Abstract
Green algae, particularly Ulva 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 Mn2+ 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 IC50 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.