Adibzadeh Nasim, Aminzadeh Saeed, Jamili Shahla, Karkhane Ali Asghar, Farrokhi Naser
Department of Animal and Marine Biotechnology, National Institute of Genetic Engineering and Biotechnology (NIGEB), P.O. Box: 14965/161, Sharek-e Pajoohesh Km 15, Tehran-Karaj Highway, Tehran, Iran.
Appl Biochem Biotechnol. 2014 May;173(1):143-54. doi: 10.1007/s12010-014-0823-4. Epub 2014 Mar 28.
Pepsin-solubilized collagen (PSC) was extracted from the skin of sea cucumber Holothuria parva and was fractionally characterized. The PSC from H. parva skin consisted of three α1 chains (α1)3, in contrast to calf skin collagen type I with two α1 and one α2 chains (α1)2α2 with approximately 130 kDa each. The maximum transition (Tm) and denaturation temperature (Td) of PSC were determined to be 46.94 and 32.5 °C, respectively. The amino acid composition analysis revealed that glycine, proline, alanine, and hydroxyproline were the abundant amino acids available in extracted PSC. The results showed that the isolated collagen from H. parva has some similar characteristics to previously reported collagens used in food and pharmaceutical industries.
胃蛋白酶可溶胶原蛋白(PSC)从糙海参的皮肤中提取并进行了分级表征。与小牛皮肤I型胶原蛋白(由两条α1链和一条α2链组成,即(α1)2α2,每条链约130 kDa)不同,糙海参皮肤中的PSC由三条α1链组成,即(α1)3 。PSC的最大转变温度(Tm)和变性温度(Td)分别测定为46.94℃和32.5℃。氨基酸组成分析表明,甘氨酸、脯氨酸、丙氨酸和羟脯氨酸是提取的PSC中含量丰富的氨基酸。结果表明,从糙海参中分离出的胶原蛋白与食品和制药行业先前报道的胶原蛋白具有一些相似的特性。