Preparation and characterization of alkali-soluble collagen from pigsking shavings
Preparation and characterization of alkali-soluble collagen from pigsking shavings
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发表时间：
2009
影响因子：
0.9
通讯作者：
Shuai Zhao;M. Zhang;L. Guoying
中科院分区：
文献类型：
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作者：
Shuai Zhao;M. Zhang;L. Guoying
皮革工业排放大量含有高价值天然胶原蛋白的固体废物。本研究以脱灰后的猪皮为原料，经无水硫酸钠脱水后，对猪皮刨花进行预处理，以去除大部分的盐和脂肪。然后采用碱处理法从猪皮刨花中提取胶原蛋白。十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）和圆二色性（CD）光谱表明，碱溶性猪皮胶原蛋白（ASPC）保留了多肽链和三螺旋构象。氨基酸谱显示与特征性胶原蛋白组成无重大偏离。ASPC的变性温度和等电点均低于胃蛋白酶增溶猪皮胶原（PSPC）。扫描电子显微镜观察表明，ASPC海绵具有多孔的纤维状网络结构，且孔径随着胶原浓度的降低和胶原溶液pH值接近ASPC的pI而增大。
The leather industry discharges large quantities of solid wastes containing high-value native collagen. In this study, the pigskin shavings, generated from the shaving of pelts which had been dehydrated with anhydrous sodium sulfate after deliming, were pretreated to remove most of salt and fat. Then alkaline treatment method was used to extract collagen from the pigskin shavings. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and circular dichroism (CD) spectra revealed that the alkali-soluble pigskin collagen (ASPC) retained the polypeptide chains and triple helix conformation. The amino acid profiles showed no major deviation from the characteristic collagen composition. Both of the denaturation temperature and the isoelectric point (pI) of ASPC were lower than those of pepsin-solubilized pigskin collagen (PSPC). Scanning electron microscopy showed that ASPC sponges had porous fibrillar network structures, and the pore sizes became larger with the decrease of collagen concentrations and as the pH of the collagen solution approached the pI of ASPC.