现代纺织技术 ›› 2025, Vol. 33 ›› Issue (02): 42-48.

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基于蛋白质组学的丝素蛋白微生物降解机理

  

  1. 浙江理工大学材料科学与工程学院, 杭州 310018
  • 出版日期:2025-02-10 网络出版日期:2025-02-24

Mechanism of microbial degradation of silk fibroin based on proteomics

  1. School of Materials Science & Engineering, Zhejiang Sci-Tech University, Hangzhou 310018, China
  • Published:2025-02-10 Online:2025-02-24

摘要: 为了揭示丝绸的微生物降解机理,利用蛋白质组学结合热场发射扫描电子显微镜、X射线衍射技术研究了丝绸在米曲霉代谢物降解前后宏观和微观结构变化,并探讨了降解作用在丝绸微生物劣化过程中的地位。形貌分析发现,丝绸经过米曲霉代谢物降解后发生了明显的黄变现象,表面纤维大量脱落;二级结构分析表明,丝蛋白分子构象遭到了破坏,结晶度明显下降;蛋白质组学分析显示,丝素蛋白重链、丝素蛋白轻链和P25都发生了不同程度的降解,而且重链蛋白的降解程度更高。经过测试分析,文章推测出一种丝素蛋白米曲霉劣化模型:米曲霉通过降解作用侧重分解丝素蛋白重链,丝素蛋白结晶区域结构崩塌,转变为松散的非晶结构,丝绸丧失原有的物理化学性能,逐渐被降解破坏。该研究结果对于深入了解古代丝绸劣化机理具有重要意义,为制定针对性的丝绸文物保护和修复策略提供了重要参考。

关键词: 丝绸, 降解机理, X射线衍射, 二级结构, 蛋白质组学

Abstract: Silk cultural relics, with their historical, cultural, and artistic value, offer invaluable insights into ancient civilizations. However, like all natural materials, silk is highly susceptible to physical, chemical and biological factors, losing its original value. Therefore, the preservation and restoration of silk cultural relics have always been the focus of cultural relic protection, and in-depth research on the microbial degradation process of silk fibers is of great importance to formulate effective strategies for the protection. The complex multi-level structure of silk fibroin leads to its complicated degradation mechanism, changes in each level of structure may lead to the degradation of silk. And the changeable environment also brings difficulties to the research of aging and degradation of silk cultural relics. The scarcity and non-renewability of silk cultural relics are also major challenges for cultural relics conservationists. To overcome these difficulties, the artificial simulation aging method can be used to study the aging and degradation behavior of silk fibroin.
To reveal the microbial degradation mechanism of silk, this paper investigated the macroscopic and microscopic structural changes of silk before and after degradation of Aspergillus oryzae metabolites using proteomics combined with thermal field emission scanning electron microscopy and XRD techniques. The results of morphological analysis showed that the color of silk changed significantly after aging, and a large number of fibres's shedding and axial cracks appeared on the surface of silk fibres. The results of secondary structure analysis showed that the molecular conformation of silk proteins was damaged, and the degree of crystallinity was significantly decreased. The proteomics results showed that both the number of polypeptides and the total abundance of proteins in silk fibroin decreased significantly, indicating that silk fibroin can be degraded by metabolites, and the abundance of heavy chains constituting the crystalline region of silk fibroin decreased the fastest.
A model of deterioration of silk fibroin by Aspergillus oryzae is postulated: Aspergillus oryzae focuses on the decomposition of fibroin heavy chain through degradation, and the structure of the crystalline region of the silk fibroin collapses into a loose amorphous structure, and the silk loses its original physicochemical properties, and is eventually completely degraded and destroyed. This study is of great significance for the in-depth understanding of the deterioration mechanism of ancient silk and provides an important basis for the targeted protection and restoration strategies for silk cultural relics.

Key words: silk, degradation mechanism, XRD, secondary structure, proteomics

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