42 research outputs found

    VIGS-mediated <i>MPF2</i> silencing phenocopies <i>MPF2</i>-RNAi.

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    <p>(<b>A</b>) An intact WT flower. (<b>B</b>) An intact <i>MPF2</i>-VIGS flower. Bars = 1 mm. (<b>C</b>) I<sub>2</sub>-KI stained pollen from WT. (<b>D</b>) I<sub>2</sub>-KI stained pollen from <i>MPF2</i>-VIGS. Active pollen is blue and sterile pollen is tawny. Bars = 100 µm. (<b>E</b>) Floral calyx epidermal cells of WT. (<b>F</b>) Floral calyx epidermal cells of <i>MPF2</i>-VIGS. Bars = 20 µm. (<b>G</b>) Size of calyx surface (gray column) and epidermal cells (white column) of the floral calyx in WT and <i>MPF2</i>-VIGS (“VIGS”). 20 cells and 20 calyces were analyzed for both WT and <i>MPF2</i>-VIGS samples. Mean values and standard deviation are presented. (<b>H</b>) Gene expression analysis of <i>MPF2</i>-RNAi and -VIGS. Expression of <i>MPF2</i> was compared between <i>MPF2</i>-RNAi flowers (R1–R3), <i>MPF2</i>-VIGS flowers (V1–V3) and wild-type (WT) <i>Physalis</i> via qRT-PCR analysis. The severe <i>MPF2</i> residual in VIGS was only 6% of that in the wild-type (WT), while in the RNAi the <i>MPF2</i> residual was 14% of that in the wild-type (WT). <i>PFACTIN</i> was used as an internal control. (<b>I</b>) <i>MPF2</i> expression was evaluated in two floral organs of VIGS flowers. Expression of <i>MPF2</i> in <i>MPF2</i>-RNAi (gray column), <i>MPF2</i>-VIGS (white column) was compared with that in the wild-type (WT, black column). The gene expression in the calyx of the WT was set as 1, and <i>PFACTIN</i> was used as an internal control. The experiments were repeated with three independent biological samples. Mean expression values and standard deviation are presented.</p

    VIGS-mediated <i>MPF3</i> silencing phenocopies <i>MPF3</i>-RNAi.

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    <p>(<b>A</b>) An intact WT small flower bud. (<b>B</b>) An intact WT flower bud. (<b>C</b>) A WT flower. (<b>D</b>) A WT ICS. (<b>E</b>) An intact <i>MPF3</i>-VIGS small flower bud. (<b>F</b>) An intact <i>MPF3</i>-VIGS flower bud. (<b>G</b>) An <i>MPF3</i>-VIGS flower. (<b>H</b>) An <i>MPF3</i>-VIGS ICS. (<b>I</b>) An <i>MPF3</i>-RNAi flower. Bars = 1 mm in <b>A</b>, <b>B</b>, <b>C</b>, <b>E</b>, <b>F</b>, <b>G,</b> and <b>I</b>. Bars = 5 mm in <b>D</b> and <b>H</b>. (<b>J</b>) <i>MPF3</i> was silenced using a VIGS approach. <i>MPF3</i> expression was evaluated in five floral organs of VIGS flowers. (<b>K</b>) <i>MPF3</i> was silenced using an RNAi approach. <i>MPF3</i> expression was evaluated in five floral organs of RNAi flowers. Total RNA from the indicated mutated floral organs was subjected to qRT-PCR. Gene expression in pedicels of WT samples were set as 1, and <i>PFACTIN</i> was used as an internal control. The dark gray column stands for the gene expression in WT organs light gray column indicates the gene expression in the organs of the mutants, as indicated. The experiments were repeated with three independent biological samples. Mean expression values and standard deviation are presented.</p

    Seedling survival and infected efficiency in different treatments.

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    <p>Seedling survival and infected efficiency in different treatments.</p

    Facile Method To Prepare Microcapsules Inspired by Polyphenol Chemistry for Efficient Enzyme Immobilization

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    In this study, a method inspired by polyphenol chemistry is developed for the facile preparation of microcapsules under mild conditions. Specifically, the preparation process includes four steps: formation of the sacrificial template, generation of the polyphenol coating on the template surface, cross-linking of the polyphenol coating by cationic polymers, and removal of the template. Tannic acid (TA) is chosen as a representative polyphenol coating precursor for the preparation of microcapsules. The strong interfacial affinity of TA contributes to the formation of polyphenol coating through oxidative oligomerization, while the high reactivity of TA is in charge of reacting/cross-linking with cationic polymer polyethylenimine (PEI) through Schiff base/Michael addition reaction. The chemical/topological structures of the resultant microcapsules are simultaneously characterized by scanning electron microscopy (SEM), transmission electron microscopy (TEM), Fourier Transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), <i>etc.</i> The wall thickness of the microcapsules could be tailored from 257 ± 20 nm to 486 ± 46 nm through changing the TA concentration. The microcapsules are then utilized for encapsulating glucose oxidase (GOD), and the immobilized enzyme exhibits desired catalytic activity and enhanced pH and thermal stabilities. Owing to the structural diversity and functional versatility of polyphenols, this study may offer a facile and generic method to prepare microcapsules and other kinds of functional porous materials

    Combination of Redox Assembly and Biomimetic Mineralization To Prepare Graphene-Based Composite Cellular Foams for Versatile Catalysis

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    Graphene-based materials with hierarchical structures and multifunctionality have gained much interest in a variety of applications. Herein, we report a facile, yet universal approach to prepare graphene-based composite cellular foams (GCCFs) through combination of redox assembly and biomimetic mineralization enabled by cationic polymers. Specifically, cationic polymers (e.g., polyethyleneimine, lysozyme, etc.) could not only reduce and simultaneously assemble graphene oxide (GO) into cellular foams but also confer the cellular foams with mineralization-inducing capability, enabling the formation of inorganic nanoparticles (e.g., silica, titania, silver, etc.). The GCCFs show highly porous structure and appropriate structural stability, where nanoparticles are well distributed on the surface of the reduced GO. Through altering polymer/inorganic pairs, a series of GCCFs are synthesized, which exhibit much enhanced catalytic performance in enzyme catalysis, heterogeneous chemical catalysis, and photocatalysis compared to nanoparticulate catalysts

    Robust and Recyclable Two-Dimensional Nanobiocatalysts for Biphasic Reactions in Pickering Emulsions

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    In this study, a facile, yet effective surface-engineering method was reported to confer graphene oxide (GO) nanosheets with amphiphilic feature and numerous binding sites toward enzymes for biphasic reactions in Pickering emulsions. Briefly, the surface of GO nanosheet is first modified and simultaneously reduced by polydopamine to endow with catechol groups. A portion of catechol groups is utilized to anchor zeolitic imidazolate framework 8 (ZIF-8) nanoparticles onto the polydopamine-modified graphene oxide (P-rGO) nanosheets through Zn<sup>2+</sup>–catechol coordination. The remaining uncoordinated catechol groups in P-rGO nanosheets are utilized to immobilize lipase onto the P-rGO nanosheets through chemical conjugation. The resulting two-dimensional P-rGO/ZIF-8/Lipase nanobiocatalysts with an enzyme loading percent values of 34.05–48.75% could be spontaneously assembled at the oil/water interface, which were then utilized to catalyze the hydrolysis of water-insoluble <i>p</i>-nitrophenyl palmitate (<i>p</i>-NPP) into water-soluble <i>p</i>-nitrophenol (<i>p</i>-NP). The Pickering emulsions, which were robustly stabilized by P-rGO/ZIF-8/Lipase, facilitated the diffusion of <i>p</i>-NP from the oil/water interface to aqueous phase, acquiring an enzymatic activity recovery of ∼60%. Moreover, P-rGO/ZIF-8/Lipase exhibited remarkably enhanced stabilities against multiple reuses and various harsh conditions compared with free lipase, GO/Lipase, and P-rGO/Lipase, showing great potential in practical applications

    Sequence comparison of EtLPP1, -2, and -3.

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    <p>(A) the three conserved motifs in LPP family are shown on top of the alignment, three domains in deduced amino acid sequences of EtLPP1, -2 and -3 are listed. The predicted transmembrane topology of each of the three proteins is shown in B. (B) arrows represent glycolated sites. Those amino acids that are essential for activity within the three conserved domains are indicated by letters. Regions of hydrophobic amino acids are denoted 1 to 6, as predicted by Split 4.0.</p
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