Investigating the microstructure of keratin extracted from wool: Peptide sequence (MALDI-TOF/TOF) and protein conformation (FTIR)
Investigating the microstructure of keratin extracted from wool: Peptide sequence (MALDI-TOF/TOF) and protein conformation (FTIR)
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DOI：
10.1016/j.molstruc.2010.01.048
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发表时间：
2010-04-22
影响因子：
3.8
通讯作者：
Cardamone, Jeanette M.
中科院分区：
文献类型：
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作者：
Cardamone, Jeanette M.
对还原水解法和碱水解法从羊毛中提取的角蛋白进行了研究，结果表明，它们的化学组成和二级结构与原羊毛相似。角蛋白分离物在氨基酸、酰胺I和II以及二级结构方面彼此相似，并且与原始羊毛相似。从SDS-PAGE电泳中，通过还原分离的角蛋白含有分子量类似于40-60 kDa的蛋白质同系物，并且从碱水解分离的角蛋白含有类似于6-8 kDa的肽片段。MALDI-TOF/TOF光谱法证实，还原分离物含有II型微纤维组分7 C、毛发II型中间丝、I型微纤维48 kDa组分8 C-1和I型微纤维47.6kDa蛋白质同系物，其含有丙氨酸、谷氨酰胺、谷氨酸、亮氨酸、丝氨酸、亮氨酸和胱氨酸，其中谷氨酸和亮氨酸氨基酸的量最高。FTIR光谱用于检查二级结构，以确认原始羊毛的α-螺旋/β-折叠/无序区域的含量（58.2%/37.9%/3.9%）;还原角蛋白的含量（36.7%/50.2%/13.1%）;以及碱水解角蛋白的含量（25.7%/51.8%/22.5%）。较高含量的β-折叠二级结构和完整的α-螺旋构象表征了这些分离物作为可行的起始材料用于化学修饰以形成可用于工业制剂和组合物的新型仓基材料。特别是通过还原原羊毛的分子量和有用的机械性能的可能性提取的角蛋白可以转化为各种形状和形式的独立产品，如多孔泡沫，海绵，垫和膜，用于生物基，适应性结构。由爱思唯尔公司出版
Investigations of keratins extracted from wool by reduction hydrolysis and by alkaline hydrolysis showed that their chemical compositions and secondary structures were similar to original wool. The keratin isolates were similar in amino acid, Amides I and II, and secondary structure to each other and to original wool. From SDS-PAGE electrophoresis, keratin isolated by reduction contained protein homologs of molecular weight, similar to 40-60 kDa and keratin isolate from alkaline hydrolysis contained peptide fragments of similar to 6-8 kDa. MALDI-TOF/TOF spectrometry confirmed that the reduction isolate contained Type II microfibrillar component 7C, hair Type II intermediate filament, Type I microfibrillar 48 kDa component 8C-1, and Type I microfibrillar 47.6 kDa protein homologs which contained alanine, glutamine, glutamic acid, leucine, serine, leucine, and cystine with highest amounts glutamic acid and leucine amino acids. FTIR spectroscopy was applied to examine secondary structure to confirm the content of alpha-helix/beta-sheet/disordered regions for original wool (58.2%/37.9%/3.9%); keratin from reduction (36.7%/50.2%/13.1%); and keratin from alkaline hydrolysis (25.7%/51.8%/22.5%). The higher content of beta-sheet secondary structure and intact alpha-helical conformation characterized these isolates as viable starting materials for chemical modification to form novel bin-based materials useful in industrial formulations and compositions. In particular keratin extracted by reduction with the molecular weight of original wool and the probability of useful mechanical properties can be transformed into stand-alone products of various shapes and forms such as porous foams, sponges, mats, and films for bio-based, adaptable structures. Published by Elsevier B.V.