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Crown sheath rot, caused by the ascomycete Gaeumannomyces graminis var. graminis that infects the root and the base of the culm of rice, causes early grains maturation, tiller death and reduced yield. As a paucity of information exists in the literature on the rice‐G. graminis var. graminis interaction at the microscopic level, this study aimed to gain novel insights into the infection process of this pathogen in the root and culm of rice using both light and scanning electron microscopy. In the roots, the fungus initially colonized the epidermal, exodermal and sclerenchyma cells. At 15 days after inoculation (dai), fungal hyphae colonized the cortex and clusters of perithecia were observed in the roots. At 20 dai, the fungus reached the central cylinder, and an intense fungal colonization at the base of the culm was observed that resulted in the formation of a mycelial mat on both adaxial and abaxial surfaces of the leaf sheaths. At 25 dai, fungal growth was noticed in the parenchyma cells, vascular bundles and airspaces. Perithecia emerged through the base of prophyllum and from the first leaf sheath at 30 dai. The results of this study provide new insights into the infection process of G. graminis var. graminis in rice and may help to find better control measures in reducing crown sheath rot development.  相似文献   
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In this work, the free lipase Eversa® Transform 2.0 was used as a catalyst for enzymatic glycerolysis reaction in a solvent-free system. The product was evaluated by nuclear magnetic resonance (1H NMR) and showed high conversion related to hydroxyl groups. In sequence, the product of the glycerolysis was used as stabilizer and biopolyol for the synthesis of poly(urea–urethane) nanoparticles (PUU NPs) aqueous dispersion by the miniemulsion polymerization technique, without the use of a further surfactant in the system. Reactions resulted in stable dispersions of PUU NPs with an average diameter of 190 nm. After, the formation of the PUU NPs in the presence of concentrated lipase Eversa® Transform 2.0 was studied, aiming the lipase immobilization on the NP surface, and a stable enzymatic derivative with diameters around 231 nm was obtained. The hydrolytic enzymatic activity was determined using ρ-nitrophenyl palmitate (ρ-NPP) and the immobilization was confirmed by morphological analysis using transmission electron microscopy and fluorescence microscopy.

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