Investigation of Maillard reaction involvement in the steam processing of Panax Notoginseng root

Purpose: To explore the possible mechanism of Maillard reaction (MR) involvement in the steam processing of Panax notoginseng (PN) root.Methods: PN root was soaked in water for 24 h and then steamed at 100 °C using an autoclave for 1, 2, 3, 4, 5 and 6 h, respectively. Several indicators associated with MR during steam processing were measured. The pH and absorbance at 420 nm (A420) of samples were measured using a pH meter and an ultraviolet-visible spectrophotometer, respectively. The contents of 5-hydroxy-methyl-furfural (5-HMF) and sugars were determined by high performance liquid chromatography (HPLC) while amino acids were evaluated using an automatic amino acid analyzer.Results: During PN root steam processing (0 - 6 h), pH value gradually decreased from 6.35 ± 0.02 to 5.88 ± 0.03 while A420 value gradually increased from 0.23 ± 0.01 to 0.44 ± 0.02. The levels of reducing sugars (maltose and glucose) and amino acids (aspartic acid, glutamate, cysteine, lysine and arginine) in PN root decreased after steaming for 6 h. However, the content of 5-HMF in PN root increased with increase in steaming time.Conclusion: The results indicate that MR occurs during steam processing of PN root, and the reaction mechanism might be closely related to the reaction between the reducing sugars and amino acids.Keywords: Panax notoginseng, Steaming, Reducing sugars, Amino acids, Maillard reactio

Poly[diaqua­bis(μ3-1H-benzimidazole-5,6-dicarboxyl­ato-κ4 N 3:O 5,O 5′:O 6)bis­(μ2-1H,3H-benzimidazolium-5,6-dicarboxyl­ato-κ3 O 5,O 5′:O 6)digadolinium(III)]

In the title complex, [Gd2(C9H4N2O4)2(C9H5N2O4)2(H2O)2]n, two of the benzimidazole-5,6-dicarboxyl­ate ligands are pro­ton­ated at the imidazole groups. Each GdIII ion is coordinated by six O atoms and one N atom from five ligands and one water mol­ecule, displaying a distorted bicapped trigonal-prismatic geometry. The GdIII ions are linked by the carboxyl­ate groups and imidazole N atoms, forming a layer parallel to (001). These layers are further connected by O—H⋯O and N—H⋯O hydrogen bonds into a three-dimensional supra­molecular network

Lite it fly: An All-Deformable-Butterfly Network

Most deep neural networks (DNNs) consist fundamentally of convolutional and/or fully connected layers, wherein the linear transform can be cast as the product between a filter matrix and a data matrix obtained by arranging feature tensors into columns. The lately proposed deformable butterfly (DeBut) decomposes the filter matrix into generalized, butterflylike factors, thus achieving network compression orthogonal to the traditional ways of pruning or low-rank decomposition. This work reveals an intimate link between DeBut and a systematic hierarchy of depthwise and pointwise convolutions, which explains the empirically good performance of DeBut layers. By developing an automated DeBut chain generator, we show for the first time the viability of homogenizing a DNN into all DeBut layers, thus achieving an extreme sparsity and compression. Various examples and hardware benchmarks verify the advantages of All-DeBut networks. In particular, we show it is possible to compress a PointNet to < 5% parameters with < 5% accuracy drop, a record not achievable by other compression schemes.Comment: 7 pages, 3 figures, accepted as a brief paper in IEEE Transactions on Neural Networks and Learning Systems (TNNLS

Hemi(4,4′-bipyridinium) hexa­fluorido­phosphate bis­(4-amino­benzoic acid) 4,4′-bipyridine monohydrate

In the title compound, 0.5C10H10N2 2+·PF6 −·C10H8N2·2C7H7NO2·H2O, the cation is located on a center of symmetry. The crystal structure is determined by a complex three-dimensional network of inter­molecular O—H⋯O, O—H⋯N, N—H⋯N and N—H⋯F hydrogen bonds. π–π stacking inter­actions between neighboring pyridyl rings are also present; the centroid–centroid distance is 3.643 (5) Å. The hexa­fluoridophosphate anion is disordered over two positions with site-occupancy factors of ca 0.6 and 0.4

HutZ is required for biofilm formation and contributes to the pathogenicity of Edwardsiella piscicida

International audienceAbstractEdwardsiella piscicida is a severe fish pathogen. Haem utilization systems play an important role in bacterial adversity adaptation and pathogenicity. In this study, a speculative haem utilization protein, HutZEp, was characterized in E. piscicida. hutZEp is encoded with two other genes, hutW and hutX, in an operon that is similar to the haem utilization operon hutWXZ identified in V. cholerae. However, protein activity analysis showed that HutZEp is probably not related to hemin utilization. To explore the biological role of HutZEp, a markerless hutZEp in-frame mutant strain, TX01ΔhutZ, was constructed. Deletion of hutZEp did not significantly affect bacterial growth in normal medium, in iron-deficient conditions, or in the presence of haem but significantly retarded bacterial biofilm growth. The expression of known genes related to biofilm growth was not affected by hutZEp deletion, which indicated that HutZEp was probably a novel factor promoting biofilm formation in E. piscicida. Compared to the wild-type TX01, TX01ΔhutZ exhibited markedly compromised tolerance to acid stress and host serum stress. Pathogenicity analysis showed that inactivation of hutZEp significantly impaired the ability of E. piscicida to invade and reproduce in host cells and to infect host tissue. In contrast to TX01, TX01ΔhutZ was defective in blocking host macrophage activation. The expression of hutZEp was directly regulated by the ferric uptake regulator Fur. This study is the first functional characterization of HutZ in a fish pathogen, and these findings suggested that HutZEp is essential for E. piscicida biofilm formation and contributes to host infection

Poly[[aqua­(μ2-oxalato)(μ2-2-oxido­pyridinium-3-carboxylato)dysprosium(III)] monohydrate]

In the title complex, {[Dy(C6H4NO3)(C2O4)(H2O)]·H2O}n, the DyIII ion is coordinated by seven O atoms from two 2-oxidopyridinium-3-carboxylate ligands, two oxalate ligands and one water mol­ecule, displaying a distorted bicapped trigonal-prismatic geometry. The carboxyl­ate groups of the 2-oxidopyridinium-3-carboxylate and oxalate ligands link dysprosium metal centres, forming layers parallel to (100). These layers are further connected by inter­molecular O—H⋯O hydrogen-bonding inter­actions involving the coordin­ated water mol­ecules, forming a three-dimensional supra­molecular network. The uncoordinated water mol­ecule is involved in N—H⋯O and O—H⋯O hydrogen-bonding inter­actions within the layer