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Special Issue Editors

Dr. Matthias Behr

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Guest Editor

Institute for Biology, Leipzig University, 04103 Leipzig, Germany
Interests: cuticle biology; chitinases; epithelial barrier formation; animal genetics

Prof. Dr. Bernard Moussian

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Guest Editor

Institut Sophia Agrobiotech, Université Côte d’Azur, INRAE, CNRS, 400 route des Chappes, 06 903 Sophia Antipolis, France
Interests: cuticle biology; cuticle lipids; chitin formation; resilin

Special Issue Information

Dear Colleagues,

Chitinases belong to the large family of glycoside hydrolases that includes non-chitinolytic proteins and chitinolytic enzymes. The family members have been identified in prokaryotes, among the animal kingdom from yeasts to humans and also in plants and, importantly, cover a wide range of functions.

Chitin-producing organisms require enzymatic chitinases to degrade chitin as part of their cell/body wall and during chitin matrix formation. In contrast, organisms that do not produce chitin use chitinases as part of their immune response to fight invading pathogens and microbes, but also arthropods use specific chitinases for their cellular immune response. In addition, chitinases promote cell proliferation and division, are associated with human diseases, such as obstructive lung diseases, and have been linked to cancer growth.

Since chitin is the second most abundant biopolymer in nature and provides the barrier-forming body wall of many pathogens, chitinases are extremely promising candidate genes as a target for pest control in crop science and food production. Furthermore, chitin-based materials possess antimicrobial, antioxidant, anticarcinogenic and anti-inflammatory properties, therefore contributing to an increasing number of applications in materials science, including biomedical and pharmaceutical applications. Therefore, the enzymatic activity of chitinases will support the production of future eco-friendly biomaterials.

We encourage you to contribute your latest research and knowledge of chitinases and other chitin-degrading enzymes. We will establish a comprehensive scientific overview of chitin-degrading enzymes, their biological functions, and translational usage in pest science, materials science, and associated biomedicine.

Dr. Matthias Behr
Prof. Dr. Bernard Moussian
Guest Editors

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Keywords

biomaterial
chitin
chitinase
chitotriosidase
chitin degradation
glycoside hydrolase
extracellular matrix
imaginal disc growth factor
immune response
molting

Published Papers (3 papers)

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Research

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15 pages, 5292 KiB

Open AccessArticle

LmCht5-1 and LmCht5-2 Promote the Degradation of Serosal and Pro-Nymphal Cuticles during Locust Embryonic Development

by Tingting Zhang, Yanjun Huo, Qing Dong, Weiwei Liu, Lu Gao, Jiannan Zhou, Daqi Li, Xueyao Zhang, Jianzhen Zhang and Min Zhang

Biology 2022, 11(12), 1778; https://doi.org/10.3390/biology11121778 - 7 Dec 2022

Cited by 3 | Viewed by 1236

Abstract

The success of the degradation of the extraembryonic serosal cuticle and the second embryonic cuticle (pro-nymphal cuticle) is essential for the development and molting of nymph from egg in Orthoptera Locusta migratoria. Chitinase 5 is an important gene for chitin degradation in nymphs and in the egg stage. In this study, we investigated the important roles of chitinase 5-1 (LmCht5-1) and chitinase 5-2 (LmCht5-2) in the degradation of the serosal and pro-nymphal cuticles during locust embryonic development. The serosal cuticle degrades from 7-day-old embryos (E7) to E13, along with the degradation of the pro-nymphal cuticle, which begins at E12 to E14. The mRNA and protein of LmCht5-1 and LmCht5-2 are expressed during the degradation process of the serosal cuticle and the pro-nymphal cuticle. RNAi experiments at the embryonic stage show that both dsLmCht5-1 and dsLmCht5-2 contribute to the failure of development in early and late embryogenesis. Further, during the serosal cuticle molting process, ultra-structure analysis indicated that dsLmCht5-1 prevented the loss of the coarse chitin layer in the upper part in both early and late embryogenesis. Meanwhile, dsLmCht5-2 blocked the degradation of the lower fine chitin layer at the early stage and blocked the chitin degradation of loose coarse chitin in the late molting process. During the degradation of the pro-nymphal cuticle, dsLmCht5-1 suppresses chitin degradation between layers in the procuticle, while dsLmCht5-2 suppresses chitin degradation into filaments inside of the layer. In summary, our results suggest that both LmCht5-1 and LmCht5-2 contribute to the degradation of the serosal and pro-nymphal cuticles during the locust embryonic stage. Full article

(This article belongs to the Special Issue Chitin-Degrading Enzymes, Breaking Barriers in Life and Material Sciences)

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Review

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20 pages, 2319 KiB

Open AccessReview

Chitinase-Assisted Bioconversion of Chitinous Waste for Development of Value-Added Chito-Oligosaccharides Products

by Siriporn Taokaew and Worawut Kriangkrai

Biology 2023, 12(1), 87; https://doi.org/10.3390/biology12010087 - 5 Jan 2023

Cited by 9 | Viewed by 3572 | Correction

Abstract

Chito-oligosaccharides (COSs) are the partially hydrolyzed products of chitin, which is abundant in the shells of crustaceans, the cuticles of insects, and the cell walls of fungi. These oligosaccharides have received immense interest in the last few decades due to their highly promising bioactivities, such as their anti-microbial, anti-tumor, and anti-inflammatory properties. Regarding environmental concerns, COSs are obtained by enzymatic hydrolysis by chitinase under milder conditions compared to the typical chemical degradation. This review provides updated information about research on new chitinase derived from various sources, including bacteria, fungi, plants, and animals, employed for the efficient production of COSs. The route to industrialization of these chitinases and COS products is also described. Full article

(This article belongs to the Special Issue Chitin-Degrading Enzymes, Breaking Barriers in Life and Material Sciences)

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