Characterization of a beta-glucosidase from Bacillus licheniformis and its effect on bioflocculant degradation
Abstract Bacillus licheniformis CGMCC 2876, an aerobic spore-forming bacterium, produces a polysaccharide bioflocculant that is biodegradable and harmless. The present study determined that β-glucosidase played a negative role in bioflocculant synthesis. The gene encoding β-glucosidase was cloned an...
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| Language: | English |
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SpringerOpen
2017-11-01
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| Series: | AMB Express |
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| Online Access: | http://link.springer.com/article/10.1186/s13568-017-0501-3 |
| _version_ | 1818511731756892160 |
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| author | Zhen Chen Tong Meng Zhipeng Li Peize Liu Yuanpeng Wang Ning He Dafeng Liang |
| author_facet | Zhen Chen Tong Meng Zhipeng Li Peize Liu Yuanpeng Wang Ning He Dafeng Liang |
| author_sort | Zhen Chen |
| collection | DOAJ |
| description | Abstract Bacillus licheniformis CGMCC 2876, an aerobic spore-forming bacterium, produces a polysaccharide bioflocculant that is biodegradable and harmless. The present study determined that β-glucosidase played a negative role in bioflocculant synthesis. The gene encoding β-glucosidase was cloned and expressed in Escherichia coli BL21. This gene consists of 1437 bp and encodes 478 amino acid residues. The recombinant β-glucosidase (Bgl.bli1) was purified and showed a molecular mass of 53.4 kDa by SDS-PAGE. The expression and reaction conditions of Bgl.bli1 were optimized; the activity of β-glucosidase reached a maximum at 45.44 U/mL. Glucose clearly inhibited the activity of β-glucosidase. The purified recombinant Bgl.bli1 hydrolysed polysaccharide bioflocculant in vitro and synergised with other cellulases. The ability of Bgl.bli1 to hydrolyse polysaccharide bioflocculant was the reason for the decrease in flocculating activity and indicated the utility of this enzyme for diverse industrial processes. |
| first_indexed | 2024-12-10T23:36:59Z |
| format | Article |
| id | doaj.art-43a63f40d79641eaa0f3f199ebe2bc89 |
| institution | Directory Open Access Journal |
| issn | 2191-0855 |
| language | English |
| last_indexed | 2024-12-10T23:36:59Z |
| publishDate | 2017-11-01 |
| publisher | SpringerOpen |
| record_format | Article |
| series | AMB Express |
| spelling | doaj.art-43a63f40d79641eaa0f3f199ebe2bc892022-12-22T01:29:09ZengSpringerOpenAMB Express2191-08552017-11-01711710.1186/s13568-017-0501-3Characterization of a beta-glucosidase from Bacillus licheniformis and its effect on bioflocculant degradationZhen Chen0Tong Meng1Zhipeng Li2Peize Liu3Yuanpeng Wang4Ning He5Dafeng Liang6Department of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen UniversityDepartment of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen UniversityDepartment of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen UniversityDepartment of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen UniversityDepartment of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen UniversityDepartment of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen UniversityGuangxi State Farms Sugar Industrial Group Company Limited, Guangxi Sugarcane Industry R&D CenterAbstract Bacillus licheniformis CGMCC 2876, an aerobic spore-forming bacterium, produces a polysaccharide bioflocculant that is biodegradable and harmless. The present study determined that β-glucosidase played a negative role in bioflocculant synthesis. The gene encoding β-glucosidase was cloned and expressed in Escherichia coli BL21. This gene consists of 1437 bp and encodes 478 amino acid residues. The recombinant β-glucosidase (Bgl.bli1) was purified and showed a molecular mass of 53.4 kDa by SDS-PAGE. The expression and reaction conditions of Bgl.bli1 were optimized; the activity of β-glucosidase reached a maximum at 45.44 U/mL. Glucose clearly inhibited the activity of β-glucosidase. The purified recombinant Bgl.bli1 hydrolysed polysaccharide bioflocculant in vitro and synergised with other cellulases. The ability of Bgl.bli1 to hydrolyse polysaccharide bioflocculant was the reason for the decrease in flocculating activity and indicated the utility of this enzyme for diverse industrial processes.http://link.springer.com/article/10.1186/s13568-017-0501-3β-GlucosidaseHeterologous expressionPolysaccharide bioflocculantBacillus licheniformis |
| spellingShingle | Zhen Chen Tong Meng Zhipeng Li Peize Liu Yuanpeng Wang Ning He Dafeng Liang Characterization of a beta-glucosidase from Bacillus licheniformis and its effect on bioflocculant degradation AMB Express β-Glucosidase Heterologous expression Polysaccharide bioflocculant Bacillus licheniformis |
| title | Characterization of a beta-glucosidase from Bacillus licheniformis and its effect on bioflocculant degradation |
| title_full | Characterization of a beta-glucosidase from Bacillus licheniformis and its effect on bioflocculant degradation |
| title_fullStr | Characterization of a beta-glucosidase from Bacillus licheniformis and its effect on bioflocculant degradation |
| title_full_unstemmed | Characterization of a beta-glucosidase from Bacillus licheniformis and its effect on bioflocculant degradation |
| title_short | Characterization of a beta-glucosidase from Bacillus licheniformis and its effect on bioflocculant degradation |
| title_sort | characterization of a beta glucosidase from bacillus licheniformis and its effect on bioflocculant degradation |
| topic | β-Glucosidase Heterologous expression Polysaccharide bioflocculant Bacillus licheniformis |
| url | http://link.springer.com/article/10.1186/s13568-017-0501-3 |
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