Solvent-assisted strategy induced surface N-modification of PtCu aerogel for enhanced electrocatalytic property

2021 ◽  
Author(s):  
Tianshan Song ◽  
Hui Xue ◽  
Jing Sun ◽  
Niankun Guo ◽  
Jiawen Sun ◽  
...  
Keyword(s):  
Nitrogen Source ◽  
Sole Nitrogen Source ◽  
Electrocatalytic Property ◽  
Methyl Pyrrolidone

A facile method of surface nitrogen modification of PtCu aerogels with N-Methyl pyrrolidone as the sole nitrogen source is reported. The E1/2 of PtCu aerogels is 0.932 V and the...

PRODUCTION OF CYTASES ACTIVE ON BARLEY GUM BY BACTERIA OF THE GENUS BACILLUS

1953 ◽  
Vol 31 (1) ◽  
pp. 28-32 ◽  
Author(s):  
A. C. Blackwood
Keyword(s):  
Bacillus Subtilis ◽  
Enzymatic Activity ◽  
Nitrogen Source ◽  
Freeze Drying ◽  
Shake Flask ◽  
Sole Nitrogen Source ◽  
Genus Bacillus ◽  
Original Activity ◽  
Bacterial Cultures ◽  
Bacillus Genus

One hundred and fourteen bacterial cultures representing most of the species in the Bacillus genus were tested for the production of extracellular barley gum cytase. Assays were made on shake-flask cultures grown on a medium containing glucose and yeast extract. Although all the organisms had some enzymatic activity, certain strains of Bacillus subtilis gave the best yields of cytase. On a medium with asparagine as the sole nitrogen source even higher yields were obtained. The crude cytase preparations were stable and after freeze-drying most of the original activity remained.

scholarly journals Monomethylamine as a Nitrogen Source for a Nonmethylotrophic Bacterium, Agrobacterium tumefaciens

2010 ◽  
Vol 76 (12) ◽  
pp. 4102-4104 ◽  
Author(s):  
Yin Chen ◽  
Kathryn L. McAleer ◽  
J. Colin Murrell
Keyword(s):  
Agrobacterium Tumefaciens ◽  
Carbon Source ◽  
Nitrogen Source ◽  
Sole Nitrogen Source ◽  
Key Enzymes ◽  
Genes Encoding

ABSTRACT Monomethylamine can be used by nonmethylotrophs as a sole nitrogen source but not as a carbon source; however, little is known about the genes and enzymes involved. The γ-glutamylmethylamide/N-methylglutamate pathway for monomethylamine utilization by methylotrophs has recently been resolved. We have identified genes encoding key enzymes of this pathway in nonmethylotrophs (e.g., Agrobacterium tumefaciens) and demonstrated that this pathway is also involved in the utilization of monomethylamine as a nitrogen source by nonmethylotrophs.

scholarly journals Mutants affecting histidine utilization inAspergillus nidulans

1975 ◽  
Vol 25 (2) ◽  
pp. 119-135 ◽  
Author(s):  
Meryl Polkinghorne ◽  
M. J. Hynes
Keyword(s):  
Carbon Source ◽  
Nitrogen Source ◽  
Sole Carbon Source ◽  
Nitrogen Sources ◽  
Limiting Factor ◽  
Sole Nitrogen Source ◽  
Wild Type ◽  
Exogenous Substrate ◽  
Growth Properties ◽  
Type Strains

SUMMARYWild-type strains ofAspergillus nidulansgrow poorly onL-histidine as a sole nitrogen source. The synthesis of the enzyme histidase (EC. 4.3.1.3) appears to be a limiting factor in the growth of the wild type, as strains carrying the mutantareA102 allele have elevated histidase levels and grow strongly on histidine as a sole nitrogen source.L-Histidine is an extremely weak sole carbon source for all strains.Ammonium repression has an important role in the regulation of histidase synthesis and the relief of ammonium repression is dependent on the availability of a good carbon source. The level of histidase synthesis does not respond to the addition of exogenous substrate.Mutants carrying lesions in thesarA orsarB loci (suppressor ofareA102) have been isolated. The growth properties of these mutants on histidine as a sole nitrogen source correlate with the levels of histidase synthesized. Mutation at thesarA andsarB loci also reduces the utilization of a number of other nitrogen sources. The data suggest that these two genes may code for regulatory products involved in nitrogen catabolism. No histidase structural gene mutants were identified and possible explanations of this are discussed.

scholarly journals Purification of arginase from Aspergillus nidulans.

1994 ◽  
Vol 41 (4) ◽  
pp. 467-471 ◽  
Author(s):  
A Dzikowska ◽  
J P Le Caer ◽  
P Jonczyk ◽  
P Wëgleński
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Neurospora Crassa ◽  
Molecular Mass ◽  
Nitrogen Source ◽  
Aspergillus Nidulans ◽  
Sole Nitrogen Source ◽  
Mass Ratio ◽  
Conserved Domains ◽  
Native Molecular Mass ◽  
High Degree

Arginase (EC 3.5.3.1) of Aspergillus nidulans, the enzyme which enables the fungus to use arginine as the sole nitrogen source was purified to homogeneity. Molecular mass of the purified arginase subunit is 40 kDa and is similar to that reported for the Neurospora crassa (38.3 kDa) and Saccharomyces cerevisiae (39 kDa) enzymes. The native molecular mass of arginase is 125 kDa. The subunit/native molecular mass ratio suggests a trimeric form of the protein. The arginase protein was cleaved and partially sequenced. Two out of the six polypeptides sequenced show a high degree of homology to conserved domains in arginases from other species.

scholarly journals Isolation of a triazophos-degrading strainKlebsiellasp. E6 effectively utilizing triazophos as sole nitrogen source

2005 ◽  
Vol 253 (2) ◽  
pp. 259-265 ◽  
Author(s):  
Lihong Wang ◽  
Lin Zhang ◽  
Huanlin Chen ◽  
Qingguo Tian ◽  
Guonian Zhu
Keyword(s):  
Nitrogen Source ◽  
Sole Nitrogen Source

scholarly journals CMO1 encodes a putative choline monooxygenase and is required for the utilization of choline as the sole nitrogen source in the yeast Scheffersomyces stipitis (syn. Pichia stipitis)

Microbiology ◽  
2014 ◽  
Vol 160 (5) ◽  
pp. 929-940 ◽  
Author(s):  
Tomas Linder
Keyword(s):  
Nitrogen Source ◽  
Nitrogen Sources ◽  
Pichia Stipitis ◽  
Sole Nitrogen Source ◽  
Scheffersomyces Stipitis ◽  
Gene Encoding ◽  
Iron Protein ◽  
Choline Monooxygenase ◽  
Haem Iron ◽  
Eukaryotic Genomes

Sixteen yeasts with sequenced genomes belonging to the ascomycete subphyla Saccharomycotina and Taphrinomycotina were assayed for their ability to utilize a variety of primary, secondary, tertiary and quartenary aliphatic amines as nitrogen sources. The results support a previously proposed pathway of quaternary amine catabolism whereby glycine betaine is first converted into choline, which is then cleaved to release trimethylamine, followed by stepwise demethylation of trimethylamine to release free ammonia. There were only a few instances of utilization of N-methylated glycine species (sarcosine and N,N-dimethylglycine), which suggests that this pathway is not intact in any of the species tested. The ability to utilize choline as a sole nitrogen source correlated strongly with the presence of a putative Rieske non-haem iron protein homologous to bacterial ring-hydroxylating oxygenases and plant choline monooxygenases. Deletion of the gene encoding the Rieske non-haem iron protein in the yeast Scheffersomyces stipitis abolished its ability to utilize choline as the sole nitrogen source, but did not affect its ability to use methylamine, dimethylamine, trimethylamine, ethylamine, diethylamine, ethanolamine or glycine as nitrogen sources. The gene was named CMO1 for putative choline monooxygenase 1. A bioinformatic survey of eukaryotic genomes showed that CMO1 homologues are found throughout the eukaryotic domain.

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