Structural and functional characterization of the cocoon silk of Habrobracon hebetor (Hymenoptera: Braconidae)
Author of the article:HU Die* HUANG Ting-Li LI Xiao-Yu YAN Yi-Bin TIAN Mao-Sheng NIE Zuo-Ming JIANG Cai-Ying**
Author's Workplace:College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, China
Key Words: Habrobracon hebetor; byproduct; silk fibers; morphological structur; performance characteristics
Abstract:
[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.