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Laccase coli

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https://www.readbyqxmd.com/read/27885197/a-thermostable-bilirubin-oxidizing-enzyme-from-activated-sludge-isolated-by-a-metagenomic-approach
#1
Nobutada Kimura, Yoichi Kamagata
A gene coding for a multicopper oxidase (BopA) was identified through the screening of a metagenomic library constructed from wastewater treatment activated sludge. The recombinant BopA protein produced in Escherichia coli exhibited oxidation activity toward 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonate) (ABTS) in the presence of copper, suggesting that BopA is laccase. A bioinformatic analysis of the bopA gene sequence indicated that it has a phylogenetically bacterial origin, possibly derived from a bacterium within the phylum Deinococcus-Thermus...
November 23, 2016: Microbes and Environments
https://www.readbyqxmd.com/read/27771851/in-vitro-refolding-and-characterization-of-recombinant-laccase-cota-from-bacillus-pumilus-mk001-and-its-potential-for-phenolics-degradation
#2
Sandeep Kumar, Kavish Kr Jain, Shikha Rani, Kailash N Bhardwaj, Manisha Goel, Ramesh Chander Kuhad
Among lignocellulolytic enzymes, laccases are the most versatile, broadly specific, and largely studied enzyme with a wide range of biotechnological potential. Putative laccase (CotA) from Bacillus pumilus MK001 was cloned and expressed in E. coli. In addition to soluble bioactive fraction, inactive inclusion body fraction was also harvested and refolded under optimized conditions resulting in 64 % of refolding efficiency. The enzyme was found to be thermostable exhibiting a half-life of 60 min at 80 °C...
October 22, 2016: Molecular Biotechnology
https://www.readbyqxmd.com/read/27741324/characterization-of-a-highly-thermostable-and-organic-solvent-tolerant-copper-containing-polyphenol-oxidase-with-dye-decolorizing-ability-from-kurthia-huakuii-lam0618t
#3
Xiang Guo, Shan Zhou, Yanwei Wang, Jinlong Song, Huimin Wang, Delong Kong, Jie Zhu, Weiwei Dong, Mingxiong He, Guoquan Hu, Zhiyong Ruan
Laccases are green biocatalysts that possess attractive advantages for the treatment of resistant environmental pollutants and dye effluents. A putative laccase-like gene, laclK, encoding a protein of 29.3 kDa and belonging to the Cu-oxidase_4 superfamily, was cloned and overexpressed in Escherichia coli. The purified recombinant protein LaclK (LaclK) was able to oxidize typical laccase substrates such as 2,6-dimethoxyphenol and l-dopamine. The characteristic adsorption maximums of typical laccases at 330 nm and 610 nm were not detected for LaclK...
2016: PloS One
https://www.readbyqxmd.com/read/27738721/a-simple-strategy-for-extracellular-production-of-cota-laccase-in-escherichia-coli-and-decolorization-of-simulated-textile-effluent-by-recombinant-laccase
#4
Tian-Nyu Wang, Min Zhao
Laccases are green oxidases with a number of potential industrial applications. In this study, recombinant Bacillus subtilis CotA laccase was secreted by Escherichia coli via both the α-hemolysin secretion system and the YebF secretion system after microaerobic induction. Meanwhile, we discovered a much simpler approach for extracellular production of recombinant CotA laccase from E. coli, involving alternation of induction conditions to release recombinant CotA following intracellular expression. By optimizing the induction parameters, the extracellular yield of recombinant CotA laccase was improved from 157...
October 13, 2016: Applied Microbiology and Biotechnology
https://www.readbyqxmd.com/read/27451019/purification-and-characterization-of-a-recombinant-laccase-like-multi-copper-oxidase-from-paenibacillus-glucanolyticus-slm1
#5
S L Mathews, C E Smithson, A M Grunden
AIMS: The aim of this study was to evaluate the activity of a novel bacterial laccase-like multi-copper oxidase (LMCO) from Paenibacillus glucanolyticus SLM1: a bacterium isolated from pulp and paper waste. METHODS AND RESULTS: A new bacterial LMCO gene (CuOx) from P. glucanolyticus SLM1 was identified and cloned into pET22b. The protein it encodes was recombinantly expressed in Escherichia coli. The recombinant P. glucanolyticus LMCO had a molecular weight of approximately 90 kDa and demonstrated oxidation of the LMCO substrates 2,2'-Azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS), catechol, and 2,6-Dimethoxyphenol (2,6-DMP), with the oxidation of ABTS occurring to the greatest extent (776 U mg(-1) under optimal conditions of pH 7 and 40°C)...
July 23, 2016: Journal of Applied Microbiology
https://www.readbyqxmd.com/read/27354563/degradation-of-dyes-using-crude-extract-and-a-thermostable-and-ph-stable-laccase-isolated-from-pleurotus-nebrodensis
#6
Xianghe Yuan, Guoting Tian, Yongchang Zhao, Liyan Zhao, Hexiang Wang, Tzi Bun Ng
Three laccase isoenzymes (Lac1, Lac2 and Lac3) have been purified to homogeneity from Pleurotus nebrodensis in our previous study. Lac2 was shown to be the dominant isoform, capable of oxidizing the majority of laccase substrates and manifesting good thermostability and pH stability. Hence, Lac2 was selected to decolourize structurally different dyes and the colour removal efficiencies of Lac2 and the crude extract of P. nebrodensis were compared. By monitoring the λmax of the reaction system during the course of biotransformation, clear hypsochromic shifts were observed for most of the dyes examined, illustrating that at least one peak disappeared as a result of laccase treatment...
August 2016: Bioscience Reports
https://www.readbyqxmd.com/read/27160378/three-steps-in-one-pot-whole-cell-biocatalytic-synthesis-of-enantiopure-and-pinoresinol-via-kinetic-resolution
#7
Esther Ricklefs, Marco Girhard, Vlada B Urlacher
BACKGROUND: Pinoresinol is a high-value plant-derived lignan with multiple health supporting effects. Enantiomerically pure pinoresinol can be isolated from natural sources, but with low efficiency. Most chemical and biocatalytic approaches that have been described for the synthesis of pinoresinol furnish the racemic mixture. In this study we devised a three-step biocatalytic cascade for the production of enantiomerically pure pinoresinol from the cheap compound eugenol. Two consecutive oxidations of eugenol through vanillyl-alcohol oxidase and laccase are followed by kinetic resolution of racemic pinoresinol by enantiospecific pinoresinol reductases...
2016: Microbial Cell Factories
https://www.readbyqxmd.com/read/27146212/a-high-effective-nadh-ferricyanide-dehydrogenase-coupled-with-laccase-for-nad-regeneration
#8
Jizhong Wang, Chengli Yang, Xing Chen, Bingxin Bao, Xuan Zhang, Dali Li, Xingfan Du, Ruofu Shi, Junfang Yang, Ronghui Zhu
OBJECTIVES: To find an efficient and cheap system for NAD(+) regeneration RESULTS: A NADH-ferricyanide dehydrogenase was obtained from an isolate of Escherichia coli. Optimal activity of the NADH dehydrogenase was at 45 °C and pH 7.5, with a K m value for NADH of 10 μM. By combining the NADH dehydrogenase, potassium ferricyanide and laccase, a bi-enzyme system for NAD(+) regeneration was established. The system is attractive in that the O2 consumed by laccase is from air and the sole byproduct of the reaction is water...
August 2016: Biotechnology Letters
https://www.readbyqxmd.com/read/27098101/gene-cloning-identification-and-characterization-of-the-multicopper-oxidase-cuma-from-pseudomonas-sp-593
#9
Sheng Yang, Yan Long, Hong Yan, Huawan Cai, Yadong Li, Xingguo Wang
The cumA, a gene encoding a multicopper oxidase (MCO), was cloned from the soil-dwelling bacterium Pseudomonas sp. 593. Its corresponding product was overexpressed in E. coli BL21 (DE3) pLysS and purified to homogeneity through Ni-affinity chromatography. The amino acid sequence of the CumA of Pseudomonas sp. 593 was strongly homologous to that of CumA as previously reported. The CumA was quite stable in neutral pH and had poor thermostability. Meanwhile, its optimum pH and temperature towards laccase substrates 2,6-dimethoxyphenol (DMP), syringaldazine (SGZ), and 2'-azino-bis(3-ethylbenzthiazolinesulfonic acid) (ABTS) were at pH 5...
April 21, 2016: Biotechnology and Applied Biochemistry
https://www.readbyqxmd.com/read/27059481/a-strategy-for-soluble-overexpression-and-biochemical-characterization-of-halo-thermotolerant-bacillus-laccase-in-modified-e-coli
#10
Azam Safary, Rezvan Moniri, Maryam Hamzeh-Mivehroud, Siavoush Dastmalchi
An efficient method was introduced for soluble expression of recombinant laccase (rpCotA(SL-1)) from a newly isolated halo-thermotolerant Bacillus sp. SL-1 in modified Escherichia coli, trxB2/gor2 mutant (Origami™ B (DE3)). The yield of purified soluble laccase in Origami strain under micro-aerobic condition was ∼20mg/L of bacterial culture, showing significant improvement over the laccase produced in E.coli BL21 strain under aerobic condition. The specific activity of 13U/mg for purified laccase produced in micro-aerobic condition was higher than that of 1...
June 10, 2016: Journal of Biotechnology
https://www.readbyqxmd.com/read/27050199/different-recombinant-forms-of-polyphenol-oxidase-a-a-laccase-from-marinomonas-mediterranea
#11
Fabio Tonin, Elena Rosini, Luciano Piubelli, Antonio Sanchez-Amat, Loredano Pollegioni
Polyphenol oxidase from the marine bacterium Marinomonas mediterranea (MmPPOA) is a membrane-bound, blue, multi-copper laccase of 695 residues. It possesses peculiar properties that distinguish it from known laccases, such as a broad substrate specificity (common to tyrosinases) and a high redox potential. In order to push the biotechnological application of this laccase, the full-length enzyme was overexpressed in Escherichia coli cells with and without a C-terminal His-tag. The previous form, named rMmPPOA-695-His, was purified to homogeneity by HiTrap chelating chromatography following solubilization by 1% SDS in the lysis buffer with an overall yield of ≈1 mg/L fermentation broth and a specific activity of 1...
July 2016: Protein Expression and Purification
https://www.readbyqxmd.com/read/26879123/isolation-and-genome-sequencing-of-four-arctic-marine-psychrobacter-strains-exhibiting-multicopper-oxidase-activity
#12
Morteza Shojaei Moghadam, Andreas Albersmeier, Anika Winkler, Lorenzo Cimmino, Kjersti Rise, Martin Frank Hohmann-Marriott, Jörn Kalinowski, Christian Rückert, Alexander Wentzel, Rahmi Lale
BACKGROUND: Marine cold-temperature environments are an invaluable source of psychrophilic microbial life for new biodiscoveries. An Arctic marine bacterial strain collection was established consisting of 1448 individual isolates originating from biota, water and sediment samples taken at a various depth in the Barents Sea, North of mainland Norway, with an all year round seawater temperature of 4 °C. The entire collection was subjected to high-throughput screening for detection of extracellular laccase activity with guaiacol as a substrate...
2016: BMC Genomics
https://www.readbyqxmd.com/read/26846788/new-approaches-to-achieve-high-level-enzyme-production-in-streptomyces-lividans
#13
Laura Sevillano, Erik Vijgenboom, Gilles P van Wezel, Margarita Díaz, Ramón I Santamaría
BACKGROUND: Actinomycetes are saprophytic soil bacteria, and a rich source of industrial enzymes. While some of these enzymes can be produced using well-characterized production platforms such as Escherichia coli or Bacillus subtilis, Streptomyces lividans may be the preferred host for proper folding and efficient secretion of active enzymes. A combination of promoters, signal peptides and hosts were tested in order to obtain the best protein expression in this actinomycete. The xylanase, Xys1, from S...
2016: Microbial Cell Factories
https://www.readbyqxmd.com/read/26784443/oxidation-of-polycyclic-aromatic-hydrocarbons-using-bacillus-subtilis-cota-with-high-laccase-activity-and-copper-independence
#14
Jun Zeng, Qinghe Zhu, Yucheng Wu, Xiangui Lin
Bacterial laccase CueO from Escherichia coli can oxidize polycyclic aromatic hydrocarbons (PAHs); however, its application in the remediation of PAH-contaminated soil mainly suffers from a low oxidation rate and copper dependence. It was reported that a laccase with a higher redox potential tended to have a higher oxidation rate; thus, the present study investigated the oxidation of PAHs using another bacterial laccase CotA from Bacillus subtilis with a higher redox potential (525 mV) than CueO (440 mV). Recombinant CotA was overexpressed in E...
April 2016: Chemosphere
https://www.readbyqxmd.com/read/26642207/multiple-genes-in-a-single-host-cost-effective-production-of-bacterial-laccase-cota-pectate-lyase-pel-and-endoxylanase-xyl-by-simultaneous-expression-and-cloning-in-single-vector-in-e-coli
#15
Sandeep Kumar, Kavish Kumar Jain, Kailash N Bhardwaj, Subhojit Chakraborty, Ramesh Chander Kuhad
This study attempted to reduce the enzyme production cost for exploiting lignocellulosic materials by expression of multiple genes in a single host. Genes for bacterial laccase (CotA), pectate lyase (Pel) and endoxylanase (Xyl), which hold significance in lignocellulose degradation, were cloned in pETDuet-1 vector containing two independent cloning sites (MCS). CotA and xyl genes were cloned in MCS1 and MCS 2, respectively. Pel gene was cloned by inserting complete cassette (T7 promoter, ribosome binding site, pel gene, His tag and complete gene ORF) preceded by cotA open reading frame in the MCS1...
2015: PloS One
https://www.readbyqxmd.com/read/26631965/molecular-modeling-and-simulation-studies-of-recombinant-laccase-from-yersinia-enterocolitica-suggests-significant-role-in-the-biotransformation-of-non-steroidal-anti-inflammatory-drugs
#16
Deepti Singh, Surender Rawat, Mohd Waseem, Sunita Gupta, Andrew Lynn, Mukesh Nitin, Nirala Ramchiary, Krishna Kant Sharma
The YacK gene from Yersinia enterocolitica strain 7, cloned in pET28a vector and expressed in Escherichia coli BL21 (DE3), showed laccase activity when oxidized with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) and guaiacol. The recombinant laccase protein was purified and characterized biochemically with a molecular mass of ≈58 KDa on SDS-PAGE and showed positive zymogram with ABTS. The protein was highly robust with optimum pH 9.0 and stable at 70 °C upto 12 h with residual activity of 70%...
January 8, 2016: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/26626349/isolation-purification-and-characterization-of-two-laccases-from-carrot-daucus-carota-l-and-their-response-to-abiotic-and-metal-ions-stresses
#17
Jing Ma, Zhi-Sheng Xu, Feng Wang, Ai-Sheng Xiong
Laccases, which belong to the blue copper oxidase enzyme family, oxidize many organic and inorganic compounds. The laccase-encoding genes DcLac1 and DcLac2 were isolated from the economically important tuberous root carrot, and their proteins were successfully expressed and purified using the Escherichia coli expression system BL21(DE3). DcLac1 and DcLac2 had molecular masses of approximately 64 and 61.9 kDa, respectively. With 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulfonate acid) as the substrate, DcLac1 and DcLac2 had K m values of 3...
December 2015: Protein Journal
https://www.readbyqxmd.com/read/26590586/cloning-and-characterization-of-a-new-laccase-from-lactobacillus-plantarum-j16-cect-8944-catalyzing-biogenic-amines-degradation
#18
S Callejón, R Sendra, S Ferrer, I Pardo
In our search for degrading activities of biogenic amines (BAs) in lactic acid bacteria, a protein annotated as laccase enzyme was identified in Lactobacillus plantarum J16 (CECT 8944). In this study, the gene of this new laccase was cloned and heterologously overexpressed in Escherichia coli. The recombinant laccase protein was purified and characterized biochemically. The purified laccase showed characteristic spectroscopic properties of blue multicopper oxidases. The enzyme has a molecular weight of ∼ 62...
April 2016: Applied Microbiology and Biotechnology
https://www.readbyqxmd.com/read/26323308/crystallization-and-x-ray-diffraction-studies-of-a-two-domain-laccase-from-streptomyces-griseoflavus
#19
Svetlana Tishchenko, Azat Gabdulkhakov, Liubov Trubitsina, Alexander Lisov, Marina Zakharova, Alexey Leontievsky
Laccase (EC 1.10.3.2) is one of the most common copper-containing oxidases; it is found in many organisms and catalyzes the oxidation of primarily phenolic compounds by oxygen. Two-domain laccases have unusual thermostability, resistance to inhibitors and an alkaline optimum of activity. The causes of these properties in two-domain laccases are poorly understood. A recombinant two-domain laccase (SgfSL) was cloned from the genome of Streptomyces griseoflavus Ac-993, expressed in Escherichia coli and purified to homogeneity...
September 2015: Acta Crystallographica. Section F, Structural Biology Communications
https://www.readbyqxmd.com/read/26314909/poly-3-hydroxybutyrate-ethyl-cellulose-based-bio-composites-with-novel-characteristics-for-infection-free-wound-healing-application
#20
Hafiz M N Iqbal, Godfrey Kyazze, Ian Charles Locke, Thierry Tron, Tajalli Keshavarz
A series of bio-composites including poly3-hydroxybutyrate [P(3HB)] grafted ethyl cellulose (EC) stated as P(3HB)-EC were successfully synthesised. Furthermore, natural phenols e.g., p-4-hydroxybenzoic acid (HBA) and ferulic acid (FA) were grafted onto the newly developed P(3HB)-EC-based bio-composites under laccase-assisted environment without the use of additional initiators or crosslinking agents. The phenol grafted bio-composites were critically evaluated for their antibacterial and biocompatibility features as well as their degradability in soil...
November 2015: International Journal of Biological Macromolecules
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