TELEX HEBDOMADAIRE NR 95 DU 17.09.82 DESTINE A L'ENSEMBLE DES DELEGATIONS EXTERIEURES ET BUREAUX DE PRESS ET D'INFORMATION INDEPENDANTS DANS LES PAYS TIERS = WEEKLY MEMO NO. 95 FOR 17.09.82 TO FOREIGN DELEGATIONS AND PRESS BUREAUS OF THIRD COUNTRIES

<p>High-performance liquid chromatography (HPLC) results of (A) commercial surfactin sample, and (B) our extract surfactin of <i>B</i>. <i>subtilis</i> HH2 in LB medium. There were three main peaks (Peak A-C) of the extract and the surfactin standard in the same location.</p

The effects of BaP on mice behavior.

<p>An open field test was used to evaluate the animal’s behavioral performance, including total grids (A), number (B) and latency (C) of entry to the central area, and the length of time in the periphery zone (D). n = 9 per BaP-treated group, n = 10 in control. Values are mean ± SEM. *, <i>p</i> < 0.05 compared to CTL.</p

Effects of BaP on DNA methylation of the NR2B gene promoter.

<p>(A) Schematic diagram of selected CpG sites in the mouse NR2B gene promoter. Letters a-c represent the three regions in the NR2B promoter, respectively (Qiang et al., 2010). Each bar represents an individual CpG. The black bars represent a significant increase in methylation and the empty bars represent unchanged levels of methylation. The level of DNA methylation in the NR2B promoter was determined by pyrosequencing. The relative levels of NR2B methylation per CpG sites were assessed in the PFC (B) and hippocampus (C). Data are shown as the average of 5 separate experimental animals. Values are presented as the means ± SEM and represent the fold increase over the control group (control = 1). *, <i>p</i> < 0.05; **, <i>p</i> < 0.01 compared with control levels.</p

BaP exposure decreases the level of NR2B gene transcription in the PFC and hippocampus.

<p>Total RNA was isolated from the two brain regions. NR2B mRNA expression was determined by RT-qPCR, and 18S was used as an internal control. The results are presented as the average ratio vs. control ± SEM of seven independent experimental animals; *, <i>p</i> < 0.05; **, <i>p</i> < 0.01 compared with control levels.</p

BaP impaired short-time memory in the Y-maze test.

<p>(A) A schematic view of Y-maze with three arms, i.e., A, B, and C. (B) Y-maze test was used to evaluate short-term memory of the animals after BaP chronic exposure. Percentages of spontaneous alternation (%) were calculated and the values are presented as the mean ± SEM. *, <i>p</i> < 0.05 compared to CTL.</p

Recent Advances in Sustainable Antimicrobial Food Packaging: Insights into Release Mechanisms, Design Strategies, and Applications in the Food Industry

In response to the issues of foodborne microbial contamination and carbon neutrality goals, sustainable antimicrobial food packaging (SAFP) composed of renewable or biodegradable biopolymer matrices with ecofriendly antimicrobial agents has emerged. SAFP offers longer effectiveness, wider coverage, more controllability, and better environmental performance. Analyzing SAFP information, including the release profile of each antimicrobial agent for each food, the interaction of each biomass matrix with each food, the material size, form, and preparation methods, and its service quality in real foods, is crucial. While encouraging reports exist, a comprehensive review summarizing these developments is lacking. Therefore, this review critically examines recent release-antimicrobial mechanisms, kinetics models, preparation methods, and key regulatory parameters for SAFPs based on slow- or controlled-release theory. Furthermore, it discusses fundamental physicochemical characteristics, effective concentrations, advantages, release approaches, and antimicrobial and preservative effects of various materials in food simulants or actual food. Lastly, inadequacies and future trends are explored, providing practical references to regulate the movement of active substances in different media, reduce the reliance on petrochemical-based materials, and advance food packaging and preservation technologies

Expression and purification of the His-tag-BmTHY fusion protein.

<p>Samples were resolved by 12% SDS-polyacrylamide gel electrophoresis under reducing conditions. A: Expression of fusion protein in Rosetta (DE3); M: protein molecular weight marker (low); 1: Rossetta (pET-28a-BmTHY) without induction; 2: Rossetta (pET-28a-BmTHY) after induction; B: Purification of the His-tag fusion protein in Rosetta (DE3); M: protein molecular weight marker (low); 1: supernatant of <i>E.coli</i> Rosetta/pET-28a-BmTHY induced by IPTG after supersonic treatment; 2: purified fusion protein expressed in <i>E.coli</i> Rosetta.</p

The tertiary structure of BmTHY.

<p>(a)The tertiary structure of BmTHY(strands); (b)The tertiary structure of BmTHY(Molecular Surface).</p

Profile of silkworm <i>BmTHY</i> gene.

<p>(a) Schematic representation of <i>BmTHY</i> gene. (b) ORF sequence and predicted amino acid sequence of <i>BmTHY</i> gene. (c) BmTHY contains two intact THY domains.</p

Transcription and expression level of BmTHY in different development stages of <i>Bombyx mori</i>.

<p>(a) Analysis of BmTHY expression was performed by RT-PCR. Relative BmTHY expression was determined in relation to the corresponding BmTHY expression level in the silkworm moth: ΔΔC_T (stage) = ΔC_T (stage)−ΔC_T (egg); (b) Western blotting analysis of the expression levels of of BmTHY in different development stages. 1,egg;2,pupa; 3,larva;4,moth.</p