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Chitin Deacetylase from TCI-16: Heterologous Expression, Characterization, and Deacetylation Performance. | LitMetric

Chitin Deacetylase from TCI-16: Heterologous Expression, Characterization, and Deacetylation Performance.

J Agric Food Chem

College of Food Science and Technology, Guangdong Ocean University, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Province Engineering Laboratory for Marine Biological Products, Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Provincial Engineering Technology Research Center of Prefabricated Seafood Processing and Quality Control, Zhanjiang 524088, China.

Published: April 2024

AI Article Synopsis

Article Abstract

Chitin deacetylase (CDA) removes the acetyl group from the chitin molecule to generate chitosan in a uniform, high-quality deacetylation pattern. Herein, BaCDA was a novel CDA discovered from our previously isolated strain TCI-16, which was excavated from mangrove soil. The gene was cloned and overexpressed in BL21 (DE3) to facilitate its subsequent purification. The purified recombinant protein BaCDA was obtained at a concentration of about 1.2 mg/mL after Ni affinity chromatography. The molecular weight of BaCDA was around 28 kDa according to the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis. In addition, BaCDA exhibited a significant deacetylation effect on colloidal chitin, and the deacetylation degree was measured from the initial 25.69 to 69.23% by Fourier transform infrared (FT-IR) spectroscopy. Scanning electron microscopy (SEM) observation showed that the surface of colloidal chitin after enzymatic digestion was rough, the crystal fibers disappeared, and the chitin structure was loose and porous with grooves. The results of electrospray ionization mass spectrometry (ESI-MS) showed that BaCDA had full-deacetylation activity against (GlcNAc). Molecular docking revealed that BaCDA had an open active pocket capable of binding to the GlcNAc unit. This study not only provides a novel enzymatic resource for the green and efficient application of chitin but also helps to deepen the understanding of the catalytic mechanism of CDA.

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http://dx.doi.org/10.1021/acs.jafc.4c00321DOI Listing

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