刊期:双月刊
主管单位:中国科学院
主办单位:中国科学院动物研究所,中国昆虫学会
地址:北京市朝阳区北辰西路1号院5号中国科学院动物研究所
邮编:100101
电话:010-64807137
传真:010-64807137
E-Mail:entom@ioz.ac.cn
刊号:ISSN 2095-1353
        CN 11-6020/Q
国内发行代号:2-151
国际发行代号:BM-407
发行范围:国内外公开发布
定价:138元/册
定价:828元/年
银行汇款:中国工商银行北京海淀西区支行
户名:中国科学院动物研究所
帐号:0200 0045 0908 8125 063

您所在位置:首页->过刊浏览->2026年63卷第2期



麦蛾柔茧蜂副产物茧丝的结构与性能研究
Structural and functional characterization of the cocoon silk of Habrobracon hebetor (Hymenoptera: Braconidae)
胡 蝶* 黄廷莉 李小雨 严艺彬 田茂生 聂作明 蒋彩英**
点击:39次 下载:2次
DOI:10.7679/j.issn.2095-1353.2026.048
作者单位:浙江理工大学生命科学与医药学院,杭州 310018
中文关键词:麦蛾柔茧蜂;副产物;丝纤维;形态结构;性能特征
英文关键词: Habrobracon hebetor; byproduct; silk fibers; morphological structur; performance characteristics
中文摘要:

【目的】 麦蛾柔茧蜂Habrobracon hebetor是一种隶属于茧蜂科Braconidae的寄生性昆虫,其所分泌的丝纤维为天然蛋白材料,相关形态结构与理化性能尚缺乏系统性研究。为探究麦蛾柔茧蜂茧丝纤维的结构与性能,挖掘昆虫丝资源,本文采用多种表征手段,对其外观形态、二级结构、丝蛋白化学组成、吸湿性能与热学特性进行分析。【方法】 采用扫描电子显微镜结合能谱分析观察茧丝的表面形貌与元素组成;利用傅立叶变换红外光谱和X射线衍射解析茧丝蛋白二级结构;通过氨基酸组分分析丝蛋白的特点;回潮率试验评估茧丝的吸湿能力;采用热重分析研究茧丝的热分解行为与热稳定性。【结果】 扫描电镜结果显示茧丝纤维为细长均匀的单丝结构,平均直径为(1.39±0.22)μm;能谱分析显示其主要元素为碳(66.95%)、氮(18.44%)和氧(12.59%),呈现典型的蛋白质特征。根据氨基酸组成分析,茧丝蛋白主要含丝氨酸(33.3%)、甘氨酸(24.2%)和天冬氨酸/天冬酰胺(16.7%);测定茧丝的回潮率为10.45%±0.26%,显著高于蚕丝(P<0.01);红外光谱与X射线衍射结果表明蛋白二级结构以β-折叠和β-转角为主。热重分析表明其热分解温度为(317.13±1.29)℃,略低于家蚕丝。【结论】 麦蛾柔茧蜂茧丝具有精细的微观结构、富含β-折叠结构和β-转角的蛋白二级结构、优异的吸湿能力和较好的热稳定性,在天然丝纤维材料的多功能化和绿色可持续开发方面展现出潜在的应用前景,为寄生蜂类昆虫丝资源的挖掘与利用提供了理论依据。

英文摘要:

 [Aim]  To investigate the structure and properties of cocoon silk fibers from Habrobracon hebetor, and investigate their potential as a silk resource. [Methods]  Multiple characterization techniques were used to analyze their morphology, secondary structure, silk protein composition, moisture absorption properties, and thermal properties, of H. hebetor silk. Scanning electron microscopy, combined with energy-dispersive spectroscopy, were used to observe the surface morphology and elemental composition of the silk. Fourier transform infrared spectroscopy and X-ray diffraction were employed to analyze the secondary structure of its proteins and its amino acid composition was determined to reveal characteristic features of its proteins. The capacity of the silk to regain moisture was measured to evaluate its hygroscopic properties. In addition, thermogravimetric analysis was used to assess its thermal decomposition behavior and thermal stability. [Results]  Scanning electron microscopy revealed that H. hebetor silk fibers are slender and uniform monofilaments with an average diameter of (1.39 ± 0.22) μm. Energy-dispersive spectroscopy analysis indicates that its main elements are carbon (66.95%), nitrogen (18.44%) and oxygen (12.59%), which is typical of a protein. Amino acid analysis showed that the silk protein is mainly composed of serine (33.3%), glycine (24.2%), and aspartic acid/asparagine (16.7%). The capacity of H. hebetor silk to regain moisture was 10.45% ± 0.26%, which is significantly higher than that of Bombyx mori silk (P<0.01). Fourier transform infrared spectroscopy and X-ray diffraction results demonstrated that the secondary protein structures are predominantly β-sheets and β-turns. Thermogravimetric analysis indicates that H. hebetor silk has a thermal decomposition temperature of (317.13 ± 1.29) , which is slightly lower than that of B. mori silk. [Conclusion]  The cocoon silk of exhibits a fine and uniform microstructure, a secondary structure rich in β-sheets and β-turns, excellent hygroscopic properties and favorable thermal stability. These findings suggest that it has the potential to be used in multifunctional natural silk-based materials. These findings provide theoretical support for the investigation and utilization of the silk produced by parasitoid wasps.

读者评论

我要评论:
版权所有©2026应用昆虫学报》编辑部 京ICP备10006425号
本系统由北京菲斯特诺科技有限公司设计开发
您是本站第13191706名访问者