A Highly<i>N</i>-Glycosylated Chitin Deacetylase Derived from a Novel Strain of<i>Mortierella</i>sp. DY-52

Zhao, Yong; Jo, Gyung-Hyun; Ju, Wan-Taek; Jung, Woo‐Jin; Park, Ro-Dong

doi:10.1271/bbb.110011

Cited by 8 publications

(5 citation statements)

References 21 publications

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“…Although both crude CDAs cannot handle chitin monomer (GlcNAc), comparable with the other fungal CDAs reported till now, it indeed shows enzyme activity on chitin oligomers with a DP ranging from 2 to 7 and their activities increase with the increasing DP (Kim et al 2008, Zhao et al 2010a. In a more recent report, Zhao et al (2011) indicated that a chemical modification of crystalline chitin using phosphate acid could indeed increase the CDA enzyme activity to 3-4 fold, however, the enzyme activity was still very low compared to water soluble chitin.…”

Section: Non-biological Modificationssupporting

confidence: 58%

Perspectives of Chitin Deacetylase Research

Yong¹,

Ju²,

Jo³

et al. 2011

Biotechnology of Biopolymers

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Section: Non-biological Modificationssupporting

confidence: 58%

Perspectives of Chitin Deacetylase Research

Yong¹,

Ju²,

Jo³

et al. 2011

Biotechnology of Biopolymers

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“…An extracellular CDA was identified [58] and purified from a Mortierella sp. as a highly glycosylated protein with maximum activity at pH 5.5–6 and 60 °C [112]. Mo CDA is active on soluble substrates as chitosans and glycol-chitin but with no detectable activity on β-chitin, colloidal chitin, and CM-chitin.…”

Section: Function and Specificity Of Ce4 Chitin Deacetylasesmentioning

confidence: 99%

Chitin Deacetylases: Structures, Specificities, and Biotech Applications

et al. 2018

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Depolymerization and de-N-acetylation of chitin by chitinases and deacetylases generates a series of derivatives including chitosans and chitooligosaccharides (COS), which are involved in molecular recognition events such as modulation of cell signaling and morphogenesis, immune responses, and host-pathogen interactions. Chitosans and COS are also attractive scaffolds for the development of bionanomaterials for drug/gene delivery and tissue engineering applications. Most of the biological activities associated with COS seem to be largely dependent not only on the degree of polymerization but also on the acetylation pattern, which defines the charge density and distribution of GlcNAc and GlcNH 2 moieties in chitosans and COS. Chitin de-N-acetylases (CDAs) catalyze the hydrolysis of the acetamido group in GlcNAc residues of chitin, chitosan, and COS. The deacetylation patterns are diverse, some CDAs being specific for single positions, others showing multiple attack, processivity or random actions. This review summarizes the current knowledge on substrate specificity of bacterial and fungal CDAs, focusing on the structural and molecular aspects of their modes of action. Understanding the structural determinants of specificity will not only contribute to unravelling structure-function relationships, but also to use and engineer CDAs as biocatalysts for the production of tailor-made chitosans and COS for a growing number of applications.

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“…Consequently, chitosan is attracting increasing attention and is already widely applied in industrial and biomedical fields (Philibert et al, 2017). However, the economic potential of chitosan is far from being fully exploited due to the environmentally unfriendly thermochemical generation method and the poor reproducibility of batch-to-batch activities (Zhao et al, 2011). An alternative production procedure could potentially be employed with the application of enzymatic de-N-acetylation, allowing the production of chitosan with specific degrees of acetylation (DA) and patterns of acetylation (PA).…”

Section: Introductionmentioning

confidence: 99%

Comparative characterization of putative chitin deacetylases from Phaeodactylum tricornutum and Thalassiosira pseudonana highlights the potential for distinct chitin‐based metabolic processes in diatoms

Shao

Thomas

Hembach³

et al. 2018

New Phytologist

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Summary Chitin is generally considered to be present in centric diatoms but not in pennate species. Many aspects of chitin biosynthetic pathways have not been explored in diatoms. We retrieved chitin metabolic genes from pennate (Phaeodactylum tricornutum) and centric (Thalassiosira pseudonana) diatom genomes. Chitin deacetylase (CDA) genes from each genome (PtCDA and TpCDA) were overexpressed in P. tricornutum. We performed comparative analysis of their sequence structure, phylogeny, transcriptional profiles, localization and enzymatic activities. The chitin relevant proteins show complex subcellular compartmentation. PtCDA was likely acquired by horizontal gene transfer from prokaryotes, whereas TpCDA has closer relationships with sequences in Opisthokonta. Using transgenic P. tricornutum lines expressing CDA‐green fluorescent protein (GFP) fusion proteins, PtCDA predominantly localizes to Golgi apparatus whereas TpCDA localizes to endoplasmic reticulum/chloroplast endoplasmic reticulum membrane. CDA‐GFP overexpression upregulated the transcription of chitin synthases and potentially enhanced the ability of chitin synthesis. Although both CDAs are active on GlcNAc5, TpCDA is more active on the highly acetylated chitin polymer DA60. We have addressed the ambiguous characters of CDAs from P. tricornutum and T. pseudonana. Differences in localization, evolution, expression and activities provide explanations underlying the greater potential of centric diatoms for chitin biosynthesis. This study paves the way for in vitro applications of novel CDAs.

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A HighlyN-Glycosylated Chitin Deacetylase Derived from a Novel Strain ofMortierellasp. DY-52

Cited by 8 publications

References 21 publications

Perspectives of Chitin Deacetylase Research

Perspectives of Chitin Deacetylase Research

Chitin Deacetylases: Structures, Specificities, and Biotech Applications

Comparative characterization of putative chitin deacetylases from Phaeodactylum tricornutum and Thalassiosira pseudonana highlights the potential for distinct chitin‐based metabolic processes in diatoms

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