Influence of nutritional and physicochemical variables on PHB production from raw glycerol obtained from a Colombian biodiesel plant by a wild-type Bacillus megaterium strain

2015 ◽  
Vol 32 (6) ◽  
pp. 682-689 ◽  
Author(s):  
Paalo Moreno ◽  
Camilo Yañez ◽  
Nilo Sérgio Medeiros Cardozo ◽  
Humberto Escalante ◽  
Marianny Y. Combariza ◽  
...  
2014 ◽  
Vol 31 ◽  
pp. S32
Author(s):  
Carolina Guzmán Luna ◽  
Paalo Andrea Moreno Yañez ◽  
Camilo Jose Yañez Diaz ◽  
Nilo Sérgio Medeiros Cardozo ◽  
Humberto Escalante ◽  
...  

2014 ◽  
Vol 31 ◽  
pp. S176
Author(s):  
Paalo Andrea Moreno Yañez ◽  
Débora Jung Luvizetto Faccin ◽  
Nilo Sérgio Medeiros Cardozo ◽  
Humberto Escalante ◽  
Marianny Y. Combariza ◽  
...  

Heliyon ◽  
2021 ◽  
Vol 7 (1) ◽  
pp. e05979
Author(s):  
Daiana Nygaard ◽  
Oxana Yashchuk ◽  
Diego G. Noseda ◽  
Beatriz Araoz ◽  
Élida B. Hermida

2007 ◽  
Vol 189 (12) ◽  
pp. 4375-4383 ◽  
Author(s):  
Graham Christie ◽  
Christopher R. Lowe

ABSTRACT Spores of Bacillus megaterium QM B1551 germinate in response to a number of trigger compounds, including glucose, proline, leucine, and inorganic salts. An approximate 6-kb region of the 165-kb plasmid was found to harbor a tricistronic receptor operon, gerU, and a monocistronic receptor component, gerVB. The gerU operon was observed to complement the germination response in plasmidless strain PV361 to glucose and leucine, with KBr acting as a cogerminant. Proline recognition is conferred by the monocistronic gerVB gene, the presence of which also improves the germination response to other single-trigger compounds. A chimeric receptor, GerU*, demonstrates interchangeability between receptor components and provides evidence that it is the B protein of the receptor that determines germinant specificity. Introduction of the gerU/gerVB gene cluster to B. megaterium KM extends the range of germinants recognized by this strain to include glucose, proline, and KBr in addition to alanine and leucine. A chromosomally encoded receptor, GerA, the B component of which is predicted to be truncated, was found to be functionally redundant. Similarly, the plasmid-borne antiporter gene, grmA, identified previously as being essential for germination in QM B1551, did not complement the germination defect in the plasmidless variant PV361. Wild-type spores carrying an insertion-deletion mutation in this cistron germinated normally; thus, the role of GrmA in spore germination needs to be reevaluated in this species.


2003 ◽  
Vol 69 (6) ◽  
pp. 3244-3250 ◽  
Author(s):  
Daniel Kadouri ◽  
Edouard Jurkevitch ◽  
Yaacov Okon

ABSTRACT When grown under suboptimal conditions, rhizobacteria of the genus Azospirillum produce high levels of poly-β-hydroxybutyrate (PHB). Azospirillum brasilense strain Sp7 and a phbC (PHB synthase) mutant strain in which PHB production is impaired were evaluated for metabolic versatility, for the ability to endure various stress conditions, for survival in soil inoculants, and for the potential to promote plant growth. The carbon source utilization data were similar for the wild-type and mutant strains, but the generation time of the wild-type strain was shorter than that of the mutant strain with all carbon sources tested. The ability of the wild type to endure UV irradiation, heat, osmotic pressure, osmotic shock, and desiccation and to grow in the presence of hydrogen peroxide was greater than that of the mutant strain. The motility and cell aggregation of the mutant strain were greater than the motility and cell aggregation of the wild type. However, the wild type exhibited greater chemotactic responses towards attractants than the mutant strain exhibited. The wild-type strain exhibited better survival than the mutant strain in carrier materials used for soil inoculants, but no difference in the ability to promote plant growth was detected between the strains. In soil, the two strains colonized roots to the same extent. It appears that synthesis and utilization of PHB as a carbon and energy source by A. brasilense under stress conditions favor establishment of this bacterium and its survival in competitive environments. However, in A. brasilense, PHB production does not seem to provide an advantage in root colonization under the conditions tested.


Author(s):  
Javier Ricardo Gómez Cardozo ◽  
Rodrigo Velasco Buscheli ◽  
Carlos del Cerro Sánchez ◽  
Isabel de la Mata Riesco ◽  
Amanda Lucía Mora Martínez

There are a few PHA-producer bacteria that can uptake glycerol to produce this biopolymer. Among them, Bacillus megaterium LVN01 has demonstrated to be able to grow up using glycerol as a carbon source. Glycerol dehydrogenase (GD) plays a key role in the synthesis of PHA from glycerol. In this study, the improvement of glycerol uptake by a recombinant strain of B. megaterium carrying pHT01-bmgd was evaluated in order to enhance PHA production. The biomass and PHA production were evaluated and compared to wild-type. It was determined that the PHA produced by both strains was PHB and the highest improvement in PHB yield was 226% at 30 h.


1997 ◽  
Vol 327 (2) ◽  
pp. 537-544 ◽  
Author(s):  
F. Catherine OLIVER ◽  
Sandeep MODI ◽  
U. William PRIMROSE ◽  
Lu-Yun LIAN ◽  
C. K. Gordon ROBERTS

Oligonucleotide-directed mutagenesis has been used to replace arginine-47 with glutamate in cytochrome P-450 BM3 from Bacillus megaterium and in its haem domain. The mutant has been characterized by sequencing, mass spectrometry, steady-state kinetics and by optical and NMR measurements of substrate binding. The mutant retains significant catalytic activity towards C12-C16 fatty acids, catalysing hydroxylation in the same (ω-1, ω-2, ω-3) positions with kcat/Km values a factor of 14-21 lower. C12-C16 alkyl trimethylammonium compounds are relatively poor substrates for the wild-type enzyme, but are efficiently hydroxylated by the arginine-47 → glutamate mutant at the ω-1, ω-2 and ω-3 positions, with kcat values of up to 19 s-1. Optical spectroscopy shows that the binding of the C14 and C16 alkyl trimethylammonium compounds to the mutant is similar to that of the corresponding fatty acids to the wild-type enzyme. Paramagnetic relaxation measurements show that laurate binds to the ferric state of the mutant in a significantly different position, 1.5 Å closer to the iron, than seen in the wild-type, although this difference is much smaller (~ 0.2 Å) in the ferrous state of the complex. The binding of a substrate having the same charge as residue 47 to the ferric state of the enzyme is roughly ten times weaker than that of a substrate having the opposite charge (and thus is able to make an ion-pair interaction with this residue). The results are discussed in the light of the three-dimensional structure of the enzyme.


2002 ◽  
Vol 68 (2) ◽  
pp. 985-988 ◽  
Author(s):  
Jun Sun ◽  
Anne Van Dommelen ◽  
Jan Van Impe ◽  
Jos Vanderleyden

ABSTRACT The role of three key nitrogen regulatory genes, glnB (encoding the PII protein), glnZ (encoding the Pz protein), and glnD (encoding the GlnD protein), in regulation of poly-3-hydroxybutyrate (PHB) biosynthesis by ammonia in Azospirillum brasilense Sp7 was investigated. It was observed that glnB glnZ and glnD mutants produce substantially higher amounts of PHB than the wild type produces during the active growth phase. glnB and glnZ mutants have PHB production phenotypes similar to that of the wild type. Our results indicate that the PII-Pz system is apparently involved in nitrogen-dependent regulation of PHB biosynthesis in A. brasilense Sp7.


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