buffered conditions. The zoll of orthosilicic acid was applied as a pretreatment, before enzymatic attack. It has been shown that buffer environment has significant influence on the changes in the structure of wool fibre keratin. Depending of the type of buffer utilised, different conformational changes are observed. Ammonia and tetraborate buffers were used (within pH = 8.2). Each of the used buffers had a different influence on the changes in the structure of wool fibre keratin. Ammonia buffer caused bigger conformational changes in the region of disulphide bonds while tetraborate buffer disrupted the stability of amide components. To evaluate the changes of wool keratin structure infrared spectroscopy and Raman spectroscopy were applied. (C) 2004 Elsevier B.V. All rights reserved.