Enhanced crystalline cellulose degradation by a novel metagenome-derived cellulase enzyme
Abstract Metagenomics has revolutionized access to genomic information of microorganisms inhabiting the gut of herbivorous animals, circumventing the need for their isolation and cultivation. Exploring these microorganisms for novel hydrolytic enzymes becomes unattainable without utilizing metagenom...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2024-04-01
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| Series: | Scientific Reports |
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| Online Access: | https://doi.org/10.1038/s41598-024-59256-4 |
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| author | Faezeh Kholousi Adab Mohammad Mehdi Yaghoobi Javad Gharechahi |
| author_facet | Faezeh Kholousi Adab Mohammad Mehdi Yaghoobi Javad Gharechahi |
| author_sort | Faezeh Kholousi Adab |
| collection | DOAJ |
| description | Abstract Metagenomics has revolutionized access to genomic information of microorganisms inhabiting the gut of herbivorous animals, circumventing the need for their isolation and cultivation. Exploring these microorganisms for novel hydrolytic enzymes becomes unattainable without utilizing metagenome sequencing. In this study, we harnessed a suite of bioinformatic analyses to discover a novel cellulase-degrading enzyme from the camel rumen metagenome. Among the protein-coding sequences containing cellulase-encoding domains, we identified and subsequently cloned and purified a promising candidate cellulase enzyme, Celcm05-2, to a state of homogeneity. The enzyme belonged to GH5 subfamily 4 and exhibited robust enzymatic activity under acidic pH conditions. It maintained hydrolytic activity under various environmental conditions, including the presence of metal ions, non-ionic surfactant Triton X-100, organic solvents, and varying temperatures. With an optimal temperature of 40 °C, Celcm05-2 showcased remarkable efficiency when deployed on crystalline cellulose (> 3.6 IU/mL), specifically Avicel, thereby positioning it as an attractive candidate for a myriad of biotechnological applications spanning biofuel production, paper and pulp processing, and textile manufacturing. Efficient biodegradation of waste paper pulp residues and the evidence of biopolishing suggested that Celcm05-2 can be used in the bioprocessing of cellulosic craft fabrics in the textile industry. Our findings suggest that the camel rumen microbiome can be mined for novel cellulase enzymes that can find potential applications across diverse biotechnological processes. |
| first_indexed | 2024-04-24T09:53:46Z |
| format | Article |
| id | doaj.art-e0951723ff8844399afe61f81a6e92bb |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-04-24T09:53:46Z |
| publishDate | 2024-04-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-e0951723ff8844399afe61f81a6e92bb2024-04-14T11:16:00ZengNature PortfolioScientific Reports2045-23222024-04-0114111510.1038/s41598-024-59256-4Enhanced crystalline cellulose degradation by a novel metagenome-derived cellulase enzymeFaezeh Kholousi Adab0Mohammad Mehdi Yaghoobi1Javad Gharechahi2Department of Biotechnology, Institute of Science and High Technology and Environmental Sciences, Graduate University of Advanced TechnologyDepartment of Biotechnology, Institute of Science and High Technology and Environmental Sciences, Graduate University of Advanced TechnologyHuman Genetic Research Center, Baqiyatallah University of Medical SciencesAbstract Metagenomics has revolutionized access to genomic information of microorganisms inhabiting the gut of herbivorous animals, circumventing the need for their isolation and cultivation. Exploring these microorganisms for novel hydrolytic enzymes becomes unattainable without utilizing metagenome sequencing. In this study, we harnessed a suite of bioinformatic analyses to discover a novel cellulase-degrading enzyme from the camel rumen metagenome. Among the protein-coding sequences containing cellulase-encoding domains, we identified and subsequently cloned and purified a promising candidate cellulase enzyme, Celcm05-2, to a state of homogeneity. The enzyme belonged to GH5 subfamily 4 and exhibited robust enzymatic activity under acidic pH conditions. It maintained hydrolytic activity under various environmental conditions, including the presence of metal ions, non-ionic surfactant Triton X-100, organic solvents, and varying temperatures. With an optimal temperature of 40 °C, Celcm05-2 showcased remarkable efficiency when deployed on crystalline cellulose (> 3.6 IU/mL), specifically Avicel, thereby positioning it as an attractive candidate for a myriad of biotechnological applications spanning biofuel production, paper and pulp processing, and textile manufacturing. Efficient biodegradation of waste paper pulp residues and the evidence of biopolishing suggested that Celcm05-2 can be used in the bioprocessing of cellulosic craft fabrics in the textile industry. Our findings suggest that the camel rumen microbiome can be mined for novel cellulase enzymes that can find potential applications across diverse biotechnological processes.https://doi.org/10.1038/s41598-024-59256-4MetagenomeCellulaseEndoglucanaseExoglucanaseBioprospectingAvicelase |
| spellingShingle | Faezeh Kholousi Adab Mohammad Mehdi Yaghoobi Javad Gharechahi Enhanced crystalline cellulose degradation by a novel metagenome-derived cellulase enzyme Scientific Reports Metagenome Cellulase Endoglucanase Exoglucanase Bioprospecting Avicelase |
| title | Enhanced crystalline cellulose degradation by a novel metagenome-derived cellulase enzyme |
| title_full | Enhanced crystalline cellulose degradation by a novel metagenome-derived cellulase enzyme |
| title_fullStr | Enhanced crystalline cellulose degradation by a novel metagenome-derived cellulase enzyme |
| title_full_unstemmed | Enhanced crystalline cellulose degradation by a novel metagenome-derived cellulase enzyme |
| title_short | Enhanced crystalline cellulose degradation by a novel metagenome-derived cellulase enzyme |
| title_sort | enhanced crystalline cellulose degradation by a novel metagenome derived cellulase enzyme |
| topic | Metagenome Cellulase Endoglucanase Exoglucanase Bioprospecting Avicelase |
| url | https://doi.org/10.1038/s41598-024-59256-4 |
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