食品科学

• 基础研究 • 上一篇    下一篇

不同来源胶原蛋白抗冻活性的研究

阮功成,曹 慧*,徐 斐,于劲松   

  1. 上海理工大学医疗器械与食品学院,上海 200093
  • 出版日期:2014-09-15 发布日期:2014-09-12

Antifreeze Activity of Collagens from Different Sources

NGUYEN Cong Thanh, CAO Hui*, XU Fei, YU Jin-song   

  1. School of Medical Instruments and Food Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China
  • Online:2014-09-15 Published:2014-09-12

摘要:

采用酶法制备不同来源的胶原蛋白,并对其纯度及氨基酸组成进行鉴定。在此基础上,利用差示扫描量热仪及低温显微镜对其热滞活性(thermal hysteresis activity,THA)和重结晶抑制效应(ice recrystallizationinhibition,IRI)进行了研究。结果表明:所制备的胶原蛋白均为典型的Ⅰ型胶原,纯度较高,其分子质量约为330 kD;相比于牛血清白蛋白,不同来源的胶原蛋白中,猪皮胶原具有较高的热滞活性,即当保留温度为-0.2 ℃,体系冰晶含量φ≤5% 时,THA为0.52 ℃;在猪皮胶原蛋白体系中形成的冰晶为不规则的圆球形,不易对细胞及组织造成伤害,且经过一次循环后,冰晶无显著增大。

关键词: 抗冻活性, 胶原蛋白, 热滞活性, 重结晶抑制效应

Abstract:

In this study, collagens from different sources were prepared by means of enzymatic hydrolysis, and their purity
and amino acid composition were identified. Differential scanning calorimetry (DSC) was used to determine the thermal
hysteresis activity (THA), and the ice recrystallization inhibition (IRI) was evaluated by cryomicroscopy. The results
showed that all the collagens prepared were typical type I collagen with high purity and molecular weight of about 330 kD.
The collagens from different sources had common amino acid composition with glycine, proline and alanine as the most
abundant amino acids. Compared with bovine serum albumin (BSA), the T0 of pig skin collagen revealed a higher THA value
(0.52 ℃), and the ice crystal content φ was equal to or less than 5% at a retention temperature Th of -0.2 ℃. As observed
under a microscope, pig skin collagen extracts formed a large number of hexagonal ice crystal, demonstrating the antifreeze
activity when compared with chicken skin collagen and fish skin collagen.

Key words: antifreeze activity, collagen, thermal hysteresis activity, ice recrystallization inhibition

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