食品与发酵工业

应用差示扫描量热法测定胶原蛋白热滞活性

  • 朱玉兵 ,
  • 曹慧 ,
  • 徐斐 ,
  • 于劲松
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网络出版日期: 2013-10-25

Differential scanning calorimetry studies on the thermal hysteresis activity of collagen

  • ZHU Yu-bing ,
  • CAO Hui ,
  • XU Fei ,
  • YU Jin-song
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Online published: 2013-10-25

摘要

采用酶法从猪皮中制备胶原蛋白,并对其纯度进行了鉴定。在此基础上,利用差示扫描量热法对制备的胶原蛋白进行热滞活性的测定,考察了保留温度(-0.18、-0.088、0.013、0.13、0.23℃)、胶原蛋白浓度(0.1、0.5、1、2.5、5、10、15、20、50 mg/ml)及升降温速率(0.5、1、2.5、5、10℃/min)对热滞活性的影响。结果表明:所制备猪皮胶原蛋白为典型的Ⅰ型胶原蛋白,纯度较高,其分子量约为330 kD;当胶原蛋白浓度为20 mg/mL,保留温度为0.12℃,升降温速率为10℃/min时胶原蛋白热滞活性最高,为0.61℃。测定胶原蛋白热滞活性时保留温度的选取至关重要,而升降温速率对热滞活性无显著影响。

本文引用格式

朱玉兵 , 曹慧 , 徐斐 , 于劲松 . 应用差示扫描量热法测定胶原蛋白热滞活性[J]. 食品与发酵工业, 2013 , 39(10) : 63 -68 . DOI: 10.13995/j.cnki.11-1802/ts.2013.10.028

Abstract

Collagen was prepared from the pigskin using enzyme method,and its purity was detected by SDSPAGE. Then,differential scanning calorimetry( DSC) was used to study the influence of holding temperature(- 0.6,- 0. 5,- 0. 4,- 0. 3,- 0. 2℃),collagen concentrations( 0. 1,0. 5,1,2. 5,5,10,15,20,50 mg / mL) and rate( 0. 5,1,2. 5,5,10℃ / min) on the thermal hysteresis activity( THA). The results suggested that the prepared pigskin collagen was a typical type I collagen and the molecular weight of collagen was about 330 KD with higher purity. A maximum THA of 0. 61℃ can be obtained with the protein concentration of 20 mg / ml,holding temperature of0. 12℃ and the heating and cooling rate of 10℃ / min. The choice of holding temperature was critical for effective measurement of THA,while the heating and cooling rates had almost no impact on the THA.
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