Water scarcity is an increasingly critical global issue, particularly in arid regions like Morocco. Innovative approaches, such as the use of alternative water sources like landfill leachate, offer promising solutions. In this study, phosphate washing sludge was used to treat landfill leachate with the aim of producing irrigation-quality water and recovering nitrogen from the resulting sediment. A total of 40 L of raw leachate was treated with three concentrations of phosphate washing sludge (25%, 37%, and 50%). This volume was processed at the laboratory scale as a proof of concept for potential larger-scale applications. After 24 to 36 h of mixing and agitation, the mixture underwent sedimentation, yielding clear supernatants and nitrogen-rich sludge pellets. These pellets showed a significant increase in organic matter content, from 6.4% to 13.5%, representing an enhancement of 110.9%, thus demonstrating partial leachate depollution and organic matter enrichment. Microbiological analyses revealed a 98.9% reduction in fecal streptococci. The supernatants met irrigation water standards in terms of pH and electrical conductivity, and phytotoxicity tests on maize seeds confirmed their suitability for irrigation. Additionally, the recovered nitrogen-rich sediment presents a valuable input for composting and soil amendment.

Pectinases are a group of enzymes widely applied in agri-food processes. This study aimed to isolate and characterize pectinase-producing yeasts and yeast-like fungi from soil and humus samples collected in a Moroccan argan forest, a region characterized by arid to semi-arid climatic conditions, with emphasis on screening and evaluating their pectinolytic activity. Among nine isolated strains, four exhibited detectable pectinolytic activity on pectin agar medium. Two promising isolates were molecularly identified by ITS region sequencing as Coniochaeta pulveracea PX765016 and Coniochaeta ligniaria PX765017. Notably, C. pulveracea PX765016 showed the highest pectinolytic potential, with a pectinolytic degradation index of 4.2 on pectin agar. This strain also exhibited maximal pectinase production after 96 h of submerged fermentation in YEPD medium under optimized conditions of pH 4, 30–35 °C, and 0.5% (w/v) pectin. The crude enzyme obtained under these conditions exhibited a specific activity of 559.90 ± 11.62 U/mg. The enzyme was subsequently subjected to sequential purification comprising ammonium sulfate precipitation, dialysis, and gel filtration chromatography on a Sephadex G-100 column, yielding a 2.99-fold purification with a final recovery of 14%. The purified enzyme exhibited optimal activity at pH 6.0 and 40–55 °C, with a reaction time of 20 min. Kinetic analysis of pectin hydrolysis revealed a Michaelis–Menten constant (Km) of 7.33 mg pectin per mL and a maximum reaction velocity (Vmax) of 1666.7 U/mg. To the best of our knowledge, this is the first report of pectinase production by a member of the genus Coniochaeta, and the first characterization of pectinase activity from C. pulveracea.