Characterisation of High Alkaline-Tolerant Novel Ulvan Lyase from <i>Pseudoalteromonas agarivorans</i>: Potential Applications of Enzyme Derived Oligo-Ulvan as Anti-Diabetic Agent
Green algae, particularly <i>Ulva</i> species, are rich in complex polysaccharides, such as ulvan, which have significant potential for biotechnological applications. However, the biochemical properties of ulvan depolymerised products remain underexplored. The enzymatic depolymerisation...
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MDPI AG
2024-12-01
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| author | Navindu Dinara Gajanayaka Eunyoung Jo Minthari Sakethanika Bandara Svini Dileepa Marasinghe Chinmayee Bawkar Yeon-Ju Lee Gun-Hoo Park Chulhong Oh Youngdeuk Lee |
| author_facet | Navindu Dinara Gajanayaka Eunyoung Jo Minthari Sakethanika Bandara Svini Dileepa Marasinghe Chinmayee Bawkar Yeon-Ju Lee Gun-Hoo Park Chulhong Oh Youngdeuk Lee |
| author_sort | Navindu Dinara Gajanayaka |
| collection | DOAJ |
| description | Green algae, particularly <i>Ulva</i> species, are rich in complex polysaccharides, such as ulvan, which have significant potential for biotechnological applications. However, the biochemical properties of ulvan depolymerised products remain underexplored. The enzymatic depolymerisation of ulvan has garnered attention owing to its cost advantages over alternative methods. Nevertheless, the biochemical characterisation of ulvan lyases, specifically those belonging to the polysaccharide lyase family 25 (PL25), is limited. In this study, we identified and biochemically characterised a novel PL25 ulvan lyase, PaUL25, which functions optimally at pH 10. Additionally, we explored the alpha (α)-glucosidase inhibitory properties of ulvan depolymerised products. PaUL25 exhibited optimum activity at 35 °C in Tris-HCl buffer (pH 10). Moreover, enzyme activity was enhanced by more than 150% in the presence of Mn<sup>2+</sup> metal ions at and below concentrations of 10 mM. The endolytic action of PaUL25 produced ulvan oligosaccharides with degrees of polymerisation of 2 and 4 as its end products. Partially and completely hydrolysed ulvan oligosaccharides exhibited α-glucosidase inhibitory activity, with half inhibitory concentration IC<sub>50</sub> values of 3.21 ± 0.13 and 2.51 ± 0.19 mg/mL, respectively. These findings expand our understanding of PL25 and highlight the pharmaceutical potential of ulvan oligosaccharides, particularly as antidiabetic agents. |
| format | Article |
| id | doaj-art-ad36f13e3d2d44709889bfb97a5a2421 |
| institution | DOAJ |
| issn | 1660-3397 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj-art-ad36f13e3d2d44709889bfb97a5a24212025-08-20T02:57:26ZengMDPI AGMarine Drugs1660-33972024-12-01221257710.3390/md22120577Characterisation of High Alkaline-Tolerant Novel Ulvan Lyase from <i>Pseudoalteromonas agarivorans</i>: Potential Applications of Enzyme Derived Oligo-Ulvan as Anti-Diabetic AgentNavindu Dinara Gajanayaka0Eunyoung Jo1Minthari Sakethanika Bandara2Svini Dileepa Marasinghe3Chinmayee Bawkar4Yeon-Ju Lee5Gun-Hoo Park6Chulhong Oh7Youngdeuk Lee8Jeju Bio Research Center, Korea Institute of Ocean Science and Technology (KIOST), Jeju-si 63349, Republic of KoreaJeju Bio Research Center, Korea Institute of Ocean Science and Technology (KIOST), Jeju-si 63349, Republic of KoreaJeju Bio Research Center, Korea Institute of Ocean Science and Technology (KIOST), Jeju-si 63349, Republic of KoreaJeju Bio Research Center, Korea Institute of Ocean Science and Technology (KIOST), Jeju-si 63349, Republic of KoreaDepartment of Marine Technology & Convergence Engineering, KIOST School, University of Science and Technology, Daejeon 34113, Republic of KoreaDepartment of Marine Technology & Convergence Engineering, KIOST School, University of Science and Technology, Daejeon 34113, Republic of KoreaJeju Bio Research Center, Korea Institute of Ocean Science and Technology (KIOST), Jeju-si 63349, Republic of KoreaJeju Bio Research Center, Korea Institute of Ocean Science and Technology (KIOST), Jeju-si 63349, Republic of KoreaJeju Bio Research Center, Korea Institute of Ocean Science and Technology (KIOST), Jeju-si 63349, Republic of KoreaGreen algae, particularly <i>Ulva</i> species, are rich in complex polysaccharides, such as ulvan, which have significant potential for biotechnological applications. However, the biochemical properties of ulvan depolymerised products remain underexplored. The enzymatic depolymerisation of ulvan has garnered attention owing to its cost advantages over alternative methods. Nevertheless, the biochemical characterisation of ulvan lyases, specifically those belonging to the polysaccharide lyase family 25 (PL25), is limited. In this study, we identified and biochemically characterised a novel PL25 ulvan lyase, PaUL25, which functions optimally at pH 10. Additionally, we explored the alpha (α)-glucosidase inhibitory properties of ulvan depolymerised products. PaUL25 exhibited optimum activity at 35 °C in Tris-HCl buffer (pH 10). Moreover, enzyme activity was enhanced by more than 150% in the presence of Mn<sup>2+</sup> metal ions at and below concentrations of 10 mM. The endolytic action of PaUL25 produced ulvan oligosaccharides with degrees of polymerisation of 2 and 4 as its end products. Partially and completely hydrolysed ulvan oligosaccharides exhibited α-glucosidase inhibitory activity, with half inhibitory concentration IC<sub>50</sub> values of 3.21 ± 0.13 and 2.51 ± 0.19 mg/mL, respectively. These findings expand our understanding of PL25 and highlight the pharmaceutical potential of ulvan oligosaccharides, particularly as antidiabetic agents.https://www.mdpi.com/1660-3397/22/12/577ulvan lyasepolysaccharide lyase family 25alpha glucosidase inhibition |
| spellingShingle | Navindu Dinara Gajanayaka Eunyoung Jo Minthari Sakethanika Bandara Svini Dileepa Marasinghe Chinmayee Bawkar Yeon-Ju Lee Gun-Hoo Park Chulhong Oh Youngdeuk Lee Characterisation of High Alkaline-Tolerant Novel Ulvan Lyase from <i>Pseudoalteromonas agarivorans</i>: Potential Applications of Enzyme Derived Oligo-Ulvan as Anti-Diabetic Agent Marine Drugs ulvan lyase polysaccharide lyase family 25 alpha glucosidase inhibition |
| title | Characterisation of High Alkaline-Tolerant Novel Ulvan Lyase from <i>Pseudoalteromonas agarivorans</i>: Potential Applications of Enzyme Derived Oligo-Ulvan as Anti-Diabetic Agent |
| title_full | Characterisation of High Alkaline-Tolerant Novel Ulvan Lyase from <i>Pseudoalteromonas agarivorans</i>: Potential Applications of Enzyme Derived Oligo-Ulvan as Anti-Diabetic Agent |
| title_fullStr | Characterisation of High Alkaline-Tolerant Novel Ulvan Lyase from <i>Pseudoalteromonas agarivorans</i>: Potential Applications of Enzyme Derived Oligo-Ulvan as Anti-Diabetic Agent |
| title_full_unstemmed | Characterisation of High Alkaline-Tolerant Novel Ulvan Lyase from <i>Pseudoalteromonas agarivorans</i>: Potential Applications of Enzyme Derived Oligo-Ulvan as Anti-Diabetic Agent |
| title_short | Characterisation of High Alkaline-Tolerant Novel Ulvan Lyase from <i>Pseudoalteromonas agarivorans</i>: Potential Applications of Enzyme Derived Oligo-Ulvan as Anti-Diabetic Agent |
| title_sort | characterisation of high alkaline tolerant novel ulvan lyase from i pseudoalteromonas agarivorans i potential applications of enzyme derived oligo ulvan as anti diabetic agent |
| topic | ulvan lyase polysaccharide lyase family 25 alpha glucosidase inhibition |
| url | https://www.mdpi.com/1660-3397/22/12/577 |
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