Isolation of a Bacterial Community Able to Use Cyanuric Acid as Its Sole Carbon and Nitrogen Source

2010 ◽  
Vol 150 ◽  
pp. 564-564
Author(s):  
I.A. Silva-Lemus ◽  
C.E. Vásquez-Ortiz ◽  
D. Ahuatzi-Chacón ◽  
A.M. Salmerón-Alcocer ◽  
N. Ruiz-Ordaz ◽  
...  
Keyword(s):  
Bacterial Community ◽  
Nitrogen Source ◽  
Cyanuric Acid ◽  
Carbon And Nitrogen

scholarly journals Molecular Basis of a Bacterial Consortium: Interspecies Catabolism of Atrazine

1998 ◽  
Vol 64 (1) ◽  
pp. 178-184 ◽  
Author(s):  
Mervyn L. de Souza ◽  
David Newcombe ◽  
Sam Alvey ◽  
David E. Crowley ◽  
Anthony Hay ◽  
...  
Keyword(s):  
Nitrogen Source ◽  
Southern Hybridization ◽  
Cyanuric Acid ◽  
Bacterial Species ◽  
Bacterial Consortium ◽  
Triazine Ring ◽  
Carbon And Nitrogen ◽  
Consortium Member ◽  
Ring Compounds ◽  
Pure Cultures

ABSTRACT Pseudomonas sp. strain ADP contains the genes,atzA, -B, and -C, that encode three enzymes which metabolize atrazine to cyanuric acid. Atrazine-catabolizing pure cultures isolated from around the world contain genes homologous to atzA, -B, and -C. The present study was conducted to determine whether the same genes are present in an atrazine-catabolizing bacterial consortium and how the genes and metabolism are subdivided among member species. The consortium contained four or more bacterial species, but two members, Clavibacter michiganese ATZ1 andPseudomonas sp. strain CN1, collectively mineralized atrazine. C. michiganese ATZ1 released chloride from atrazine, produced hydroxyatrazine, and contained a homolog to theatzA gene that encoded atrazine chlorohydrolase. C. michiganese ATZ1 stoichiometrically metabolized hydroxyatrazine to N-ethylammelide and contained genes homologous toatzB and atzC, suggesting that either a functional AtzB or -C catalyzed N-isopropylamine release from hydroxyatrazine. C. michiganese ATZ1 grew on isopropylamine as its sole carbon and nitrogen source, explaining the ability of the consortium to use atrazine as the sole carbon and nitrogen source. A second consortium member, Pseudomonassp. strain CN1, metabolized the N-ethylammelide produced byC. michiganese ATZ1 to transiently form cyanuric acid, a reaction catalyzed by AtzC. A gene homologous to the atzCgene of Pseudomonas sp. strain ADP was present, as demonstrated by Southern hybridization and PCR. Pseudomonassp. strain CN1, but not C. michiganese, metabolized cyanuric acid. The consortium metabolized atrazine faster than didC. michiganese individually. Additionally, the consortium metabolized a much broader set of triazine ring compounds than did previously described pure cultures in which the atzABCgenes had been identified. These data begin to elucidate the genetic and metabolic bases of catabolism by multimember consortia.

Access to 2-Arylquinazolines via Catabolism/Reconstruction of Amino Acids with Insertion of Dimethyl Sulfoxide

2021 ◽  
Author(s):  
Jin-Tian Ma ◽  
Li-Sheng Wang ◽  
Zhi Chai ◽  
Xin-Feng Chen ◽  
Bo-Cheng Tang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Dimethyl Sulfoxide ◽  
Nitrogen Source ◽  
Carbon And Nitrogen ◽  
First Time

Quinazoline skeletons are synthesized by amino acids catabolism/reconstruction combined with dimethyl sulfoxide insertion/cyclization for the first time. The amino acid acts as a carbon and nitrogen source through HI-mediated catabolism...

Facile preparation of C, N co-modified Nb2O5 nanoneedles with enhanced visible light photocatalytic activity

2016 ◽  
Vol 45 (41) ◽  
pp. 16519-16525 ◽  
Author(s):  
Jiao Xue ◽  
Runwei Wang ◽  
Zongtao Zhang ◽  
Shilun Qiu
Keyword(s):  
Photocatalytic Activity ◽  
Visible Light ◽  
Nitrogen Source ◽  
Hydrothermal Method ◽  
Niobium Pentoxide ◽  
Facile Hydrothermal Method ◽  
Carbon And Nitrogen ◽  
Niobium Chloride ◽  
Facile Preparation ◽  
Visible Light Photocatalytic

C, N co-modified niobium pentoxide (Nb2O5) nanoneedles have been successfully synthesized via a facile hydrothermal method with Niobium Chloride (NbCl5) as a precursor and triethylamine as both the carbon and nitrogen source.

scholarly journals Production of Feruloyl Esterase from Aspergillus niger by Solid-State Fermentation on Different Carbon Sources

2011 ◽  
Vol 2011 ◽  
pp. 1-4 ◽  
Author(s):  
Shiyi Ou ◽  
Jing Zhang ◽  
Yong Wang ◽  
Ning Zhang
Keyword(s):  
Carbon Source ◽  
Nitrogen Source ◽  
Wheat Bran ◽  
Cell Walls ◽  
Carbon Sources ◽  
Feruloyl Esterase ◽  
Plant Cell Walls ◽  
Optimal Conditions ◽  
Carbon And Nitrogen ◽  
Maize Bran

A mixture of wheat bran with maize bran as a carbon source and addition of (NH4)SO4 as nitrogen source was found to significantly increase production of feruloyl esterase (FAE) enzyme compared with wheat bran as a sole carbon and nitrogen source. The optimal conditions in conical flasks were carbon source (30 g) to water 1 : 1, maize bran to wheat bran 1 : 2, (NH4)SO4 1.2 g and MgSO4 70 mg. Under these conditions, FAE activity was 7.68 mU/g. The FAE activity on the mixed carbon sources showed, high activity against the plant cell walls contained in the cultures.

Straw management, crop rotation and nitrogen source effect on carbon and nitrogen dynamics: A laboratory study

2009 ◽  
Vol 325 (1-2) ◽  
pp. 243-253 ◽  
Author(s):  
A. Montoya-González ◽  
O. E. González-Navarro ◽  
B. Govaerts ◽  
K. D. Sayre ◽  
I. Estrada ◽  
...  
Keyword(s):  
Nitrogen Source ◽  
Crop Rotation ◽  
Laboratory Study ◽  
Nitrogen Dynamics ◽  
Straw Management ◽  
Source Effect ◽  
Carbon And Nitrogen ◽  
Carbon And Nitrogen Dynamics

scholarly journals A Mannose Family Phosphotransferase System Permease and Associated Enzymes Are Required for Utilization of Fructoselysine and Glucoselysine in Salmonella enterica Serovar Typhimurium

2015 ◽  
Vol 197 (17) ◽  
pp. 2831-2839 ◽  
Author(s):  
Katherine A. Miller ◽  
Robert S. Phillips ◽  
Paul B. Kilgore ◽  
Grady L. Smith ◽  
Timothy R. Hoover
Keyword(s):  
Nitrogen Source ◽  
Nitrogen Sources ◽  
Maillard Reaction Products ◽  
Reaction Products ◽  
Phosphotransferase System ◽  
Carbon And Nitrogen Sources ◽  
Content Type ◽  
Carbon And Nitrogen ◽  
Serovar Typhimurium ◽  
Food Borne Illness

ABSTRACTSalmonella entericserovar Typhimurium, a major cause of food-borne illness, is capable of using a variety of carbon and nitrogen sources. Fructoselysine and glucoselysine are Maillard reaction products formed by the reaction of glucose or fructose, respectively, with the ε-amine group of lysine. We report here thatS. Typhimurium utilizes fructoselysine and glucoselysine as carbon and nitrogen sources via a mannose family phosphotransferase (PTS) encoded bygfrABCD(glucoselysine/fructoselysine PTS components EIIA, EIIB, EIIC, and EIID; locus numbers STM14_5449 to STM14_5454 inS. Typhimurium 14028s). Genes coding for two predicted deglycases within thegfroperon,gfrEandgfrF, were required for growth with glucoselysine and fructoselysine, respectively. GfrF demonstrated fructoselysine-6-phosphate deglycase activity in a coupled enzyme assay. The biochemical and genetic analyses were consistent with a pathway in which fructoselysine and glucoselysine are phosphorylated at the C-6 position of the sugar by the GfrABCD PTS as they are transported across the membrane. The resulting fructoselysine-6-phosphate and glucoselysine-6-phosphate subsequently are cleaved by GfrF and GfrE to form lysine and glucose-6-phosphate or fructose-6-phosphate. Interestingly, althoughS. Typhimurium can use lysine derived from fructoselysine or glucoselysine as a sole nitrogen source, it cannot use exogenous lysine as a nitrogen source to support growth. Expression ofgfrABCDEFwas dependent on the alternative sigma factor RpoN (σ54) and an RpoN-dependent LevR-like activator, which we designated GfrR.IMPORTANCESalmonellaphysiology has been studied intensively, but there is much we do not know regarding the repertoire of nutrients these bacteria are able to use for growth. This study shows that a previously uncharacterized PTS and associated enzymes function together to transport and catabolize fructoselysine and glucoselysine. Knowledge of the range of nutrients thatSalmonellautilizes is important, as it could lead to the development of new strategies for reducing the load ofSalmonellain food animals, thereby mitigating its entry into the human food supply.

scholarly journals Production and characterization of rhamnolipids from Pseudomonas aeruginosa san ai

2012 ◽  
Vol 77 (1) ◽  
pp. 27-42 ◽  
Author(s):  
Milena Rikalovic ◽  
Gordana Gojgic-Cvijovic ◽  
Miroslav Vrvic ◽  
Ivanka Karadzic
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Response Surface Methodology ◽  
Nitrogen Source ◽  
Testing Effect ◽  
Carbon And Nitrogen ◽  
Rhamnolipid Production ◽  
Proteose Peptone ◽  
Isolated Compound ◽  
Rhamnolipid Biosurfactant

Production and characterization of rhamnolipid biosurfactant obtained by strain Pseudomonas aeruginosa san ai was investigated. With regard to carbon and nitrogen source several media were tested to enhance production of rhamnolipids. Phosphate-limited proteose peptone-ammonium salt (PPAS) medium supplemented with sun flower oil as a source of carbon and mineral ammonium chloride and peptone as a nitrogen source greatly improved rhamnolipid production, from 0.15 on basic PPAS (C/N ratio 4.0), to 3 g L-1, on optimized PPAS medium (C/N ratio 7.7). Response surface methodology analysis was used for testing effect of three factors: temperature, concentration of carbon and nitrogen source (w/w), in optimized PPAS medium on rhamnolipid production. Isolated rhamnolipids were characterized by IR and ESI-MS. IR spectra confirmed that isolated compound corresponds to rhamnolipid structure, whereas MS indicated that isolated preparation is a mixture of mono-rhamno-mono-lipidic, mono-rhamno-di-lipidic- and dirhamno- di-lipidic congeners.

scholarly journals Mechanisms for Induction of Microbial Extracellular Proteases in Response to Exterior Proteins

2020 ◽  
Vol 86 (19) ◽  
Author(s):  
Yu-Zhong Zhang ◽  
Wei-Xin Zhang ◽  
Xiu-Lan Chen
Keyword(s):  
Amino Acids ◽  
Nitrogen Source ◽  
Organic Nitrogen ◽  
Nutrient Acquisition ◽  
Extracellular Proteases ◽  
Carbon And Nitrogen ◽  
Heterotrophic Microorganisms ◽  
Organic Nitrogen Source ◽  
Host Infection ◽  
Made In

ABSTRACT Proteins are a main organic nitrogen source for microorganisms. Many heterotrophic microorganisms secrete extracellular proteases (ex-proteases) to efficiently decompose proteins into oligopeptides and amino acids when exterior proteins are required for growth. These ex-proteases not only play important roles in microbial nutrient acquisition or host infection but also contribute greatly to the global recycling of carbon and nitrogen. Moreover, may microbial ex-proteases have important applications in industrial, medical, and biotechnological areas. Therefore, uncovering the mechanisms by which microorganisms initiate the expression of ex-protease genes in response to exterior proteins is of great significance. In this review, the progress made in understanding the induction mechanisms of microbial ex-proteases in response to exterior proteins is summarized, with a focus on the inducer molecules, membrane sensors, and downstream pathways. Problems to be solved for better understanding of the induction mechanisms of microbial ex-proteases are also discussed.

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