{"title":"一种新型几丁质脱乙酰酶的结合稳定性、催化机理及壳聚糖的制备。","authors":"Bicheng Liang, , , Tong Zhang, , , Guantian Li, , , Haoyue Yang, , , Zongji Wang, , , Kecheng Li, , , Song Liu, , , Huahua Yu, , and , Ronge Xing*, ","doi":"10.1021/acs.jafc.5c08532","DOIUrl":null,"url":null,"abstract":"<p >This study reports the heterologous expression, purification, and functional characterization of a novel chitin deacetylase (CDA) from <i>Cytobacillus firmus</i>. The recombinant <i>Cf</i>CDA exhibited optimal activity at pH 7 and 35 °C, with Mg<sup>2+</sup> enhancing its function. Deep eutectic solvent (DES) pretreatment significantly improved chitin accessibility, enabling <i>Cf</i>CDA to produce chitosan with a high degree of deacetylation (71.2%) and recovery rate (14.2%). Structural analyses confirmed reduced crystallinity and successful acetyl removal. Molecular docking and dynamics simulations identified Asp318, His470, and Trp433 as key catalytic residues with stable binding to (GlcNAc)<sub>4</sub>. These findings highlight <i>Cf</i>CDA’s potential for eco-friendly chitosan production and provide a basis for future enzyme engineering.</p>","PeriodicalId":41,"journal":{"name":"Journal of Agricultural and Food Chemistry","volume":"73 39","pages":"24866–24881"},"PeriodicalIF":6.2000,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Binding Stability and Catalytic Mechanism of a Novel Chitin Deacetylase from Cytobacillus firmus and Preparation of Chitosan\",\"authors\":\"Bicheng Liang, , , Tong Zhang, , , Guantian Li, , , Haoyue Yang, , , Zongji Wang, , , Kecheng Li, , , Song Liu, , , Huahua Yu, , and , Ronge Xing*, \",\"doi\":\"10.1021/acs.jafc.5c08532\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p >This study reports the heterologous expression, purification, and functional characterization of a novel chitin deacetylase (CDA) from <i>Cytobacillus firmus</i>. The recombinant <i>Cf</i>CDA exhibited optimal activity at pH 7 and 35 °C, with Mg<sup>2+</sup> enhancing its function. Deep eutectic solvent (DES) pretreatment significantly improved chitin accessibility, enabling <i>Cf</i>CDA to produce chitosan with a high degree of deacetylation (71.2%) and recovery rate (14.2%). Structural analyses confirmed reduced crystallinity and successful acetyl removal. Molecular docking and dynamics simulations identified Asp318, His470, and Trp433 as key catalytic residues with stable binding to (GlcNAc)<sub>4</sub>. These findings highlight <i>Cf</i>CDA’s potential for eco-friendly chitosan production and provide a basis for future enzyme engineering.</p>\",\"PeriodicalId\":41,\"journal\":{\"name\":\"Journal of Agricultural and Food Chemistry\",\"volume\":\"73 39\",\"pages\":\"24866–24881\"},\"PeriodicalIF\":6.2000,\"publicationDate\":\"2025-09-22\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Agricultural and Food Chemistry\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://pubs.acs.org/doi/10.1021/acs.jafc.5c08532\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"AGRICULTURE, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Agricultural and Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://pubs.acs.org/doi/10.1021/acs.jafc.5c08532","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, MULTIDISCIPLINARY","Score":null,"Total":0}
Binding Stability and Catalytic Mechanism of a Novel Chitin Deacetylase from Cytobacillus firmus and Preparation of Chitosan
This study reports the heterologous expression, purification, and functional characterization of a novel chitin deacetylase (CDA) from Cytobacillus firmus. The recombinant CfCDA exhibited optimal activity at pH 7 and 35 °C, with Mg2+ enhancing its function. Deep eutectic solvent (DES) pretreatment significantly improved chitin accessibility, enabling CfCDA to produce chitosan with a high degree of deacetylation (71.2%) and recovery rate (14.2%). Structural analyses confirmed reduced crystallinity and successful acetyl removal. Molecular docking and dynamics simulations identified Asp318, His470, and Trp433 as key catalytic residues with stable binding to (GlcNAc)4. These findings highlight CfCDA’s potential for eco-friendly chitosan production and provide a basis for future enzyme engineering.
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The Journal of Agricultural and Food Chemistry publishes high-quality, cutting edge original research representing complete studies and research advances dealing with the chemistry and biochemistry of agriculture and food. The Journal also encourages papers with chemistry and/or biochemistry as a major component combined with biological/sensory/nutritional/toxicological evaluation related to agriculture and/or food.
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