文章摘要
超声波预处理对大米蛋白酶解产物ACE抑制率的影响
Effects of ultrasound pretreatment rice protein on angiotensin-I-converting enzyme (ACE) inhibitory rate of hydrolysate
投稿时间:2016-08-06  修订日期:2016-08-06
DOI:
中文关键词: 超声波  大米蛋白  血管紧张素转化酶(ACE)抑制肽  蛋白结构
英文关键词: Ultrasound  rice protein  angiotensin converting enzyme (ACE) inhibitory peptide  protein structure
基金项目:国家自然科学基金项目(面上项目,重点项目,重大项目)
作者单位E-mail
杨雪 江苏大学食品与生物工程学院 yangxue19891012@163.com 
李云亮 江苏大学食品与生物工程学院  
王禹程 江苏大学食品与生物工程学院  
黄姗芬 江苏大学食品与生物工程学院  
马海乐 江苏大学食品与生物工程学院  
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中文摘要:
      本文研究了大米蛋白经过三频平板式超声波(Tri-frequency flat ultrasound, TFFU)设备预处理对碱性蛋白酶酶解后的大米多肽血管紧张素转换酶(angiotensin converting enzyme, ACE)抑制活性的影响。同时分别采用紫外可见分光光谱仪,傅立叶变换红外光谱仪,荧光分光光度计对超声后的大米蛋白进行了测定,探讨了超声影响酶解产物活性的机制。结果表明,三频20,28,40 kHz同步超声预处理可显著提高酶解产物的ACE抑制活性。在此超声模式条件下,大米多肽的ACE抑制率62.39%,较对照组(未经超声处理)提高了9.42%。通过超声后大米蛋白的紫外光谱,红外光谱,表面疏水性的变化表明,超声能改变蛋白的紫外吸收峰,降低蛋白二级结构中α-螺旋和β-转角的含量,同时提高β-折叠的含量。通过蛋白表面疏水性可知,超声能显著提高大米蛋白的表面疏水性。因此可以得出,超声通过影响蛋白的结构,使碱性蛋白酶更加容易与酶切位点结合,从而影响其酶解产物的ACE抑制活性。
英文摘要:
      The effect of Tri-frequency flat ultrasound (TFFU) on preparation of angiotensin converting enzyme (ACE) inhibitory peptide from rice protein using alcalase was studied. UV-visible spectrophotometer, Fourier transform infrared (FTIR) spectroscopy and fluorescence spectrophotometer were employed to investigate the mechanism of ultrasound infulencing ACE inhibitory activity. The results showed that 20, 28 and 40 kHz frequency synchronization ultrasonic pretreatment has significant influence on ACE inhibitory activity of hydrolysate. Under this condition, ACE inhibition rate were 62.39%, compared with the control group (without ultrasonic processing), and increased by 9.42%. Ultrasound can change ultraviolet absorption peak, caused unfolding of the α-helical and β-turn region, following by the formation of β-sheet. The results further showed that ultrasound exposed the hydrophobic regions, loosened the protein structure. In conclusion, ultrasound influenced the structure of rice protein, made the alcalase attact restriction sites more frequently so that the ACE inhibitory activity of hydrolysate increased.
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