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| Auteurs principaux: | , , , , , , , |
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| Format: | Artículo científico |
| Langue: | en |
| Publié: |
Marine drugs
2025
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| Sujets: | |
| Accès en ligne: | https://pubmed.ncbi.nlm.nih.gov/40137279/ |
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| _version_ | 1868266226135859200 |
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| author | Gu, Chenxi Chen, Jianrong Huang, Xinyue Jiang, Yongqiang Ou, Na Yang, Dengfeng Jiang, Mingguo Pan, Lixia |
| author_facet | Gu, Chenxi Chen, Jianrong Huang, Xinyue Jiang, Yongqiang Ou, Na Yang, Dengfeng Jiang, Mingguo Pan, Lixia Gu, Chenxi Chen, Jianrong Huang, Xinyue Jiang, Yongqiang Ou, Na Yang, Dengfeng Jiang, Mingguo Pan, Lixia |
| collection | PubMed - marine biology |
| contents | The Impact of Chitinase Binding Domain Truncation on the Properties of Chi18B from CSC-1. Gu, Chenxi Chen, Jianrong Huang, Xinyue Jiang, Yongqiang Ou, Na Yang, Dengfeng Jiang, Mingguo Pan, Lixia Betaproteobacteria Protein Domains Chitinases Bacterial Proteins Hydrolysis Recombinant Proteins Chitin Substrate Specificity Conserved Sequence Amino Acid Sequence The chitinase binding domain (ChBD) plays a crucial role in the properties of enzymes. To assess its impact, we cloned a truncated mutant of the chitinase gene from the novel chitinase-producing facultative anaerobic bacterium CSC-1, designated as . The recombinant chitinase was successfully expressed and purified, exhibiting a specific activity of 3.48 U/mg on colloidal chitin, with optimal conditions at 45 °C and pH 6.0, and retaining over 80% activity at temperatures up to 40 °C. Kinetic analysis revealed that the value was 1.159 mg mL and the was 10.37 μM min mg. Compared to Chi18B_ΔChBD, which has only the first ChBD truncated at the N-terminus, Chi18B_ΔChBD exhibited minor changes in the optimal temperature and pH, while the and values increased significantly. Chi18B_ΔChBD exhibited tolerance to various metal ions, with K and NH enhancing activity, while Cu significantly inhibited it. Most organic reagents had minimal impact, except for formic acid, which severely reduced activity. The primary hydrolysis product in the initial phase was GlcNAc, contrasting with (GlcNAc) for Chi18B_ΔChBD. These findings indicated that the ChBD influences the enzyme's , , and product distribution, enhancing our understanding of ChBD's roles and advancing chitin utilization. |
| format | Artículo científico |
| id | pubmed_40137279 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Marine drugs |
| record_format | pubmed |
| spellingShingle | The Impact of Chitinase Binding Domain Truncation on the Properties of Chi18B from CSC-1. Gu, Chenxi Chen, Jianrong Huang, Xinyue Jiang, Yongqiang Ou, Na Yang, Dengfeng Jiang, Mingguo Pan, Lixia Betaproteobacteria Protein Domains Chitinases Bacterial Proteins Hydrolysis Recombinant Proteins Chitin Substrate Specificity Conserved Sequence Amino Acid Sequence The Impact of Chitinase Binding Domain Truncation on the Properties of Chi18B from CSC-1. Gu, Chenxi Chen, Jianrong Huang, Xinyue Jiang, Yongqiang Ou, Na Yang, Dengfeng Jiang, Mingguo Pan, Lixia Betaproteobacteria Protein Domains Chitinases Bacterial Proteins Hydrolysis Recombinant Proteins Chitin Substrate Specificity Conserved Sequence Amino Acid Sequence The chitinase binding domain (ChBD) plays a crucial role in the properties of enzymes. To assess its impact, we cloned a truncated mutant of the chitinase gene from the novel chitinase-producing facultative anaerobic bacterium CSC-1, designated as . The recombinant chitinase was successfully expressed and purified, exhibiting a specific activity of 3.48 U/mg on colloidal chitin, with optimal conditions at 45 °C and pH 6.0, and retaining over 80% activity at temperatures up to 40 °C. Kinetic analysis revealed that the value was 1.159 mg mL and the was 10.37 μM min mg. Compared to Chi18B_ΔChBD, which has only the first ChBD truncated at the N-terminus, Chi18B_ΔChBD exhibited minor changes in the optimal temperature and pH, while the and values increased significantly. Chi18B_ΔChBD exhibited tolerance to various metal ions, with K and NH enhancing activity, while Cu significantly inhibited it. Most organic reagents had minimal impact, except for formic acid, which severely reduced activity. The primary hydrolysis product in the initial phase was GlcNAc, contrasting with (GlcNAc) for Chi18B_ΔChBD. These findings indicated that the ChBD influences the enzyme's , , and product distribution, enhancing our understanding of ChBD's roles and advancing chitin utilization. |
| title | The Impact of Chitinase Binding Domain Truncation on the Properties of Chi18B from CSC-1. |
| topic | Betaproteobacteria Protein Domains Chitinases Bacterial Proteins Hydrolysis Recombinant Proteins Chitin Substrate Specificity Conserved Sequence Amino Acid Sequence |
| url | https://pubmed.ncbi.nlm.nih.gov/40137279/ |