Purification and Characterization of the Enzyme Fucoidanase from <i>Cobetia amphilecti</i> Utilizing Fucoidan from <i>Undaria pinnatifida</i>
Fucoidanase is an unstable enzyme with high specificity that requires a large about of time to screen it from microorganisms. In this study, enzymatic hydrolysis was used to produce low-molecular-weight fucoidan from microorganisms via the degradation of high-molecular-weight fucoidan without damage...
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MDPI AG
2023-04-01
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| Series: | Foods |
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| author | Shu Liu Qiukuan Wang Zhenwen Shao Qi Liu Yunhai He Dandan Ren Hong Yang Xiang Li |
| author_facet | Shu Liu Qiukuan Wang Zhenwen Shao Qi Liu Yunhai He Dandan Ren Hong Yang Xiang Li |
| author_sort | Shu Liu |
| collection | DOAJ |
| description | Fucoidanase is an unstable enzyme with high specificity that requires a large about of time to screen it from microorganisms. In this study, enzymatic hydrolysis was used to produce low-molecular-weight fucoidan from microorganisms via the degradation of high-molecular-weight fucoidan without damage to the sulfate esterification structure of oligosaccharide. The microbial strain HN-25 was isolated from sea mud and was made to undergo mutagenicity under ultraviolet light. Fucoidanase was extracted via ultrasonication and its enzymatic activity was improved via optimization of the ultrasonic conditions. The enzymatic properties and degradation efficiency of fucoidanase were characterized. The microbial strain HN-25 is a Gram-negative aerobic and rod-shaped-cell bacterium, and therefore was identified as <i>Cobetia amphilecti</i> via 16s rDNA. The results proved that fucoidanase is a hydrolytic enzyme with a molecular weight of 35 kDa and with high activity and stability at 30 °C and pH 8.0. The activity of fucoidanase was significantly enhanced by sodium and calcium ions and inhibited by a copper ion and ethylenediaminetetraacetate (EDTA). There was a significant decrease in the molecular weight of fucoidan after enzymatic hydrolysis. The low-molecular-weight fuicodan was divided into four fractions, mainly concentrated at F3 (20~10 kDa) and F4 (≤6 kDa). These consequences suggest that fucoidanase obtained from <i>Cobetia amphilecti</i> is stable and efficient and could be a good tool in the production of bioactive compounds. |
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| last_indexed | 2024-03-11T05:36:54Z |
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| spelling | doaj.art-765ef120586344d9a9a5fe02af290a852023-11-17T16:42:55ZengMDPI AGFoods2304-81582023-04-01127155510.3390/foods12071555Purification and Characterization of the Enzyme Fucoidanase from <i>Cobetia amphilecti</i> Utilizing Fucoidan from <i>Undaria pinnatifida</i>Shu Liu0Qiukuan Wang1Zhenwen Shao2Qi Liu3Yunhai He4Dandan Ren5Hong Yang6Xiang Li7Colleage of Food Science and Technology, Huazhong Agriculture University, Wuhan 430070, ChinaKey Laboratory of Aquatic Products Processing and Utilization of Liaoning Province, National R and D Branch Center for Seaweed Processing, College of Food Science and Engineering, Dalian Ocean University, Dalian 116023, ChinaQingdao Seawit Life Science Co., Ltd., Qingdao 370200, ChinaBureau of Science and Technology of Qingdao West Area, Qingdao 266555, ChinaKey Laboratory of Aquatic Products Processing and Utilization of Liaoning Province, National R and D Branch Center for Seaweed Processing, College of Food Science and Engineering, Dalian Ocean University, Dalian 116023, ChinaKey Laboratory of Aquatic Products Processing and Utilization of Liaoning Province, National R and D Branch Center for Seaweed Processing, College of Food Science and Engineering, Dalian Ocean University, Dalian 116023, ChinaColleage of Food Science and Technology, Huazhong Agriculture University, Wuhan 430070, ChinaKey Laboratory of Aquatic Products Processing and Utilization of Liaoning Province, National R and D Branch Center for Seaweed Processing, College of Food Science and Engineering, Dalian Ocean University, Dalian 116023, ChinaFucoidanase is an unstable enzyme with high specificity that requires a large about of time to screen it from microorganisms. In this study, enzymatic hydrolysis was used to produce low-molecular-weight fucoidan from microorganisms via the degradation of high-molecular-weight fucoidan without damage to the sulfate esterification structure of oligosaccharide. The microbial strain HN-25 was isolated from sea mud and was made to undergo mutagenicity under ultraviolet light. Fucoidanase was extracted via ultrasonication and its enzymatic activity was improved via optimization of the ultrasonic conditions. The enzymatic properties and degradation efficiency of fucoidanase were characterized. The microbial strain HN-25 is a Gram-negative aerobic and rod-shaped-cell bacterium, and therefore was identified as <i>Cobetia amphilecti</i> via 16s rDNA. The results proved that fucoidanase is a hydrolytic enzyme with a molecular weight of 35 kDa and with high activity and stability at 30 °C and pH 8.0. The activity of fucoidanase was significantly enhanced by sodium and calcium ions and inhibited by a copper ion and ethylenediaminetetraacetate (EDTA). There was a significant decrease in the molecular weight of fucoidan after enzymatic hydrolysis. The low-molecular-weight fuicodan was divided into four fractions, mainly concentrated at F3 (20~10 kDa) and F4 (≤6 kDa). These consequences suggest that fucoidanase obtained from <i>Cobetia amphilecti</i> is stable and efficient and could be a good tool in the production of bioactive compounds.https://www.mdpi.com/2304-8158/12/7/1555enzymatic activityenzymatic propertiesfucoidanaselow molecular weightultrasonication |
| spellingShingle | Shu Liu Qiukuan Wang Zhenwen Shao Qi Liu Yunhai He Dandan Ren Hong Yang Xiang Li Purification and Characterization of the Enzyme Fucoidanase from <i>Cobetia amphilecti</i> Utilizing Fucoidan from <i>Undaria pinnatifida</i> Foods enzymatic activity enzymatic properties fucoidanase low molecular weight ultrasonication |
| title | Purification and Characterization of the Enzyme Fucoidanase from <i>Cobetia amphilecti</i> Utilizing Fucoidan from <i>Undaria pinnatifida</i> |
| title_full | Purification and Characterization of the Enzyme Fucoidanase from <i>Cobetia amphilecti</i> Utilizing Fucoidan from <i>Undaria pinnatifida</i> |
| title_fullStr | Purification and Characterization of the Enzyme Fucoidanase from <i>Cobetia amphilecti</i> Utilizing Fucoidan from <i>Undaria pinnatifida</i> |
| title_full_unstemmed | Purification and Characterization of the Enzyme Fucoidanase from <i>Cobetia amphilecti</i> Utilizing Fucoidan from <i>Undaria pinnatifida</i> |
| title_short | Purification and Characterization of the Enzyme Fucoidanase from <i>Cobetia amphilecti</i> Utilizing Fucoidan from <i>Undaria pinnatifida</i> |
| title_sort | purification and characterization of the enzyme fucoidanase from i cobetia amphilecti i utilizing fucoidan from i undaria pinnatifida i |
| topic | enzymatic activity enzymatic properties fucoidanase low molecular weight ultrasonication |
| url | https://www.mdpi.com/2304-8158/12/7/1555 |
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