scholarly journals Physiological changes of Candida tropicalis population degrading phenol in fed batch reactor

2003 ◽  
Vol 46 (4) ◽  
pp. 537-543 ◽  
Author(s):  
Eliska Komarkova ◽  
Jan Paca ◽  
Eva Klapkova ◽  
Marie Stiborova ◽  
Carlos R Soccol ◽  
...  

Candida tropicalis can use phenol as the sole carbon and energy source. Experiments regarding phenol degradations from the water phase were carried out. The fermentor was operated as a fed-batch system with oxistat control. Under conditions of nutrient limitation and an excess of oxygen the respiration activity of cells was suppressed and some color metabolites (black-brown) started to be formed. An accumulation of these products inhibited the cell growth under aerobic conditions. Another impact was a decrease of the phenol hydroxylase activity as the key enzyme of the phenol degradation pathway at the end of the cell respiration activity. This decrease is linked with the above mentioned product inhibition. The cell death studied by fluorescent probe proceeded very slowly after the loss of the respiration activity. The starvation stress induced an increase of the endogenous respiration rate at the expense of phenol oxidation.

2014 ◽  
Vol 167 ◽  
pp. 510-513 ◽  
Author(s):  
Lucie Křiklavová ◽  
Martin Truhlář ◽  
Petra Škodová ◽  
Tomáš Lederer ◽  
Vladimír Jirků

2020 ◽  
Vol 53 (2) ◽  
pp. 16820-16825
Author(s):  
Carlos Martínez ◽  
Jean-Luc Gouzé

2013 ◽  
Vol 21 (2) ◽  
pp. 360-371 ◽  
Author(s):  
S. Bahroun ◽  
F. Couenne ◽  
C. Jallut ◽  
C. Valentin

1993 ◽  
Vol 8 (5-6) ◽  
pp. 263-269 ◽  
Author(s):  
B. W. Kim ◽  
E. H. Kim ◽  
S. C. Lee ◽  
H. N. Chang

2004 ◽  
Vol 70 (11) ◽  
pp. 6767-6775 ◽  
Author(s):  
He-Long Jiang ◽  
Joo-Hwa Tay ◽  
Abdul Majid Maszenan ◽  
Stephen Tiong-Lee Tay

ABSTRACT Aerobic granules are self-immobilized aggregates of microorganisms and represent a relatively new form of cell immobilization developed for biological wastewater treatment. In this study, both culture-based and culture-independent techniques were used to investigate the bacterial diversity and function in aerobic phenol- degrading granules cultivated in a sequencing batch reactor. Denaturing gradient gel electrophoresis (DGGE) analysis of PCR-amplified 16S rRNA genes demonstrated a major shift in the microbial community as the seed sludge developed into granules. Culture isolation and DGGE assays confirmed the dominance of β-Proteobacteria and high-G+C gram-positive bacteria in the phenol-degrading aerobic granules. Of the 10 phenol-degrading bacterial strains isolated from the granules, strains PG-01, PG-02, and PG-08 possessed 16S rRNA gene sequences that matched the partial sequences of dominant bands in the DGGE fingerprint belonging to the aerobic granules. The numerical dominance of strain PG-01 was confirmed by isolation, DGGE, and in situ hybridization with a strain-specific probe, and key physiological traits possessed by PG-01 that allowed it to outcompete and dominate other microorganisms within the granules were then identified. This strain could be regarded as a functionally dominant strain and may have contributed significantly to phenol degradation in the granules. On the other hand, strain PG-08 had low specific growth rate and low phenol degradation ability but showed a high propensity to autoaggregate. By analyzing the roles played by these two isolates within the aerobic granules, a functional model of the microbial community within the aerobic granules was proposed. This model has important implications for rationalizing the engineering of ecological systems.


2014 ◽  
Vol 955-959 ◽  
pp. 455-458
Author(s):  
Lin Zhou ◽  
Zi Xiong Zhou ◽  
Shuang Zhu

Catechol 2,3-dioxygenase (C23O), the key enzyme catalyzing the second step in the phenol degradation meta-cleavage pathway has been purified to homogeneity by one-step chromatography from bacterial strain Bacillus cereus ZL1. The culture condition was optimized according to the analysis of the biomass and C23O activity, and the separation process was monitored by SDS-PAGE method. The molecular weight of the purified C23O was 37±3KDa and the active enzyme was eluted by potassium phosphate buffer with 400 mmol NaCL using linear gradient mode on DEAE-Sepharose Fast Flow.


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