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Endophytes can be developed into biocontrol agents and can be fungi, bacteria, or archaea that live inside plant tissues without causing symptoms of disease. Phomopsis liquidambari is an endophytic fungus that plays an important ecosystem role as a biofertilizer by helping its host obtain soil nitrogen. How this fungus impacts N mineralization and microbial communities is little known. Our understanding of soil nutrient transformations and soil-plant-microbe interactions in Phomopsis liquidambari -crop versus conventional crop systems is incomplete. This study provided a better understanding of the effect of Phomopsis liquidambari on nitrogen mineralization and investigated the interaction between P . liquidambari and nitrogen, which in turn will be helpful to the farmer in reducing the required amount of soil N fertilizer. This change in N availability in maize soil will have significant implications for soil productivity and plant N utilization, especially in N-limited soils, and significantly reduce the required amount of soil N fertilizer. The effect of P . liquidambari on N mineralization in maize soil was investigated by treating it with four levels of N (urea) at rates of 0, 1.25, 2.5, and 3.75 g of nitrogen. N-mineralization was determined by the anaerobic incubation method. Were stored for 7 days in an incubator at a constant 37 C. A colorimetric microplate procedure was used for NH 4 + -N analysis. A significant increase in the available NH 4 + -N contents was reported in soil maize ( Zea mays L.) inoculated with P . liquidambari , which increased by 80%. A significant increase in N-mineralization was observed under all N conditions. This work highlighted the importance of the fungal endophyte for soil N-mineralization with lower N input. Using this fungal agent will almost certainly help reduce fertilizer input.

Enterobacter aerogenes Lipase used in this study was heterologously expressed by Pichia pastoris. D152, D152H, D151H, D113, 724), three types of anion resins (D380, D 301R, D311) and two types of chelating r activities of the immobilized (EAL). According to the results, D152 was selected for haydrolysis activity as the immobilized enzyme (EAL). The D152 was selected for hydrolysis activity since the immobilized lipase exhibited the highest specific hydrolysis activity. Immobilization conditions (enzyme loading, immobilization time, temperature, and pH value). The best results were enzyme loading 4mg/g, time 80min, temperature 30°C, and buffer pH 8; and under the optimized conditions the immobilization efficiency was 95% and the specific activity was 532841.34 U/g.esins (D401, D418) were sieved as support matrix. Hydrolysis assay was employed to evaluate the specific.