Search results for: 33kDa
#33051012 2020/08/31 To Up
Expression of a novel α-glucosidase from Aspergillus neoniger in Pichia pastoris and its efficient recovery for synthesis of isomaltooligosaccharides.A gene conferring α-glucosidase (AG) with high transglycosylation activity from Aspergillus neoniger (a non-niger strain belonging to section Nigri) was cloned and expressed in Pichia pastoris. As the cDNA construction retained intronic portions due to alternative splicing, the exonic portions of the gene were stitched using restriction digestion and overlap extension PCR. Pre-determined open-loop exponential feeding strategies were evaluated for methanol dosage to improve the recombinant enzyme synthesis during high-cell density cultivation in 5 L bioreactor. Specific growth rate of 0.1 h resulted in the highest enzyme activity of 182.3 mU/mL in the supernatant, whereas the activity of 3.8 U/g dry cell weight was obtained in the cell pellet. There was negligible enzyme activity in the cell lysate, indicating that approximately 80 % accumulation of total enzyme is in the periplasm. Later, this unreleased fraction was extracted to 90 % yield using 25 mM cysteine. The enzyme was purified and validated using western blot analysis and MS/MS profile. The SDS PAGE analysis revealed three bands corresponding to 80, 38, and 33 kDa indicating the multimeric nature of the enzyme. Thus, obtained enzyme was utilized in synthesis of a potential prebiotic molecule, isomaltooligosaccharides (IMOs), which can be used as a sweetener and bulk filler in the food industry. This is the first report to demonstrate challenges in cloning and expression of transglycosylating α-glucosidase from Aspergillus neoniger.
Sandeep Kumar, Sarma Mutturi
1369 related Products with: Expression of a novel α-glucosidase from Aspergillus neoniger in Pichia pastoris and its efficient recovery for synthesis of isomaltooligosaccharides.100 µg300 units1 mL1 mg251mg
#32987191 2020/09/25 To Up
Genetic diversity of Merozoite surface protein 1-42 (MSP1-42) fragment of Plasmodium vivax from Indonesian isolates: Rationale implementation of candidate MSP1 vaccine.Morbidity and mortality related to malaria in Indonesia are attributed to both Plasmodium falciparum and P. vivax parasites. In addition to vaccines for P. falciparum, vaccines against P. vivax are urgently needed for the prevention of the disease. An extensively studied antigen is the carboxyl-terminus of the 42 kDa region of P. vivax merozoite surface protein-1 (PvMSP1-42). The design of a vaccine based on this antigen requires an understanding of the extent of polymorphism. However, there is no information on the genetic diversity of the antigen in Indonesia. This study aimed to profile the diversity of PvMSP1-42 and its two subdomains (PvMSP1-33 and PvMSP1-19) among Indonesian P. vivax isolates. A total of 52 P. vivax-infected blood samples were collected from patients in two different endemic areas in Indonesia: Banjarmasin (Kalimantan) and Sumba Timur (Nusa Tenggara Timur). The polymorphic characteristics and natural selection of PvMSP1-42 were analyzed using the DnaSP, MEGA, and Structure software. Thirty distinct haplotypes of PvMSP1-42 were identified. They displayed amino acid changes compared to the reference PVP01 sequence. Most of the mutations were concentrated in the 33 kDa fragment. PvMSP1-42 of the Indonesian isolates appeared to be under positive selection. Recombination may also play a role in the resulting genetic diversity of PvMSP1. In conclusion, PvMSP1-42 of Indonesian isolates displayed allelic polymorphisms caused by mutation, recombination, and positive selection. These results will aid the understanding of the P. vivax population in Indonesia and to develop a PvMSP1 based vaccine against P. vivax.
E Elsa Herdiana Murhandarwati, E Henny Herningtyas, Puspawati Puspawati, Fridolina Mau, Shen-Bo Chen, Hai-Mo Shen, Jun-Hu Chen
2917 related Products with: Genetic diversity of Merozoite surface protein 1-42 (MSP1-42) fragment of Plasmodium vivax from Indonesian isolates: Rationale implementation of candidate MSP1 vaccine.1 mg200 1 mg50 5 G0.2 mg96 Tests/kit96 Tests/kit0.1 mg200
#31499109 2019/09/06 To Up
Tetrastigma hemsleyanum tubers polysaccharide ameliorates LPS-induced inflammation in macrophages and Caenorhabditis elegans.Tetrastigma hemsleyanum Diels et Gilg, a rare herbal plant native to China, possesses high medicinal value. More researches have focused on the flavones in the tubers of Tetrastigma hemsleyanum whereas polysaccharides attract few attentions. In this study, a purified polysaccharide (TTP-1) with the average molecular weights of 478.33 kDa was extracted from Tetrastigma hemsleyanum and conducted multiple analysis to identify its structural information. In vitro, TTP-1 could suppress the inflammation, cytotoxicity, genotoxicity, mitochondrial dysfunction and oxidative damage induced by LPS in RAW264.7 cells. Meanwhile, TTP-1 could attenuate inflammation via COX-2, iNOS, MAPKs pathways and ameliorate oxidative damage through Nrf2-Keap1, Sirt1-FoxO1 pathways in RAW264.7 cells. In vivo, the inflammation induced by LPS triggered the suppression of survival ratio and growing development, as well as the restrain of athletic ability in Caenorhabditis elegans. The treatment of TTP-1 reversed the situation induced by LPS. In a word, TTP-1 could ameliorate LPS-induced inflammation both in vitro and in vivo.
Qiang Chu, Ruoyi Jia, Meng Chen, Yonglu Li, Xin Yu, Yaxuan Wang, Wen Chen, Xiang Ye, Yangyang Liu, Yong Jiang, Xiaodong Zheng
2731 related Products with: Tetrastigma hemsleyanum tubers polysaccharide ameliorates LPS-induced inflammation in macrophages and Caenorhabditis elegans.16-22 Sample Kit50 ul1216 Arrays/Slide8 Sample Kit100ug1 mg4 Sample Kit 100ul4 Arrays/Slide1-8 Sample Kit
#31450350 2019/04/29 To Up
Ultrasonic-assisted citrus pectin modification in the bicarbonate-activated hydrogen peroxide system: Chemical and microstructural analysis.The modified pectin (MP) showed the improved functional properties than the native one. The aim of present study was to develop the ultrasonic accelerated bicarbonate-hydrogen peroxide system for pectin modification to generate short fragments with advanced bioactive properties. The depolymerization effects of this system on the physicochemical properties, structural features, and bioactivity of the degraded fragments were studied systematically. The results indicated that the molecular weight of pectin was reduced drastically from 1088 kDa to 33 kDa within 50 min under an optimized condition (M-M = 1:2.5, 50 °C, and ultrasound intensity = 11.4 W/cm). The resulting fragments also showed lower degree of methoxylation and rheological viscosity. The investigation on the sample structures and active oxygen species demonstrated that the highly active O species generated from HCO of NaHCO-HO acted preferentially on the GalA backbone in the HG region, while the RG-I region was maintained; and ultrasound enhanced the degradation efficiency via both chemical effects (increasing the transformation of free radicals) and mechanical effects (disaggregating polysaccharide clusters). The atomic force microscope (AFM) imaging directly verified the branched-chain morphology of pectin and the small-strand degradation fragments. Moreover, ultrasound and NaHCO-HO treatment induced high galactose content in the degraded products, contributing to an improved inhibitory activity against A549 lung cancer cells, as shown by MTT assay.
Weiwei Hu, Shiguo Chen, Dongmei Wu, Jiaqi Zheng, Xingqian Ye
2329 related Products with: Ultrasonic-assisted citrus pectin modification in the bicarbonate-activated hydrogen peroxide system: Chemical and microstructural analysis.1 kit1 kit200 assays0.1mg1 lt2 x 96 well plate 1000 ml
#30936047 2019/03/29 To Up
Molecular cloning, characterization, and expression level analysis of a marine teleost homolog of catalase from big belly seahorse (Hippocampus abdominalis).Organisms possess a cellular antioxidant defense system inclusive of ROS scavengers to maintain the homeostasis of antioxidant levels. Catalase is a major ROS scavenger enzyme that plays a significant role in the antioxidant defense mechanism of organisms by reducing toxic hydrogen peroxide molecules into a nontoxic form of oxygen and water with a high turnover rate. In the present study, we performed molecular and functional characterization of the catalase homolog from Hippocampus abdominalis (HaCat). The HaCat cDNA sequence was identified as a 1578 bp ORF (open reading frame) that encodes a polypeptide of 526 amino acids with 59.33 kDa molecular weight. Its estimated pI value is 7.7, and it does not have any signal sequences. HaCat shared a conserved domain arrangement including the catalase proximal active site signature and heme ligand signature domain with the previously identified catalase counterparts. Phylogenetic analysis displayed close evolutionary relationships between HaCat and catalases from other teleost fish. According to our qPCR results, ubiquitous expression of HaCat transcripts were observed in all the tested tissues with high expression in the kidney followed by liver. Significant modulations of HaCat transcription were observed in blood, liver, and kidney tissues post-challenge with Streptococcus iniae, Edwardsiella tarda, poly I:C, and LPS. Peroxidase activity of recombinant HaCat (rHaCat) was evaluated using an ABTS assay and the ROS removal effect was further confirmed by oxidative DNA damage protection and cell viability assays. The rHaCat showed more than 97% activity over a temperature and pH range of 10 °C-40 °C and 5 to 6, respectively. The above results suggest that HaCat plays an indispensable role in the oxidative homeostasis of the seahorse during pathogenic attack.
Sarithaa Sellaththurai, Thanthrige Thiunuwan Priyathilaka, Jehee Lee
2983 related Products with: Molecular cloning, characterization, and expression level analysis of a marine teleost homolog of catalase from big belly seahorse (Hippocampus abdominalis).100 μg100ug1 module 25 MG100 assays1 module1 module100 300 units25 mg
#30817966 2019/02/25 To Up
Structural and biological properties of polysaccharides from lotus root.To investigate the structure, in vitro digestibility and activity of polysaccharides from lotus root, their main fractions named LRPs were isolated and purified by gel filtration chromatography. Structural analyses indicated that: LRPs were α‑(1 → 6)‑d‑heteroglucans mainly composed of Glc-(1→, →6)-Glc-(1→, →6)-Gal-(1→, →4,6)-Gal-(1→ and →3,6)-Glc-(1→ at a molar ratio of 1.00: 4.33: 0.83: 0.13: 1.14; the total molar percentage of other monosaccharides in LRPs, including Man, Rha, GalA and Ara, was 8.10%; the molecular weights of LRPs was in the range of 1.33 kDa to 5.30 kDa. According to the change of molecular weight and the productions of reducing sugar and free monosaccharide, the simulated experiments of salivary, gastric and intestinal digestion confirmed that LRPs were almost undigestible. Moreover, LRPs showed the scavenging ability against DPPH and hydroxyl radicals, the growth inhibition ability against SGC7901 and HepG2 cancer cells in vitro, and the immunostimulating effect on the NO and TNF-α productions of macrophages in vitro. LRPs nearly remain their initial structure and activities in upper gastrointestinal tract and have health-improving potentials.
Yang Yi, Xiao-Yun Huang, Zhao-Tian Zhong, Fei Huang, Shu-Yi Li, Li-Mei Wang, Ting Min, Hong-Xun Wang
1547 related Products with: Structural and biological properties of polysaccharides from lotus root.500 MG10 ug25 mg5ml10 mg100ug100ul50 mg1000 25 mg2ml96T
#30716334 2019/02/01 To Up
The Role of SurA PPIase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpT.SurA is a conserved ATP-independent periplasmic chaperone involved in the biogenesis of outer-membrane proteins (OMPs). Escherichia coli SurA has a core domain and two peptidylprolyl isomerase (PPIase) domains, the role(s) of which remain unresolved. Here we show that while SurA homologues in early proteobacteria typically contain one or no PPIase domains, the presence of two PPIase domains is common in SurA in later proteobacteria, implying an evolutionary advantage for this domain architecture. Bioinformatics analysis of >350,000 OMP sequences showed that their length, hydrophobicity and aggregation propensity are similar across the proteobacterial classes, ruling out a simple correlation between SurA domain architecture and these properties of OMP sequences. To investigate the role of the PPIase domains in SurA activity, we deleted one or both PPIase domains from E.coli SurA and investigated the ability of the resulting proteins to bind and prevent the aggregation of tOmpA (19 kDa) and OmpT (33 kDa). The results show that wild-type SurA inhibits the aggregation of both OMPs, as do the cytoplasmic OMP chaperones trigger factor and SecB. However, while the ability of SurA to bind and prevent tOmpA aggregation does not depend on its PPIase domains, deletion of even a single PPIase domain ablates the ability of SurA to prevent OmpT aggregation. The results demonstrate that the core domain of SurA endows its generic chaperone ability, while the presence of PPIase domains enhances its chaperone activity for specific OMPs, suggesting one reason for the conservation of multiple PPIase domains in SurA in proteobacteria.
Julia R Humes, Bob Schiffrin, Antonio N Calabrese, Anna J Higgins, David R Westhead, David J Brockwell, Sheena E Radford
1364 related Products with: The Role of SurA PPIase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpT.1mg102
#30583005 2018/12/22 To Up
Portulaca elatior root contains a trehalose-binding lectin with antibacterial and antifungal activities.Lectins are carbohydrate-binding proteins broadly distributed in plants and have several biological functions, including antimicrobial action. Portulaca elatior is a Caatinga plant whose chemical composition and biotechnological potential have not been extensively studied. In this work, a lectin was isolated from P. elatior root extract and evaluated for antimicrobial activity. The P. elatior root lectin (PeRoL) showed native molecular mass of 33 kDa, pI 3.8 and is comprised of two subunits of 15 kDa linked by disulfide bonds. No sequence similarities with Viridiplantae proteins were observed. The PeRoL hemagglutinating activity (HA) was not affected by heating and was detected in a pH ranging from 4.0 to 8.0. Trehalose was identified as an endogenous inhibitor of PeRoL present in the roots. Bacteriostatic activity was detected against Enterococcus faecalis, Pseudomonas aeruginosa and Staphylococcus aureus (minimal inhibitory concentration of 8.1, 32.5 and 4.06 μg/mL, respectively). PeRoL induced the death of Candida albicans, Candida parapsilosis, Candida krusei, and Candida tropicalis cells, with a minimal fungicidal concentration of 16 μg/mL. The lectin (100 μg/mL) was not cytotoxic to human peripheral blood mononuclear cells (PBMCs) and did not show hemolytic activity. In conclusion, the roots of P. elatior contain a trehalose-binding, thermostable, and antimicrobial lectin.
José Dayvid Ferreira da Silva, Suéllen Pedrosa da Silva, Pollyanna Michelle da Silva, Amanda Mota Vieira, Larissa Cardoso Correa de Araújo, Thâmarah de Albuquerque Lima, Ana Patrícia Silva de Oliveira, Lidiane Vasconcelos do Nascimento Carvalho, Maira Galdino da Rocha Pitta, Moacyr Jesus Barreto de Melo Rêgo, Irapuan Oliveira Pinheiro, Russolina Benedeta Zingali, Maria do Socorro de Mendonça Cavalcanti, Thiago Henrique Napoleão, Patrícia Maria Guedes Paiva
2162 related Products with: Portulaca elatior root contains a trehalose-binding lectin with antibacterial and antifungal activities.1000 TESTS/0.65ml100 μg48 assays0.2 mg25 mg1 kit10 mg100 ml200ug500 MG25 Tests
#30572050 2018/12/17 To Up
Self-assembly behavior of the keratose proteins extracted from oxidized Ovis aries wool fibers.Water soluble keratose proteins were obtained from an Ovis Aries wool using peracetic acid oxidation. The wool samples and the extracted keratose proteins were characterized by using FTIR, XRD, SEM and TGA techniques. Fractions of α-keratose (MW = 43-53 kDa) along with protein species with molecular weights between 23 kDa and 33 kDa were identified in the SDS-PAGE analysis result of the extracted protein mixture. DLS and AFM experiments indicated that self-assembled globular nanoparticles with diameters between 15 nm and 100 nm formed at 5 mg/ml keratose concentration. On the other hand, upon incubation of 10 w % keratose solutions at 37 °C and 50 °C, interconnected keratose hydrogels with respective storage modulus (G') values of 0.17 ± 0.03 kPa and 3.7 ± 0.5 kPa were obtained. It was shown that the keratose hydrogel prepared at 37 °C supported L929 mouse fibroblast cell proliferation which suggested that these keratose hydrogels could be promising candidates in soft tissue engineering applications.
Efecan Pakkaner, Damla Yalçın, Berk Uysal, Ayben Top
1488 related Products with: Self-assembly behavior of the keratose proteins extracted from oxidized Ovis aries wool fibers.1mg20 1022 mg1mg5001 mg101500IU50 KU10
#30144564 2018/08/23 To Up
Biological function of a gC1qR homolog (EcgC1qR) of Exopalaemon carinicauda in defending bacteria challenge.The gC1qR is a ubiquitously expressed cell protein that interacts with the globular heads of C1q (gC1q) and many other ligands. In this study, one gC1qR homolog gene was obtained from Exopalaemon carinicauda and named EcgC1qR. The complete nucleotide sequence of EcgC1qR contained a 774 bp open reading frame (ORF) encoding EcgC1qR precursor of 257 amino acids. The deduced amino acid sequence of EcgC1qR revealed a 55-amino-acid-long mitochondrial targeting sequence at the N-terminal and a mitochondrial acidic matrix protein of 33 kDa (MAM33) domain. The genomic organization of EcgC1qR gene showed that EcgC1qR gene contained five exons and four introns. EcgC1qR could express in all of the detected tissues and its expression was much higher in hepatopancreas and hemocytes. The expression of EcgC1qR in the hepatopancreas of prawns challenged with Vibrio parahaemolyticus and Aeromonas hydrophila changed in a time-dependent manner. The expression of EcgC1qR in prawns challenged with V. parahaemolyticus was up-regulated at 6 h (p < 0.05), and significantly up-regulated at 12 h and 24 h (p < 0.01), and then returned to the control levels at 48 h post-challenge (p > 0.05). At the same time, the expression in Aeromonas-challenged group was significantly up-regulated at 6, 12 and 24 h. The recombinant EcgC1qR could inhibit the growth of two tested bacteria. In addition, we successfully deleted EcgC1qR gene through CRISPR/Cas9 technology and it was the first time to obtain the mutant of gC1qR homolog gene in crustacean. It's a great progress to study the biological function of gC1qR in crustacean in future.
Jiquan Zhang, Yujie Liu, Yanyan Li, Naike Su, Yaru Zhou, Jianhai Xiang, Yuying Sun
2288 related Products with: Biological function of a gC1qR homolog (EcgC1qR) of Exopalaemon carinicauda in defending bacteria challenge.100 μg100 μg100 μg1 ml1 Set100ug100ug
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