| 摘要: |
| 利用酸溶法和酶溶法制备马面鲀鱼头酸溶性胶原蛋白(ASC)和酶溶性胶原蛋白(PSC), 并对所制备的ASC 和PSC 的氨基酸组成、SDS-PAGE、红外光谱、黏度和热变性温度, 以及溶解度等性质进行分析。结果表明: 马面鲀鱼头中ASC 和PSC 的提取率分别为0.94% ± 0.07%和3.91% ± 0.14%。Gly(265.0 和251.8 残基/1000 残基)、Ala(111.0 和107.6 残基/1000 残基)和Pro(87.0 和83.1 残基/1000残基)含量较高, 而His 和Tyr 的含量较少, 且未检测到Cys。ASC 和PSC 中亚氨基酸(Pro 和Hyp)含量为169.3 和160.6 残基/1000 残基。氨基酸组成分析、SDS-PAGE 和红外光谱(FTIR)证实ASC 和PSC 均属于I 型胶原蛋白, 热变性温度分别为17.6 ℃ 和16.5 ℃。在酸性pH 值范围内, ASC 和 PSC的溶解度较高; 当NaCl 溶液浓度高于2%, ASC 和 PSC 的溶解度会显著降低。综上, 相对于哺乳动物类胶原蛋白, 马面鲀鱼头ASC 和PSC 的亚氨基酸含量和热变性温度较低, 结构稳定性差, 易于降解, 可作为胶原蛋白肽的制备原料进行开发。 |
| 关键词: 马面鲀 鱼头 酸溶性胶原蛋白 酶溶性胶原蛋白 |
| DOI：10.11693/hyhz20150100016 |
| 分类号: |
| 基金项目:浙江省科技厅公益信息技术研究社会发展项目, 2014C33034 号; 浙江省科技厅重大科技专项社会发展项目, 2011C02003 号;浙江省教育厅项目, Y201225031 号。 |
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| ISOLATION AND CHARACTERIZATION OF ACID AND PEPSIN SOLUBLE COLLAGENS FROM THE HEAD OF BLUEFIN LEATHERJACKET (NAVODON SEPTENTRIONALIS) |
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ZHAO Yu-Qin1, WANG Yu-Mei1, WANG Bin1, CHI Chang-Feng2, DING Guo-Fang1
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1.School of Food and Pharmacy, Zhejiang Provincial Key Engineering Technology Research Center of Marine Biomedical Products, Zhejiang Ocean University, Zhoushan 316022, China;2.School of Marine Science and Technology, National Engineering Research Center of Marine Facilities Aquaculture, Zhejiang Ocean University, Zhoushan 316022, China
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| Abstract: |
| Every year about 100000 tons of by-product are wasted in food industry in processing bluefin leatherjacket (Navodon septentrionalis) in China. To make more effective use of the wastes, acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the head of bluefin leatherjacket were extracted, and their properties were determined by using amino acid analysis, SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel), and FTIR (Fourier transform infrared) technologies. The yields of ASC and PSC were 0.94% ± 0.07% and 3.91% ± 0.14% (on wet weight basis), respectively. ASC and PSC contained glycine (265.0 and 251.8 residues/1000 residues) as the major amino acid and the contents of imino acids were 169.3 and 160.6 residues/1000 residues, respectively. Amino acid composition, SDS-PAGE, and FTIR confirmed that ASC and PSC were mainly composed of type I collagen with slight differences in molecular structure. The denaturation temperatures (Td) of ASC and PSC were 17.6 ℃ and 16.5 ℃, much lower than those of mammalian and tropical fish species due to low imino acid contents. Therefore, the collagen helices of ASC and PSC might be less stable than those of mammalian because of lower imino acid contents and Td. All the collagens were soluble at acidic pH (1—4) and their solubility became low in NaCl concentration above 2% (W/V). Therefore, the isolated collagens from the bluefin leatherjacket head could be utilized as a substitute to mammalian collagen in the preparation of peptides. |
| Key words: bluefin leatherjacket (Navodon septentrionalis) fish head acid soluble collagen (ASC) pepsin soluble collagen (PSC) |
