李小雨,胡蝶,黄廷莉,姚洪渭,蒋彩英,2024,二化螟盘绒茧蜂茧丝纤维的形态结构与理化性能[J].环境昆虫学报,46(5):1255-1260
二化螟盘绒茧蜂茧丝纤维的形态结构与理化性能
Morphological structure and physicochemical properties of silk fibers from the cocoons of the parasitoid wasp, Cotesia chilonis (Matsumura) (Hymenoptera: Braconidae)
  
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中文关键词:  二化螟盘绒茧蜂    丝纤维  形态结构  理化性能
英文关键词:Cotesia chilonis (Matsumura)  cocoon  silk fibers  morphological structure  physicochemical properties
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作者单位
李小雨,胡蝶,黄廷莉,姚洪渭,蒋彩英 1. 浙江理工大学生命科学与医药学院杭州 3100182. 浙江大学昆虫科学研究所浙江省作物病虫生物学重点实验室水稻生物学国家重点为实验室杭州 310058 
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中文摘要:
      本文通过扫描电镜(SEM)、氨基酸分析、傅立叶红外光谱(FTIR)、X射线晶体衍射(XRD)和热重分析(TG)等技术对二化螟盘绒茧蜂Cotesia chilonis茧丝纤维的微观形态、氨基酸类别与组成、二级结构和热稳定性等作了分析。结果表明,二化螟盘绒茧蜂的茧丝纤维表面较为粗糙,直径为1.89 ± 0.04 μm。茧丝纤维主要由碳(60.67%)、氮(21.17%)和氧(17.22%)等元素组成,其丝蛋白主要成分包括天冬氨酸/天冬酰胺、丝氨酸和丙氨酸等;蛋白二级结构主要为β-折叠;其峰值降解温度为332.27℃ ± 2.58℃。本文研究揭示了二化螟盘绒茧蜂茧丝纤维的结构特征与理化性能,为拓展该蜂的应用领域、开发性能优越的非蚕丝蛋白以及设计改造新型丝蛋白纤维提供基础。
英文摘要:
      In this paper, the morphological structure, amino acid composition, secondary structure and thermal stability of silk fibers from the cocoons of the parasitoid wasp, Cotesia chilonis (Matsumura) (Hymenoptera: Braconidae) were analyzed by the scanning electron microscopy (SEM), amino acid analysis, Fourier transform infrared spectroscopy (FTIR), X-ray crystallography (XRD) and thermogravimetric analysis (TG). The results showed that the surface of the silk fiber from C. chilonis cocoons was relatively rough, and its diameter was 1.89 ± 0.04 μm. It was mainly composed of elements such as carbon (60.67%), nitrogen (21.17%), and oxygen (17.22%). The protein components of C. chilonis cocoons mainly included aspartic acid/asparagine, serine and alanine. The secondary structure of silk proteins from C. chilonis cocoons was mainly β-sheet, and its peak degradation temperature was 332.27 ± 2.58℃. This study reveals the ultrastructural characteristics and physicochemical properties of silk fibers from C. chilonis cocoons, which provides a basis for expanding the application field of C. chilonis, developing non-worm silk proteins with superior performance, and designing and transforming new silk protein fibers.
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