Mining Arylsulfatase from Genome-Scale Metabolic Pathways of Pseudoalteromonas sp. SR43-6 and Its Agar-Based Desulfurization Applications.

Arylsulfatase catalyzes the cleavage of sulfate ester bonds and plays a role in agar desulfation, thereby enhancing agar gel strength and quality. While studying the desulfurization pathway in Pseudoalteromonassp. SR43-6, a sequence encoding a potential arylsulfatase-Pseudoalteromonas Ars (Ps-Ars)-was found. The enzyme, with p-nitrophenyl sulfate as a substrate, exhibited optimal activity at 35 °C and pH 8.0. Its relative activity (206 U/mg) exceeded that of the recently identified arylsulfatases. Four hundred units of the enzyme removed 86.4% of sulfate groups from Gelidium amansii agar in 4 h, whereas 800 U of the enzyme removed 71.3% of sulfate groups from Gracilaria lemaneiformis agar in 8 h. After enzymatic treatment, G. amansii agar gel strength was enhanced by 32%, and a similar improvement was observed in G. lemaneiformis agar gel strength. Enzymatic agar desulfurization offers mild, quality-retaining, and environmentally friendly advantages, augmenting industrial application prospects.