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In vitro digestion and human gut microbiota fermentation of longan pulp polysaccharides as affected by Lactobacillus fermentum fermentation.

This study investigated the effect of Lactobacillus fermentum fermentation treatment on the gastrointestinal digestion and fermentation in vitro of polysaccharides from longan pulp. Polysaccharide isolated from unfermented and fermented longan pulp named LP and LP-F, respectively. The molecular weight of LP-F declined from 109.62 ± 10.66 kDa to 51.46 ± 6.26 kDa while that of LP declined from 221.63 ± 2.41 kDa to 69.68 ± 2.36 kDa with gastrointestinal digestion. At same time, the reducing sugars content of LP and LP-F were both increased significantly. In addition, after 48 h gut microbiota fermentation, there were more total short chain fatty acids and acetic acid, as well as more Enterococcus, Bifidobacterium, and Clostridium in LP-F fermentation culture than those in LP fermentation culture. Moreover, LP-F fermentation culture showed lower pH value and less residual carbohydrate percentage than that of LP. These results indicated that LP-F is easier than LP to be fermented by human gut microbiota.

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Purification and partial biochemical characterization of recombinant lactate dehydrogenase 1 (LDH-1) of the white shrimp Litopenaeus vannamei.

Lactate dehydrogenase (LDH) is a key enzyme to produce energy during hypoxia by anaerobic glycolysis. In the white shrimp Litopenaeus vannamei, two protein subunits (LDH-1 and LDH-2) were previously identified, deduced from two different transcripts that come from the same LDH gene by processing via mutually exclusive alternative splicing. LDH-1 contains exon five and LDH-2 contains exon six and the two proteins differ only in 15 amino acid residues. Both subunits were independently cloned and overexpressed in E. coli as a fusion protein containing a chitin binding domain. Previously, recombinant LDH-2 was successfully purified and characterized, but LDH-1 was insoluble and aggregated forming inclusion bodies. We report the production of soluble LDH-1 by testing different pHs in the buffers used to lyse the bacterial cells before the purification step and the characterization of the purified protein to show that the cDNA indeed codes for a functional and active protein. The recombinant native protein is a homotetramer of approximately 140 kDa composed by 36 kDa subunits and has higher affinity for pyruvate than for lactate. LDH-1 has an optimum pH of 7.5 and is stable between pH 8.0 and 9.0; pH data analysis showed two pKa values of 6.1 ± 0.15 and 8.8 ± 0.15 suggesting a histidine and asparagine, respectively, involved in the active site. The enzyme optimal temperature was 44 °C and it was stable between 20 and 60 °C. LDH-1 was slightly activated by NaCl, KCl and MgCl and fully inhibited by ZnCl.

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Development of a quantitative assay for 2´-fucosyllactose via one-pot reaction with α1,2-fucosidase and l-fucose dehydrogenase.

2'-Fucosyllactose (2'-FL) is the most abundant milk oligosaccharide in human breast milk and it has several benefits for infant health. The quantification of 2'-FL in breast milk or in samples from other sources generally requires lengthy analyses. These methods cannot be used to simultaneously detect 2'-FL in numerous samples, which would be more time-efficient. In this study, two genes, namely α1,2-fucosidase from Xanthomonas manihotis and l-fucose dehydrogenase from Pseudomonas sp. no. 1143, were identified, cloned and overexpressed in E. coli. The recombinant enzymes were produced as 6 × His-tagged proteins and were purified to homogeneity using Ni affinity chromatography. The purified α1,2-fucosidase and l-fucose dehydrogenase are monomers with molecular masses of 63 kDa and 36 kDa, respectively. Both enzymes have sufficiently high activities in phosphate-buffered saline (pH 7.0) at 37 °C, making it possible to develop a coupled enzyme reaction in a single buffer system for the quantitative determination of 2'-FL in a large number of samples simultaneously. This method can be used to quantify 2'-FL in infant formulas and in samples collected from different phases of the biotechnological production of this oligosaccharide. Furthermore, the method is applicable for the rapid screening of active variants during the development of microbial strains producing 2'-FL.

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Blimp-1 is involved in B cell activation and maturation in Nile tilapia (Oreochromis niloticus).

B lymphocyte-induced maturation protein 1 (Blimp-1), a transcription factor containing zinc finger, is required and sufficient to trigger terminal differentiation of B cells in mammals. The Blimp-1 (OnBlimp-1) from Nile tilapia (Oreochromis niloticus) was identified and characterized its expression pattern during B cell activation and maturation. The cDNA of OnBlimp-1 open reading frame is 2547 bp encoding a protein of 848 amino acids and the predicted molecular weight is 93.36 kDa. OnBlimp-1 contains a SET domain and five ZnF_C2H2 domains, which shares high homology with that of other species. OnBlimp-1 transcription was detected in all examined tissues with high expression in the spleen (SPL). Analysis of sorted lymphocyte populations, including IgM and IgM cells from peripheral blood (PBL), SPL and anterior kidney (AK), indicated that the OnBlimp-1 transcription was highly expressed in the IgM B cells. Upon LPS stimulation, OnBlimp-1 expression was up-regulated in tissues of PBL, SPL and AK significantly. The expression of OnBlimp-1, as well as the secreted IgM, was significantly up-regulated in the SPL and AK leukocytes stimulated with anti-OnIgM monoclonal antibody and LPS in vitro, respectively. Above results suggest that OnBlimp-1, a cytokine regulating the terminal differentiation of activated B cells to antibody-secreting cells, is likely to play important roles in B cell activation and maturation in Nile tilapia.

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Atypical organic-solvent tolerant bacterial hormone sensitive lipase-like homologue EstAG1 from Staphylococcus saprophyticus AG1: Synthesis and characterization.

Biocatalysts exerting activity against ester bonds have a broad range of applications in modern biotechnology. Some of the most industrially relevant enzymes of this type are lipolytic and their market is predicted to uphold leadership up till 2024. In this study, a novel bacterial hormone-sensitive lipase-like (bHSL) family homologue, designated EstAG1, was discovered by mining gDNA of bacteria isolated from fat contaminated soil in Lithuania. Putative lipolytic enzyme was cloned, overexpressed in E. coli, purified and characterized determining its biochemical properties. While the true physiological role of the discovered leaderless, ~36 kDa enzyme is unknown, metal-activated EstAG1 possessed optima at 45-47.5 °C, pH 7.5-8, with a generally intermediate activity profile between esterases and lipases. Furthermore, EstAG1 was hyperactivated by ethanol, dioxane and DMSO, implicating that it could be industrially applicable enzyme for the synthesis of valuable products such as biodiesel, flavor esters, etc. Sequence analysis and structure modeling revealed that the highest sequence homology of EstAG1 with the closest structurally and functionally described protein makes up only 26%. It was also revealed that EstAG1 has some differences in the bHSL family-characteristic conserved sequence motives. Therefore, EstAG1 presents interest both in terms of biotechnological applications and basic research.

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Intestinal epithelial cell apoptosis due to a hemolytic toxin from Vibrio vulnificus and protection by a 36 kDa glycoprotein from Rhus verniciflua Stokes.

Rhus verniciflua stokes (RVS) has been used as a functional food to cure inflammatory diseases in Korea. In the present study, we carry out an investigation of the cellular mechanism of a 36 kDa glycoprotein isolated from RVS fruit (RVS glycoprotein) during the apoptosis of human gastrointestinal epithelial HCT116 cells induced by the hemolytic toxin (VvhA) produced by V. vulnificus. Recombinant protein (r) VvhA produced by V. vulnificus stimulated apoptosis by activating the phosphorylation of protein kinase C (PKC) through the production of intracellular reactive oxygen species (ROS). However, RVS glycoprotein significantly inhibited the level of ROS production and PKC activation in rVvhA-stimulated HCT116 cells. Interestingly, we found that RVS glycoprotein has inhibitory effects on the phosphorylation of c-Jun N-terminal kinase (JNK) and nuclear factor-kappa B (NF-κB), which are responsible for the expression of Bax and cleaved caspase-3 in HCT116 cells treated with rVvhA, respectively. On the basis of these results, we suggest that RVS glycoprotein blocks mitochondrial apoptotic cell death induced by rVvhA via the inhibition of ROS-mediated signaling events in HCT116 cells.

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Speciation of zinc in fish feed by size exclusion chromatography coupled to inductively coupled plasma mass spectrometry - using fractional factorial design for method optimisation and mild extraction conditions.

Zinc (Zn) is an element essential to all living organisms and it has an important role as a cofactor of several enzymes. In fish, Zn deficiency has been associated with impaired growth, cataracts, skeletal abnormalities and reduced activity of various Zn metalloenzymes. Fish meal and fish oil traditionally used in salmon feed preparation are being replaced by plant-based ingredients. Zinc additives are supplemented to salmon feed to ensure adequate Zn levels, promoting good health and welfare in Atlantic salmon (Salmo salar). The main objective of the present study was to evaluate Zn species found in an Atlantic salmon feed. This work describes a Zn extraction method that was optimized using a fractional factorial design (FFD), whereby the effect of six factors could be studied by performing only eight experiments. The effects of the type of extraction solution and its molar concentration, pH, presence of sodium dodecyl sulphate, temperature and extraction time on Zn extraction were investigated. Mild extraction conditions were chosen in order to keep the Zn species intact. Total Zn (soluble fractions and non-soluble fractions) was determined by inductively coupled plasma mass spectrometry (ICP-MS). The highest Zn recovery was obtained using 100 mM Tris-HCl, pH 8.5 at a temperature of 4 °C for 24 h where the total Zn in soluble fraction and non-soluble fraction was 9.9 ± 0.2% and 98 ± 6%, respectively. Zinc speciation analysis (on the soluble fractions) was further conducted by size exclusion inductively coupled plasma mass spectroscopy (SEC-ICP-MS). The SEC-ICP-MS method provided qualitative and semi-quantitative information regarding Zn species present in the soluble fractions of the feed. Four Zn-containing peaks were found, each with different molecular weights: Peak 1 (high molecular weight - ≥600 kDa), peak 2 and peak 3 (medium molecular weight - 32 to 17 kDa) were the least abundant (1-6%), while peak 4 (low molecular weight - 17 to 1.36 kDa) was the most abundant (84-95%).

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Opposing roles of inter-α-trypsin inhibitor heavy chain 4 in recurrent pregnancy loss.

The mechanism behind an increased risk of recurrent pregnancy loss (RPL) remains largely unknown. In our previous study, we identified that inter-α-trypsin inhibitor heavy chain 4 (ITI-H4) is highly expressed at a modified molecular weight of 36 kDa in serum derived from RPL patients. Yet, the precise molecular mechanism and pathways by which the short form of ITI-H4 carries out its function remain obscure.

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Fecal Calprotectin.

Calprotectin is a 36kDa member of the S100 family of proteins. It is derived predominantly from neutrophils and has direct antimicrobial effects and a role within the innate immune response. Calprotectin is found in various body fluids in proportion to the degree of any existing inflammation and its concentration in feces is about six times that of plasma. Measurement of fecal calprotectin is a useful surrogate marker of gastrointestinal inflammation. It has a high negative predictive value in ruling out inflammatory bowel disease (IBD) in undiagnosed, symptomatic patients and a high sensitivity for diagnosing the disease making it useful as a tool for prioritising endoscopy. In patients with known IBD, fecal calprotectin can be a useful tool to assist management, providing evidence of relapse or mucosal healing to enable therapy to be intensified or reduced. There are a number of commercial calprotectin assays with marked difference in performance as judged by external quality assessment and at present no standardised reference material exists. Various factors may affect results including age, medication and day to day variation. Laboratories should therefore be mindful of the characteristics of their own assay and factors that may affect results.

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Enhanced thermostability of halo-tolerant glutaminase from Bacillus licheniformis ATCC 14580 by immobilization onto nano magnetic cellulose sheet and its application in production of glutamic acid.

A halo-tolerant glutaminase gene (BlglsA) was isolated from Bacillus licheniformis. Heterologous expression of BlglsA revealed that it encodes for a 36 kDa protein containing 327 amino acid residues. The purified enzyme showed optimal activity at a pH of 9.5 while 35 °C was found to be the optimum temperature. The enzyme retained about 92 and 97% stability at pH 12 and temperature (40 °C) respectively. Subsequent immobilization of BlglsA on nano magnetic cellulose sheet (NMCS) led to an enhanced tolerance to higher temperature. NMCS-BlglsA showed optimum activity at 45 °C, although it was stable even at 60 °C. NaCl tolerance (≥90% in 0.3 M) was almost similar to BlglsA and NMCS-BlglsA. The metal ions Fe (5 mM) and Mn (2.5 mM) improved the BlglsA relative activity by 61 and 48%, respectively. In contrast, 5 mM Mn was found suitable to enhance the activity of NMCS-BlglsA up to 72%. The production of glutamic acid by NMCS-BlglsA was 1.61 g/l in 48 h. Reusability test of NMCS-BlglsA showed 76 and 35% retention of the actual activity after 4th and 7th cycle, respectively. Such remarkable biochemical properties of NMCS-BlglsA make it an attractive enzyme for food industries.

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