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| 脉冲超声波对黄粉虫幼虫水溶性蛋白结构的影响 | |
| 引用本文： | 代春华,汤坚,顾小红,马海乐.脉冲超声波对黄粉虫幼虫水溶性蛋白结构的影响[J].江苏大学学报(自然科学版),2012,33(2):130-133,186. |
| 作者姓名： | 代春华 汤坚 顾小红 马海乐 |
| 作者单位： | 1. 江苏大学食品与生物工程学院,江苏镇江212013;江南大学食品科学与技术国家重点实验室,江苏无锡214122 2. 江南大学食品科学与技术国家重点实验室,江苏无锡,214122 3. 江苏大学食品与生物工程学院,江苏镇江,212013 |
| 基金项目： | 国家“863”计划项目(2007AA10Z321) |
| 摘 要： | 采用功率1 000 W的脉冲超声波处理黄粉虫幼虫水溶性蛋白,并对蛋白的结构变化进行研究.结果表明:在脉冲超声波处理时间25 min内,蛋白的紫外吸收随着处理时间的延长而增强;蛋白的表面疏水性在处理10 min时达到最大,随后逐渐降低;游离巯基的含量在脉冲超声波处理5min时稍有降低,随后逐渐增加;蛋白粒径随着处理时间的延长而减小,当处理时间达到20 min时,粒径显著增大;蛋白二级结构中α-螺旋的含量降低,β-链及无规则卷曲的含量升高;脉冲超声波处理后蛋白的变性聚丙烯酰胺凝胶电泳图谱未发生改变,表明蛋白的一级结构未受到影响. |
| 关 键 词： | 脉冲 超声波 黄粉虫幼虫 水溶性蛋白 结构 |
Influence of pulse ultrasonic on water soluble protein conformation of Tenebrio molitor( L.) larva |
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| Dai Chunhua , Tang Jian , Gu Xiaohong , Ma Haile.Influence of pulse ultrasonic on water soluble protein conformation of Tenebrio molitor( L.) larva[J].Journal of Jiangsu University:Natural Science Edition,2012,33(2):130-133,186. | |
| Authors: | Dai Chunhua Tang Jian Gu Xiaohong Ma Haile |
| Institution: | 1(1.School of Food and Biological Engineering,Jiangsu University,Zhenjiang,Jiangsu 212013,China;2.State Key Laboratory of Food Science and Technology,Jiangnan University,Wuxi,Jiangsu 214122,China) |
| Abstract: | The effects of pulse ultrasonic treatment with power of 1 000 W on water soluble protein conformation of Tenebrio molitor(L.) larva were investigated.The results show that the ultraviolet absorption of protein is increased within 25 min ultrasonic treatment.The surface hydrophobicity has remarkable change with maximum value at 10 min,and decreases gradually from 10 to 25 min.The free sulfhydryl(SH) content decreases slightly after pulse ultrasonic treatment for 5 min,and then increases gently.Protein particle size decreases with treatment time from 0 to 15 min,and increases significantly after 20 min treatment.The CD analysis indicates that α-helix content is decreased,while β-structure and random coil content are increased by pulse ultrasonic treatment.SDS-PAGE demonstrates that the primary structure of water soluble protein is not changed by pulse ultrasonic treatment. |
| Keywords: | pulse ultrasonic larva of Tenebrio molitor(L ) water soluble protein conformation |
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