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Laccase coli

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https://www.readbyqxmd.com/read/29224621/functional-expression-enhancement-of-bacillus-pumilus-cota-laccase-mutant-wlf-through-site-directed-mutagenesis
#1
Quan Luo, Yu Chen, Jing Xia, Kai-Qiang Wang, Yu-Jie Cai, Xiang-Ru Liao, Zheng-Bing Guan
Bacterial laccases are potential enzymes for biotechnological applications, such as detoxification of industrial effluents, decolorization of textile, and dimerization of phenolic acids, due to their remarkable advantages, including broad substrate spectrum, high thermostability, wide pH scope, and tolerance to alkaline environments. L386W/G417L/G57F (abbreviated as WLF), a good mutant of CotA-laccase from Bacillus pumilus W3, has been constructed and reported by our laboratory with highly improved catalytic efficiency...
February 2018: Enzyme and Microbial Technology
https://www.readbyqxmd.com/read/29112275/expression-purification-and-characterization-of-a-novel-laccase-from-setosphaeria-turcica-in-eschericha-coli
#2
Shuangxin Ma, Ning Liu, Hui Jia, Dongqing Dai, Jinping Zang, Zhiyan Cao, Jingao Dong
Laccases are multicopper oxidases (E.C. 1.10.3.2) that catalyze the oxidation of many phenolic compounds. In this study, a novel laccase, Stlac4, from Setosphaeria turcica was cloned and expressed in Escherichia coli by insertion into the pET-30a expression plasmid. The recombinant laccase was purified and visualized on SDS-PAGE as a single band with an apparent molecular weight of 71.5 KDa, and confirmed by Western blot. The maximum activity of the purified laccase was 127.78 U · mg(-1) , the optimum temperature and pH value were 60 °C and 4...
November 7, 2017: Journal of Basic Microbiology
https://www.readbyqxmd.com/read/29078699/functional-surface-display-of-laccase-in-a-phenol-inducible-bacterial-circuit-for-bioremediation-purposes
#3
Mehrnoosh Fathi-Roudsari, Mehrdad Behmanesh, Ali-Hatef Salmanian, Majid Sadeghizadeh, Khosro Khajeh
Background: Phenolic compounds, which are produced routinely by industrial and urban activities, possess dangers to live organisms and environment. Laccases are oxidoreductase enzymes with the ability of remediating a wide variety of phenolic compounds to more benign molecules. The purpose of the present research is surface display of a laccase enzyme with adhesin involved in diffuse adhesion (AIDA-I) autotransporter system on the surface of Escherichia coli cells for bioremediation of phenolic compounds...
October 28, 2017: Iranian Biomedical Journal
https://www.readbyqxmd.com/read/29063287/characterization-of-a-mildly-alkalophilic-and-thermostable-recombinant-thermus-thermophilus-laccase-with-applications-in-decolourization-of-dyes
#4
Arpana Kumari, Nitin Kishor, Purnananda Guptasarma
OBJECTIVE: To examine the potential for applications of TthLAC, a monomeric (~ 53 kDa) laccase encoded by the genome of Thermus thermophilus (strain HB 27) which can be produced at low cost in Escherichia coli. RESULT: Functional, thermostable and mildly alkalophilic TthLAC of high purity (> 90%) was produced through simple heating of suspended (TthLAC overexpressing) E.coli cells at 65 °C. For reactions of short duration (< 1 h) the temperature for optimal activity is ~ 90 °C...
October 23, 2017: Biotechnology Letters
https://www.readbyqxmd.com/read/29051758/identification-of-yfih-and-the-catalase-cata-as-polyphenol-oxidases-of-aeromonas-media-and-cata-as-a-regulator-of-pigmentation-by-its-peroxyl-radical-scavenging-capacity
#5
Baozhong Chai, Yunqian Qiao, He Wang, Xiaoming Zhang, Jiao Wang, Choushi Wang, Ping Zhou, Xiangdong Chen
Pyomelanin is the major constituent of pigment in melanogenic Aeromonas strains of bacteria. However, eumelanin, synthesized from tyrosine via L-DOPA and polyphenol oxidases (PPOs), may also be present in this genus since L-DOPA is frequently detected in culture fluids of several species. To address this question, we used a deletion mutant of Aeromonas media strain WS, in which pyomelanin synthesis is completely blocked under normal culture conditions. When tyrosine was supplied to the medium, we observed residual melanin accumulation, which we interpret as evidence for existence of the DOPA-melanin pathway...
2017: Frontiers in Microbiology
https://www.readbyqxmd.com/read/29020076/recombinant-laccase-from-pediococcus-acidilactici-cect-5930-with-ability-to-degrade-tyramine
#6
Sara Callejón, Ramón Sendra, Sergi Ferrer, Isabel Pardo
Biogenic amines degradation by bacterial laccases is little known, so we have cloned and heterologously expressed, in E. coli, a new laccase from Pediococcus acidilactici CECT 5930 (Lpa5930), a lactic acid bacterium commonly found in foods able to degrade tyramine. The recombinant enzyme has been characterized by physical and biochemical assays. Here we report the optimization of expression and purification procedures of this laccase. DNA encoding sequence of laccase from P. acidilactici was amplified by PCR and cloned into the expression plasmid pET28a for induction by isopropyl-β-D-thiogalactoipyranoside...
2017: PloS One
https://www.readbyqxmd.com/read/28920394/-bioinformatic-analysis-and-characterization-of-myxobacteria-laccase-like-multicopper-oxidases
#7
Xiuyan Zhao, Fei Chang, Zemin Fang, Yinliang Zhang, Yazhong Xiao
Laccase is a widely-used environment-friendly copper-containing oxidase found in many plants, insects and fungi. Recently, more and more laccases are also found in bacteria. Myxobacteria are an important bacteria resource. However, myxobacteria are much more difficult to isolate and purify than other bacteria. We used bioinformatic approach to screen myxobacteria proteomes available in NCBI. Based on conserved sequences of four copper binding sites in multicopper oxidase, 30 potential laccase sequences were obtained...
April 25, 2017: Sheng Wu Gong Cheng Xue Bao, Chinese Journal of Biotechnology
https://www.readbyqxmd.com/read/28858869/overexpression-of-a-laccase-with-dye-decolorization-activity-from-bacillus-sp-induced-in-escherichia-coli
#8
Haipeng Guo, Bingsong Zheng, Dean Jiang, Wensheng Qin
Laccases from bacteria have been widely studied in the past 2 decades due to the higher growth rate of bacteria and their excellent thermal and alkaline pH stability. In this study, a novel laccase gene was cloned from Bacillus sp., analyzed, and functionally expressed in Escherichia coli. The laccase was highly induced in the E. coli expression system with a maximum intracellular activity of 16 U mg-1 protein. The optimal temperature and pH of the purified laccase were 40°C and 4.6, respectively, when ABTS (2,2'-azino-bis[3-ethylbenzothiazoline-6-sulfonate]) was used as the substrate...
September 1, 2017: Journal of Molecular Microbiology and Biotechnology
https://www.readbyqxmd.com/read/28589226/the-first-acidobacterial-laccase-like-multicopper-oxidase-revealed-by-metagenomics-shows-high-salt-and-thermo-tolerance
#9
Luka Ausec, Francesca Berini, Carmine Casciello, Mariana Silvia Cretoiu, Jan Dirk van Elsas, Flavia Marinelli, Ines Mandic-Mulec
Metagenomics is a powerful tool that allows identifying enzymes with novel properties from the unculturable component of microbiomes. However, thus far only a limited number of laccase or laccase -like enzymes identified through metagenomics has been subsequently biochemically characterized. This work describes the successful bio-mining of bacterial laccase-like enzymes in an acidic bog soil metagenome and the characterization of the first acidobacterial laccase-like multicopper oxidase (LMCO). LMCOs have hitherto been mostly studied in fungi and some have already found applications in diverse industries...
June 6, 2017: Applied Microbiology and Biotechnology
https://www.readbyqxmd.com/read/28554383/high-level-expression-of-a-bacterial-laccase-cueo-from-escherichia-coli-k12-in-pichia-pastoris-gs115-and-its-application-on-the-decolorization-of-synthetic-dyes
#10
Xiaojian Ma, Lu Liu, Qingqing Li, Yunyun Liu, Li Yi, Lixin Ma, Chao Zhai
Laccases are oxidoreductase catalyze the oxidation of a wide range of substrates with oxygen as the electron acceptor. This report was aimed to the high-level expression of a laccase, CueO from Escherichia coli K12 in Pichia pastoris GS115 and its application on decolorization of synthetic dyes. The yacK gene coding CueO was cloned into an expression vector of Pichia pastoris, pHBM905BDM and expressed in a secretory form with Pichia pastoris GS115 as the host. The yield of the recombinant protein was 556mg/L with high-density fermentation and the enzyme activity was about 41,000U/L...
August 2017: Enzyme and Microbial Technology
https://www.readbyqxmd.com/read/28452015/biodegradation-of-ciprofloxacin-by-white-rot-fungus-pleurotus-ostreatus
#11
Sushil Kumar Singh, Robinka Khajuria, Loveleen Kaur
Unrestricted and reckless use of antibiotics has resulted in their accumulation in environment. This, in turn, has led to the emergence of multiple drug-resistant microbes. The present study focuses on degradation of ciprofloxacin (CIP) by an edible white rot fungus Pleurotus ostreatus. Effect of CIP was determined on radial growth and biomass of P. ostreatus. Titrimetric and spectrophotometric assays were carried out to assess the degrading potential of P. ostreatus towards CIP. It was found that CIP has a stimulatory effect on growth and enzyme activity of P...
May 2017: 3 Biotech
https://www.readbyqxmd.com/read/28439850/heterologous-expression-of-a-streptomyces-cyaneus-laccase-for-biomass-modification-applications
#12
Selin Ece, Camilla Lambertz, Rainer Fischer, Ulrich Commandeur
Laccases are used for the conversion of biomass into fermentable sugars but it is difficult to produce high yields of active laccases in heterologous expression systems. We overcame this challenge by expressing Streptomyces cyaneus CECT 3335 laccase in Escherichia coli (ScLac) and we achieved a yield of up to 104 mg L(-1) following purification by one-step affinity chromatography. Stability and activity assays using simple lignin model substrates showed that the purified enzyme preparation was active over a broad pH range and at high temperatures, suggesting it would be suitable for biomass degradation...
December 2017: AMB Express
https://www.readbyqxmd.com/read/28389772/anoxybacillus-sp-strain-uark-01-a-new-thermophilic-soil-bacterium-with-hyperthermostable-alkaline-laccase-activity
#13
Thamir H Al-Kahem Al-Balawi, Adam L Wood, Alexis Solis, Ted Cooper, Ravi D Barabote
We describe the isolation and characteristics of a novel thermophilic bacterium from soil. The organism is a member of the Anoxybacillus genus based on phylogenetic analysis of the 16S rRNA gene. The 16S rRNA of the organism shares >99% sequence identity with those of two species, Anoxybacillus rupiensis and A. geothermalis. We named this isolate as Anoxybacillus sp. strain UARK-01. UARK-01 grows optimally in the presence of oxygen at 55 °C and pH 8. It grew excellently in the presence of lignin as the sole carbon source...
June 2017: Current Microbiology
https://www.readbyqxmd.com/read/28358283/characterization-of-a-thermo-alkali-stable-laccase-from-bacillus-subtilis-cjp3-and-its-application-in-dyes-decolorization
#14
Weichuan Qiao, Jingping Chu, Shaojun Ding, Xin Song, Lei Yu
In this work, a novel bacterial strain exhibiting laccase activity was isolated from black liquor and identified as Bacillus subtilis cjp3. The CotA-laccase gene was cloned from strain cjp3 and expressed in Escherichia coli. The purified recombinant laccase has a maximum activity of 7320 U/L, maintaining high stabilities under a wide pH range and high temperature conditions. Nearly no loss of laccase activity was observed even at pH 9.0 after 10 h of incubation. Reactive blue 19, reactive black 5 and indigo carmine could be efficiently decolorized by the purified laccase in the presence of a mediator ABTS...
July 3, 2017: Journal of Environmental Science and Health. Part A, Toxic/hazardous Substances & Environmental Engineering
https://www.readbyqxmd.com/read/28314922/identification-of-a-novel-copper-activated-and-halide-tolerant-laccase-in-geobacillus-thermopakistaniensis
#15
Saadia Basheer, Naeem Rashid, Raza Ashraf, Muhammad Sohail Akram, Masood Ahmed Siddiqui, Tadayuki Imanaka, Muhammad Akhtar
Genome search of Geobacillus thermopakistaniensis, formerly Geobacillus sp. SBS-4S, revealed the presence of an open reading frame (ESU71923) annotated as laccase. However, the gene product did not display any laccase-like activity against the substrates examined. The laccase activity was, therefore, purified from G. thermopakistaniensis cells and N-terminal amino acid residues of the enzyme were determined. These residues matched the N-terminal sequence of an open reading frame annotated as a copper oxidase (ESU72270)...
May 2017: Extremophiles: Life Under Extreme Conditions
https://www.readbyqxmd.com/read/28273567/transformation-and-toxicity-evaluation-of-tetracycline-in-humic-acid-solution-by-laccase-coupled-with-1-hydroxybenzotriazole
#16
Kai Sun, Qingguo Huang, Shunyao Li
Enzyme-based catalyzed oxidative coupling reactions (E-COCRs) are considered as viable technologies to transform a variety of pharmaceutical antibiotics. This study indicated that the extracellular fungal laccase from Pleurotus ostreatus was effective in transforming tetracycline (TC) with 1-hydroxybenzotriazole (HBT) present at varying conditions during E-COCRs. The presence of humic acid (HA) showed suppressive effect on the transformation rate constants (k) of TC, and the k values for TC decreased as HA concentration increased...
March 1, 2017: Journal of Hazardous Materials
https://www.readbyqxmd.com/read/28259434/effect-of-yeasts-on-biodegradation-potential-of-immobilized-cultures-of-white-rot-fungi
#17
Pavlína Šlosarčíková, Čeněk Novotný, Kateřina Malachová, Hana Válková, Jindřich Fojtík
The aim was to investigate the effect of yeast organisms on the degradation process by immobilized cultures of ligninolytic fungi. Immobilization was accomplished by 7-day colonization of polyamide mesh with mycelial fragments. Irpex lacteus decolorized >90% of the initial concentration of 150mgl(-1) of anthraquinone Remazol Brilliant Blue R dye in three subsequent decolorization cycles and the degradation capacity was not negatively affected by the presence of 10(6)Saccharomyces cerevisiae cells per ml in the mixed culture...
March 1, 2017: Science of the Total Environment
https://www.readbyqxmd.com/read/28146098/comprehensive-analysis-of-rice-laccase-gene-oslac-family-and-ectopic-expression-of-oslac10-enhances-tolerance-to-copper-stress-in-arabidopsis
#18
Qingquan Liu, Le Luo, Xiaoxiao Wang, Zhenguo Shen, Luqing Zheng
Laccases are encoded by a multigene family and widely distributed in plant genomes where they play roles oxidizing monolignols to produce higher-order lignin involved in plant development and stress responses. We identified 30 laccase genes (OsLACs) from rice, which can be divided into five subfamilies, mostly expressed during early development of the endosperm, growing roots, and stems. OsLACs can be induced by hormones, salt, drought, and heavy metals stresses. The expression level of OsLAC10 increased 1200-fold after treatment with 20 μM Cu for 12 h...
January 30, 2017: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/27885197/a-thermostable-bilirubin-oxidizing-enzyme-from-activated-sludge-isolated-by-a-metagenomic-approach
#19
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...
December 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
#20
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...
December 2016: Molecular Biotechnology
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