Screening, Identification and Characterization of a Marine Chitinase-Producing Strain Gallaecimonas xiamenensis Chi34
Objective: The marine ecosystem contains the most chitin in nature, which incubates a large number of microorganisms that can degrade and utilize chitin, therefore, the degradation of chitin by marine microbial chitinase is an important way to produce high value-added chitooligosaccharides. The aim...
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| Format: | Article |
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The editorial department of Science and Technology of Food Industry
2023-06-01
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| Series: | Shipin gongye ke-ji |
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| Online Access: | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2022090266 |
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| author | Qifa XIE Xiaoxu XUE Zhifa HUANG Haoyu MI Fuxiang HE Yaowei FANG Shu LIU |
| author_facet | Qifa XIE Xiaoxu XUE Zhifa HUANG Haoyu MI Fuxiang HE Yaowei FANG Shu LIU |
| author_sort | Qifa XIE |
| collection | DOAJ |
| description | Objective: The marine ecosystem contains the most chitin in nature, which incubates a large number of microorganisms that can degrade and utilize chitin, therefore, the degradation of chitin by marine microbial chitinase is an important way to produce high value-added chitooligosaccharides. The aim of this study was to screen a stable chitinase-producing strain from the marine mud in Lianyungang. Methods: The chitinase-producing strain Chi34 was screened by plate screening and flask shaking fermentation re-screening and identified by morphological analysis and 16S rDNA sequence analysis. Then, effects of temperature, pH, metal ions, EDTA and SDS on Chi34 chitinase were studied. Finally, the TLC experiment was taken to analyze products of colloidal chitin hydrolyzed by Chi34 chitinase. Result: The isolated strain Chi34 was identified as Gallaecimonas xiamenensis and the activity of Chi34 chitinase was 0.631 U/mL. The optimum pH and temperature for the chitinolytic activity were 6.0 and 35 ℃, respectively. Chi34 chitinase was highly activated by Na+, Ca2+, Mn2+, and K+, while inhibited by Cu2+, Fe3+, Ba2+, Zn2+, Cd2+, Co2+, EDTA, and SDS. The main products of chitin hydrolyzed by Chi34 chitinase were (GlcNAc)2 with little GlcNAc. Conclusion: The Chi34 chitinase could hydrolyze chitin to produce (GlcNAc)2 and GlcNAc, which would provide a certain theoretical reference for the high value utilization of chitin. |
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| language | zho |
| last_indexed | 2024-03-12T13:34:23Z |
| publishDate | 2023-06-01 |
| publisher | The editorial department of Science and Technology of Food Industry |
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| series | Shipin gongye ke-ji |
| spelling | doaj.art-6b980232a856493092947693a02628c32023-08-24T06:00:59ZzhoThe editorial department of Science and Technology of Food IndustryShipin gongye ke-ji1002-03062023-06-01441211612310.13386/j.issn1002-0306.20220902662022090266-12Screening, Identification and Characterization of a Marine Chitinase-Producing Strain Gallaecimonas xiamenensis Chi34Qifa XIE0Xiaoxu XUE1Zhifa HUANG2Haoyu MI3Fuxiang HE4Yaowei FANG5Shu LIU6Jiangsu Ocean University, Lianyungang 222000, ChinaKangda College of Nanjing Medical University, Lianyungang 222000, ChinaJiangsu Ocean University, Lianyungang 222000, ChinaJiangsu Ocean University, Lianyungang 222000, ChinaJiangsu Ocean University, Lianyungang 222000, ChinaJiangsu Ocean University, Lianyungang 222000, ChinaJiangsu Ocean University, Lianyungang 222000, ChinaObjective: The marine ecosystem contains the most chitin in nature, which incubates a large number of microorganisms that can degrade and utilize chitin, therefore, the degradation of chitin by marine microbial chitinase is an important way to produce high value-added chitooligosaccharides. The aim of this study was to screen a stable chitinase-producing strain from the marine mud in Lianyungang. Methods: The chitinase-producing strain Chi34 was screened by plate screening and flask shaking fermentation re-screening and identified by morphological analysis and 16S rDNA sequence analysis. Then, effects of temperature, pH, metal ions, EDTA and SDS on Chi34 chitinase were studied. Finally, the TLC experiment was taken to analyze products of colloidal chitin hydrolyzed by Chi34 chitinase. Result: The isolated strain Chi34 was identified as Gallaecimonas xiamenensis and the activity of Chi34 chitinase was 0.631 U/mL. The optimum pH and temperature for the chitinolytic activity were 6.0 and 35 ℃, respectively. Chi34 chitinase was highly activated by Na+, Ca2+, Mn2+, and K+, while inhibited by Cu2+, Fe3+, Ba2+, Zn2+, Cd2+, Co2+, EDTA, and SDS. The main products of chitin hydrolyzed by Chi34 chitinase were (GlcNAc)2 with little GlcNAc. Conclusion: The Chi34 chitinase could hydrolyze chitin to produce (GlcNAc)2 and GlcNAc, which would provide a certain theoretical reference for the high value utilization of chitin.http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2022090266chitinaseidentificationgallaecimonas xiamenensisenzymatic properties |
| spellingShingle | Qifa XIE Xiaoxu XUE Zhifa HUANG Haoyu MI Fuxiang HE Yaowei FANG Shu LIU Screening, Identification and Characterization of a Marine Chitinase-Producing Strain Gallaecimonas xiamenensis Chi34 Shipin gongye ke-ji chitinase identification gallaecimonas xiamenensis enzymatic properties |
| title | Screening, Identification and Characterization of a Marine Chitinase-Producing Strain Gallaecimonas xiamenensis Chi34 |
| title_full | Screening, Identification and Characterization of a Marine Chitinase-Producing Strain Gallaecimonas xiamenensis Chi34 |
| title_fullStr | Screening, Identification and Characterization of a Marine Chitinase-Producing Strain Gallaecimonas xiamenensis Chi34 |
| title_full_unstemmed | Screening, Identification and Characterization of a Marine Chitinase-Producing Strain Gallaecimonas xiamenensis Chi34 |
| title_short | Screening, Identification and Characterization of a Marine Chitinase-Producing Strain Gallaecimonas xiamenensis Chi34 |
| title_sort | screening identification and characterization of a marine chitinase producing strain gallaecimonas xiamenensis chi34 |
| topic | chitinase identification gallaecimonas xiamenensis enzymatic properties |
| url | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2022090266 |
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