Biological control of phytopathogenic fungi and insects continues to inspire the research and development of environmentally friendly bioactive alternatives. Potentially lytic enzymes, chitinases can act as a biocontrol agent against agriculturally important fungi and insects. The cell wall in fungi and protective covers, i.e. cuticle in insects shares a key structural polymer, chitin, a β-1,4-linked N-acetylglucosamine polymer. Therefore, it is advantageous to develop a common biocontrol agent against both of these groups. As chitin is absent in plants and mammals, targeting its metabolism will signify an eco-friendly strategy for the control of agriculturally important fungi and insects but is innocuous to mammals, plants, beneficial insects and other organisms. In addition, development of chitinase transgenic plant varieties probably holds the most promising method for augmenting agricultural crop protection and productivity, when properly integrated into traditional systems. Recently, human proteins with chitinase activity and chitinase-like proteins were identified and established as biomarkers for human diseases. This review covers the recent advances of chitinases as a biocontrol agent and its various applications including preparation of medically important chitooligosaccharides, bioconversion of chitin as well as in implementing chitinases as diagnostic and prognostic markers for numerous diseases and the prospect of their future utilization.

Chitinases: in agriculture and human healthcare

Diseases and other stress factors working synergistically weaken honey bee health and may play a major role in the losses of bee populations in recent years. Among a large number of bee diseases, chalkbrood has been on the rise. We present here the experimental identification of honey bee genes that are differentially expressed in response to infection of honey bee larvae with the chalkbrood fungus, Ascosphaera apis. We used cDNA-AFLP ®Technology to profile transcripts in infected and uninfected bee larvae. From 64 primer combinations, over 7,400 transcriptionally-derived fragments were obtained A total of 98 reproducible polymorphic cDNA-AFLP fragments were excised and sequenced, followed by quantitative real-time RT-PCR (qRT-PCR) analysis of these and additional samples. We have identified a number of differentially-regulated transcripts that are implicated in general mechanisms of stress adaptation, including energy metabolism and protein transport. One of the most interesting differentially-regulated transcripts is for a chitinase-like enzyme that may be linked to anti-fungal activities in the honey bee larvae, similarly to gut and fat-body specific chitinases found in mosquitoes and the red flour beetle. Surprisingly, we did not find many components of the well-characterized NF-κB intracellular signaling pathways to be differentially-regulated using the cDNA-AFLP approach. Therefore, utilizing qRT-PCR, we probed some of the immune related genes to determine whether the lack of up-regulation of their transcripts in our analysis can be attributed to lack of immune activation or to limitations of the cDNA-AFLP approach. Using a combination of cDNA-AFLP and qRT-PCR analyses, we were able to determine several key transcriptional events that constitute the overall effort in the honey bee larvae to fight natural fungal infection. Honey bee transcripts identified in this study are involved in critical functions related to transcriptional regulation, apoptotic degradation of ubiquitinated proteins, nutritional regulation, and RNA processing. We found that immune regulation of the anti-fungal responses in honey bee involves highly coordinated activation of both NF-κB signaling pathways, leading to production of anti-microbial peptides. Significantly, activation of immune responses in the infected bee larvae was associated with down-regulation of major storage proteins, leading to depletion of nutritional resources.

https://link.springer.com/content/pdf/10.1186%2F1471-2164-11-391.pdf

Transcriptional responses in Honey Bee larvae infected with chalkbrood fungus

https://bqexperimental.files.wordpress.com/2010/01/articulo-purificacion.pdf

Purification and characterization of chitinase from the stomach of silver croaker Pennahia argentatus

Purification and characterization of a novel chitinase from Trichosanthes dioica seed with antifungal activity

Biochemistry of fish stomach chitinase.

75-kDa chitinase, which showed potential as a biocontrol agent against Japanese pine sawyer, was characterized after purification from the integument of the fifth instar larvae of Bombyx mori by chromatography on diethylaminoethyl (DEAE)-Toyoperal 650 (M), hydroxylapatite, and Fractogel EMD DEAE 650 (M) columns. The optimum pH was 6.0 toward N-acetylchitopentaose (GlcNAc5) and 10 toward glycolchitin. The optimum temperature was 60 °C toward GlcNAc5 and 25 °C toward glycolchitn. The enzyme was stable at pH 7–10 and below 40 °C. Kinetic analysis and reaction-pattern analysis using glycolchitin and N-acetylchitooligosacchraides as substrates indicated that 75-kDa chitinase is an endo- or random-type hydrolytic enzyme to produce the β anomeric product and that it prefers the longer N-acetylchitooligosaccharides, suggesting, together with the N-terminal amino acid sequence, that the 75-kDa chitinase belongs to family 18 of glycosyl hydrolases.

https://www.tandfonline.com/doi/pdf/10.1271/bbb.70.252

Purification and Characterization of a Novel Isozyme of Chitinase from Bombyx mori

PROBLEM TO BE SOLVED: To provide a novel chitinase, especially a silkworm chitinase having an insecticidal effect on Monochamus alternatus, to allow the development of a chitinase agent effective as a safe Monochamus alternatus-controlling agent derived from organism. SOLUTION: Provided is a chitinase having the following characteristics: (1) pH stability range: 7-12; (2) thermal stability range: 0-40°C; (3) kcat/Km value: 0.68 ml/mg/sec; and (4) cleavage pattern: end type. Also provided is a chitinase belonging to family 18 chitinase, wherein the 10 residues of the amino acid sequence of the N terminal end thereof is ADSXAXIVXY and the chitinase has a molecular weight of 75 kDa and is derived from a silkworm. COPYRIGHT: (C)2008,JPO&INPIT

Silkworm chitinase and insect-controlling agent comprising the same

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Purification and Characterization of a Novel Isozyme of Chitinase from Bombyx mori

Silkworm chitinase and insect-controlling agent comprising the same