Hwanglester3612

09, 0.14 and 0.19, respectively.Lignocellulosic raw materials are being utilised in many industrial sectors as a natural source of interesting biopolymers. In the present research, tomato plant agri-waste, were subjected to an enzymatic treatment (pectinase, hemicellulase, xylanase and laccase) with the aim of recovering polymeric matrices contained therein and obtain a good quality fibre. The cellulose content in the enzyme-treated fibres was enriched of 25% compared to the untreated, and a fair reduction in hemicellulose and lignin was registered. Morphological analyses at SEM demonstrated the cleanliness and fibrillation of fibres. Moreover, the thermal profile, water absorption and pulp viscosity of fibres was strongly affected by the composition changes. The paperboard manufactured from an enzymatically treated sample showed increased stiffness when subjected to tensile testing respect to the control. Therefore, the use of enzyme in fibre pulping has a potential application in the design of sustainable materials.Fatty acyl desaturase 2 (fads2) is a rate-limiting enzyme in long chain polyunsaturated fatty acids (LC-PUFAs) biosynthesis. In mammals, the lipid metabolism is modulated by a transcription factor, peroxisome proliferator-activated receptor alpha β (pparαβ); however, the detailed mechanism via pparαβ regulates fads2 remains unclear in fish. In the present study, we identified the sequence features of Trachinotus ovatus fatty acyl desaturase 2a (Tofads2a) and fatty acyl desaturase 2b (Tofads2b), which both encoded 442 amino acid polypeptides containing cytochrome-b5-like domains and three representative histidine-rich domains. The Phylogenetic and genome organization analyses revealed characteristic phylogeny the majority of fads2s exhibited a highly conserved exon/intron architecture. Tissue expression patterns by quantitative real-time PCR (qRT-PCR) showed that the two Tofads2s were prominently expressed in the brain. A nutritional study indicated that the transcription of the two Tofads2s was significantly implicated by treatment with a 1 1 ratio of fish oil soybean oil (FOSO) in the liver and brain. Furthermore, functional characterization in yeast demonstrated that both Tofads2a and Tofads2b possessed Δ4/Δ5/Δ8 desaturation activity. Furthermore, promoter activity assays showed that the expressions of the two Tofads2s were actively regulated by pparαβ. Moreover, mutation analyses showed that the M1 and M4/M5 binding sites of pparαβ were functionally vital for binding to Tofads2a and Tofads2b promoters, respectively. Transcriptional activities of the two Tofads2s promoters were significantly reduced after targeted mutation of M1 or M4/M5. Electrophoretic mobile shift assays (EMSAs) verified that pparαβ interacted with the M1 binding site in Tofads2a promoter to accommodate Tofads2a transcription. Briefly, pparαβ plays an important role in Tofads2 expression and may promote the LC-PUFAs biosynthesis by regulating the expression of two Tofads2s.Bio-based nanomaterials with antimicrobial functions hold promise in replacing petroleum-based packaging for food preservation. A nanocellulose-based hybrid film with antimicrobial properties was developed from sugarcane bagasse and nisin. Cellulose nanofibrils (CNFs) were prepared from sugarcane bagasse pulp by mechanical grinding, and mixed with nisin to prepare CNFs/nisin nanohybrid films. The concentration of nisin has a remarkable influence on the mechanical, light transmission, gas barrier, and antimicrobial properties of these films. CNFs/nisin hybrid films with 1920 mg/L nisin exhibit good light transmission, relatively high tensile strength, low oxygen permeability, and low water vapor transmission rates. This hybrid film was used as a liner of low-density polyethylene plastic packaging for ready-to-eat ham; it completely inhibited Listeria monocytogenes during 7 days of storage at 4 °C. Opicapone Such novel CNFs/nisin nanohybrid films are expected to expand the application of bagasse nanocellulose in active packaging for food preservation.This study reports a ≅12.5 kDa protein tetrachloro-1,4-benzoquinone reductase (CpsD) from Bacillus cereus strain AOA-CPS1 (BcAOA). CpsD is purified to homogeneity with a total yield of 35% and specific activity of 160 U·mg-1 of protein. CpsD showed optimal activity at pH 7.5 and 40 °C. The enzyme was found to be functionally stable between pH 7.0-7.5 and temperature between 30 °C and 35 °C. CpsD activity was enhanced by Fe2+ and inhibited by sodium azide and SDS. CpsD followed Michaelis-Menten kinetic exhibiting an apparent vmax, Km, kcat and kcat/Km values of 0.071 μmol·s-1, 94 μmol, 0.029 s-1 and 3.13 × 10-4 s-1·μmol-1, respectively, for substrate tetrachloro-1,4-benzoquinone. The bioinformatics analysis indicated that CpsD belongs to the PCD/DCoH superfamily, with specific conserved protein domains of pterin-4α-carbinolamine dehydratase (PCD). This study proposed that CpsD catalysed the reduction of tetrachloro-1,4-benzoquinone to tetrachloro-p-hydroquinone and released the products found in phenylalanine hydroxylation system (PheOHS) via a Ping-Pong or atypical ternary mechanism; and regulate expression of phenylalanine 4-monooxygenase by blocking reverse flux in BcAOA PheOHS using a probable Yin-Yang mechanism. The study also concluded that CpsD may play a catalytic and regulatory role in BcAOA PheOHS and pentachlorophenol degradation pathway.Mutation in TMEM240 is suggested to cause SCA21, but the specific mechanism has not been clarified. The subcellular localization, specific biological function, and corresponding mechanism of action of TMEM240 have also not been delineated. In this study, the mRNA and protein expression of TMEM240 were assessed using qPCR and western blotting, respectively. Live cell imaging was used to establish the sub-cellular location of TMEM240, and electron microscopy was used to determine the morphology and distribution of TMEM240 in the cell. TMEM240 was specifically expressed in the neurons. Exogenous TMEM240 formed a multilayered cell structure, which we refer to as TMEM240-Body (T240-Body). T240-Body was separated and purified by centrifugation and filtration. An anchor protein His-tagged-GFP-BP on Ni-NTA agarose was used to pull down T240-GFP binding proteins. Both the N-terminal and the C-terminal of TMEM240 were confirmed to be inside the T240-Body. Co-localization experiments suggested that peroxisomes might contribute to T240-Body formation, and the two transmembrane regions of TMEM240 appear to be essential for formation of the T240-Body.