Chitin Organizing and Modifying Enzymes and Proteins Involved In Remodeling of the Insect Cuticle

  • Subbaratnam MuthukrishnanEmail author
  • Hans Merzendorfer
  • Yasuyuki Arakane
  • Qing Yang
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 1142)


Chitin, the extracellular matrix polysaccharide of insects and arthropods is widely distributed in nature in all kingdoms of life and serves a variety of functions. After synthesis by membrane-bound chitin synthases, it is extensively remodeled before incorporation into divergent matrices with wide-ranging physical and biological properties. This chapter discusses the properties of a variety of insect enzymes and proteins involved in this process. Chitin remodeling involves chitin synthases, which make the nascent chitin chains, and chitin deacetylases that partially deacetylate some of the N-acetylglucosamine residues either randomly or sequentially to yield local chitosan-like regions. Other proteins secreted into the procuticle or the midgut help in the assembly of single chitin chains into larger crystalline aggregates that measure in a few 100 nanometers. They are further embedded in a complex matrix of cuticular proteins or become associated with proteins containing chitin-binding domains to constitute the laminar procuticle or the lattice-like peritrophic matrix. During molting, previously formed laminar cuticle or PM are decrystallized/depolymerized to unmask the chitin chains, which then are degraded by a mixture of chitinolytic enzymes consisting of chitinases and N-acetylglucosaminidases present in molting fluid or in gut secretions. Some of the degradation products may be recycled for the synthesis of new matrices. We present a model of chitin synthesis, assembly, and degradation and the roles of these chitin-remodeling enzymes in this overall process.


Chitin Chitin remodeling Chitin synthase Chitinase Chitin deacetylase N-acetylglucosaminidase Knickkopf Cuticular proteins Peritrophic matrix 



This work was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Korea government (MSIT) (2018R1A2B6005106) to YA.


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Copyright information

© Springer Nature Singapore Pte Ltd. 2019

Authors and Affiliations

  • Subbaratnam Muthukrishnan
    • 1
    Email author
  • Hans Merzendorfer
    • 2
  • Yasuyuki Arakane
    • 3
  • Qing Yang
    • 4
  1. 1.Department of Biochemistry and Molecular BiophysicsKansas State UniversityManhattanUSA
  2. 2.Institute of Biology, University of SiegenSiegenGermany
  3. 3.Department of Applied BiologyChonnam National UniversityGwangjuSouth Korea
  4. 4.School of BioengineeringDalian University of TechnologyDalianChina

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