Mise en évidence d'une activité uréasique chez Streptococcus thermophilus

1988 ◽  
Vol 34 (6) ◽  
pp. 818-822 ◽  
Author(s):  
V. Juillard ◽  
M. J. Desmazeaud ◽  
H. E. Spinnler
Keyword(s):  
Amino Acids ◽  
Urease Activity ◽  
Culture Medium ◽  
Colorimetric Method ◽  
Streptococcus Thermophilus ◽  
Stationary Growth Phase ◽  
Optimal Temperature ◽  
Ammonium Ions ◽  
Stationary Growth ◽  
Optimal Ph

In Streptococcus thermophilus CNRZ 404, the presence of urease activity was demonstrated by means of a specific colorimetric method for ammonium ions. The main physicochemical properties of the enzyme were determined. The Km with urea as substrate was 1.19 mM and the optimal pH was approximately 7.5. Because both thermolability and enzyme activity increased as the temperature was increased to 70 °C, the optimal temperature could not be determined with precision. Urease activity was maximal at the beginning of the stationary growth phase; it was stimulated by the presence of urea and of certain amino acids such as arginine and glutamic acid in the culture medium. This activity has been detected in several other strains of Streptococcus thermophilus. [Translated by the journal]

Production ofD-amino acid oxidase byAspergillussp. strain O20 active on cephalosporin C

1997 ◽  
Vol 43 (3) ◽  
pp. 292-295 ◽  
Author(s):  
Salim K. Mujawar ◽  
Jaiprakash G. Shewale
Keyword(s):  
Amino Acids ◽  
Enzyme Activity ◽  
Amino Acid ◽  
Stationary Growth Phase ◽  
Acid Oxidase ◽  
Cephalosporin C ◽  
Production Medium ◽  
Stationary Growth ◽  
Amino Acid Oxidase ◽  
Aspergillus Sp

Aspergillus sp. strain O20 produces inducible D-amino acid oxidase intracellularly, only in the presence of some amino acids. The enzyme was induced most effectively by the addition of DL-alanine (1% w/v) to the production medium. Among the various compounds studied, production of the D-amino acid oxidase was enhanced by Aerosol-22, glucose, and sodium nitrate. D-Amino acid oxidase formation was observed during the onset of the stationary growth phase. Maximum enzyme activity was recorded after 96 h of fermentation (1000 IU/L).Key words: D-amino acid oxidase, Aspergillus sp., 7-aminocephalosporanic acid, cephalosporin C.

scholarly journals Arthroderma tuberculatum and Arthroderma multifidum Isolated from Soils in Rook (Corvus frugilegus) Colonies as Producers of Keratinolytic Enzymes and Mineral Forms of N and S

2020 ◽  
Vol 17 (24) ◽  
pp. 9162
Author(s):  
Justyna Bohacz ◽  
Michał Możejko ◽  
Ignacy Kitowski
Keyword(s):  
Amino Acids ◽  
Culture Medium ◽  
Agricultural Practice ◽  
Ammonium Ions ◽  
Mineral N ◽  
Corvus Frugilegus ◽  
Keratinolytic Fungi ◽  
Sulfate Release ◽  
Proteins And Peptides

Keratinolytic fungi representing the genus Arthroderma that were isolated from the soils of a rook (Corvus frugilegus) colony were used as biological agents for the disposal of waste feathers. The aim of this study was to assess the abilities of Arthroderma tuberculatum and Arthroderma multifidum fungi with a varied inflow of keratin matter to biodegrade waste feathers. The evaluation was based on the determination of feather mass loss, the activity of keratinolytic enzymes, and the content of mineral N and S forms. It was found that the activity of protease released by the fungi contributed to an increase in the level of soluble proteins and peptides and the concentration of ammonium ions, as well as alkalization of the culture medium. Keratinase activity was significantly correlated with sulfate release, especially in A. tuberculatum cultures. The strains of A. tuberculatum fungi isolated from the soil with the highest supply of organic matter, i.e., strains III, IV, and V, had the lowest enzymatic activity, compared to the A. multifidum strains, but they released mineral nitrogen and sulfur forms that are highly important for fertilization, as well as nutritionally important peptides and amino acids. A. tuberculatum strains can be used for the management of waste feathers that can be applied in agricultural practice.

scholarly journals Sequencing and Transcriptional Analysis of the Streptococcus thermophilus Histamine Biosynthesis Gene Cluster: Factors That Affect Differential hdcA Expression

2010 ◽  
Vol 76 (18) ◽  
pp. 6231-6238 ◽  
Author(s):  
Marina Calles-Enríquez ◽  
Benjamin Hjort Eriksen ◽  
Pia Skov Andersen ◽  
Fergal P. Rattray ◽  
Annette H. Johansen ◽  
...  
Keyword(s):  
Streptococcus Thermophilus ◽  
Stationary Growth Phase ◽  
Cell Number ◽  
Fermented Food ◽  
Transcriptional Analysis ◽  
Growth Phases ◽  
Stationary Growth ◽  
Biosynthesis Gene Cluster ◽  
Polycistronic Mrna ◽  
Maximum Expression

ABSTRACT Histamine, a toxic compound that is formed by the decarboxylation of histidine through the action of microbial decarboxylases, can accumulate in fermented food products. From a total of 69 Streptococcus thermophilus strains screened, two strains, CHCC1524 and CHCC6483, showed the capacity to produce histamine. The hdc clusters of S. thermophilus CHCC1524 and CHCC6483 were sequenced, and the factors that affect histamine biosynthesis and histidine-decarboxylating gene (hdcA) expression were studied. The hdc cluster began with the hdcA gene, was followed by a transporter (hdcP), and ended with the hdcB gene, which is of unknown function. The three genes were orientated in the same direction. The genetic organization of the hdc cluster showed a unique organization among the lactic acid bacterial group and resembled those of Staphylococcus and Clostridium species, thus indicating possible acquisition through a horizontal transfer mechanism. Transcriptional analysis of the hdc cluster revealed the existence of a polycistronic mRNA covering the three genes. The histidine-decarboxylating gene (hdcA) of S. thermophilus demonstrated maximum expression during the stationary growth phase, with high expression levels correlated with high histamine levels. Limited expression was evident during the lag and exponential growth phases. Low-temperature (4°C) incubation of milk inoculated with a histamine-producing strain showed lower levels of histamine than did inoculated milk kept at 42°C. This reduction was attributed to a reduction in the activity of the HdcA enzyme itself rather than a reduction in gene expression or the presence of a lower cell number.

scholarly journals Aspartate Biosynthesis Is Essential for the Growth of Streptococcus thermophilus in Milk, and Aspartate Availability Modulates the Level of Urease Activity

2007 ◽  
Vol 73 (18) ◽  
pp. 5789-5796 ◽  
Author(s):  
Stefania Arioli ◽  
Christophe Monnet ◽  
Simone Guglielmetti ◽  
Carlo Parini ◽  
Ivano De Noni ◽  
...  
Keyword(s):  
Aspartic Acid ◽  
Phosphoenolpyruvate Carboxylase ◽  
Parent Strain ◽  
Urease Activity ◽  
Streptococcus Thermophilus ◽  
Defined Medium ◽  
Lactobacillus Delbrueckii ◽  
Chemically Defined Medium ◽  
Ammonium Ions ◽  
Carboxylase Activity

ABSTRACT We investigated the carbon dioxide metabolism of Streptococcus thermophilus, evaluating the phenotype of a phosphoenolpyruvate carboxylase-negative mutant obtained by replacement of a functional ppc gene with a deleted and inactive version, Δppc. The growth of the mutant was compared to that of the parent strain in a chemically defined medium and in milk, supplemented or not with l-aspartic acid, the final product of the metabolic pathway governed by phosphoenolpyruvate carboxylase. It was concluded that aspartate present in milk is not sufficient for the growth of S. thermophilus. As a consequence, phosphoenolpyruvate carboxylase activity was considered fundamental for the biosynthesis of l-aspartic acid in S. thermophilus metabolism. This enzymatic activity is therefore essential for growth of S. thermophilus in milk even if S. thermophilus was cultured in association with proteinase-positive Lactobacillus delbrueckii subsp. bulgaricus. It was furthermore observed that the supplementation of milk with aspartate significantly affected the level of urease activity. Further experiments, carried out with a p ureI -gusA recombinant strain, revealed that expression of the urease operon was sensitive to the aspartate concentration in milk and to the cell availability of glutamate, glutamine, and ammonium ions.

scholarly journals Conversion of Daidzein and Genistein by an Anaerobic Bacterium Newly Isolated from the Mouse Intestine

2008 ◽  
Vol 74 (15) ◽  
pp. 4847-4852 ◽  
Author(s):  
Anastasia Matthies ◽  
Thomas Clavel ◽  
Michael Gütschow ◽  
Wolfram Engst ◽  
Dirk Haller ◽  
...  
Keyword(s):  
Stationary Phase ◽  
Enzyme Induction ◽  
Growth Phase ◽  
Anaerobic Bacterium ◽  
Stationary Growth Phase ◽  
Gut Bacteria ◽  
Soy Isoflavones ◽  
Strictly Anaerobic ◽  
Stationary Growth ◽  
Mouse Intestine

ABSTRACT The metabolism of isoflavones by gut bacteria plays a key role in the availability and bioactivation of these compounds in the intestine. Daidzein and genistein are the most common dietary soy isoflavones. While daidzein conversion yielding equol has been known for some time, the corresponding formation of 5-hydroxy-equol from genistein has not been reported previously. We isolated a strictly anaerobic bacterium (Mt1B8) from the mouse intestine which converted daidzein via dihydrodaidzein to equol as well as genistein via dihydrogenistein to 5-hydroxy-equol. Strain Mt1B8 was a gram-positive, rod-shaped bacterium identified as a member of the Coriobacteriaceae. Strain Mt1B8 also transformed dihydrodaidzein and dihydrogenistein to equol and 5-hydroxy-equol, respectively. The conversion of daidzein, genistein, dihydrodaidzein, and dihydrogenistein in the stationary growth phase depended on preincubation with the corresponding isoflavonoid, indicating enzyme induction. Moreover, dihydrogenistein was transformed even more rapidly in the stationary phase when strain Mt1B8 was grown on either genistein or daidzein. Growing the cells on daidzein also enabled conversion of genistein. This suggests that the same enzymes are involved in the conversion of the two isoflavones.

Renin and angiotensins in cultured mouse adrenocortical tumour cells

1985 ◽  
Vol 108 (4) ◽  
pp. 545-549 ◽  
Author(s):  
Mitsuhide Naruse ◽  
Kazuo Shizume ◽  
Tadashi Inagami
Keyword(s):  
Adrenal Gland ◽  
Substrate Specificity ◽  
Cell Line ◽  
Cathepsin D ◽  
Culture Medium ◽  
Renin Activity ◽  
Cell Lysate ◽  
Specific Affinity ◽  
Adrenocortical Tumour ◽  
Optimal Ph

Abstract. Mouse adrenal tissue has been reported to contain high renin activity. However, it is not clear whether the renin is produced inside the tissue or is derived from a blood-borne component. We have investigated a cloned cell line of mouse adrenocortical tumour (Y-1) which has a steroidogenic activity. Sizable quantities of renin were demonstrated, predominantly in the cell lysate. This renin activity was distinguished from cathepsin D in view of its specific affinity to anti-renin antibody, optimal pH was determined, and the substrate specificity was checked with haemoglobin. Immunoreactive angiotensins were also detectable, but were demonstrated both in the cell and in the culture medium. This study provides further evidence for the existence of renin intrinsic to the adrenal gland. This study also suggests an intracellular role for renin and possible secretion of generated angiotensins.

scholarly journals The extracellular proteome of Rhizobium etli CE3 in exponential and stationary growth phase

2010 ◽  
Vol 8 (1) ◽  
pp. 51 ◽  
Author(s):  
Niurka Meneses ◽  
Guillermo Mendoza-Hernández ◽  
Sergio Encarnación
Keyword(s):  
Growth Phase ◽  
Stationary Growth Phase ◽  
Rhizobium Etli ◽  
Stationary Growth ◽  
Extracellular Proteome

scholarly journals Extruction of keratinase from the local isolate Bacillus licheniformis and partially purified and characterized

2009 ◽  
Vol 3 (2) ◽  
pp. 41-52
Author(s):  
Rasha T. Abdullah ◽  
Abdulkareem J. Hashim ◽  
JASIM M. Karhout
Keyword(s):  
Enzyme Activity ◽  
Bovine Serum Albumin ◽  
Ion Exchange ◽  
Bacillus Licheniformis ◽  
Enzyme Characterization ◽  
Optimal Temperature ◽  
Chicken Feathers ◽  
Local Isolate ◽  
Cellulose Column ◽  
Optimal Ph

The keratinase produced from local isolate Bacillus licheniformis was purified by two steps included precipitation by ammonium sulphate with 40% saturation; followed by ion exchange using CM-Cellulose column. The enzyme was purified to 12.6 times in the last step with an enzyme yield of 17%. Enzyme characterization results indicated that: The optimal pH for enzyme activity was 7.5 and it was stable at 7-9.5. The optimal temperature for enzyme activity was 50°C and it was stable for 30 min at 25-45 °C. Substrate specifity was tested using casein, Bovine serum albumin, gelatin, hooves, human hair, chicken feathers and wool; higher specifity was recorded using casein gave 0.6 unit /ml. The enzyme was inhibited by PMSF and metal ions like Hg+2, Fe+2, Cu+2 and Mn+2, and activated by Ca+2, Mg+2, Zn+2and Al+3.

scholarly journals Effect of the Concentration of Extracellular Polymeric Substances (EPS) and Aeration Intensity on Waste Glycerol Valorization by Docosahexaenoic Acid (DHA) Produced in Heterotrophic Culture of Schizochytrium sp.

2021 ◽  
Vol 11 (20) ◽  
pp. 9573
Author(s):  
Natalia Kujawska ◽  
Szymon Talbierz ◽  
Marcin Dębowski ◽  
Joanna Kazimierowicz ◽  
Marcin Zieliński
Keyword(s):  
Docosahexaenoic Acid ◽  
Culture Medium ◽  
Extracellular Polymeric Substances ◽  
Stationary Growth Phase ◽  
Operating Costs ◽  
Glycerol Conversion ◽  
Waste Glycerol ◽  
Dry Cell Weight ◽  
Dha Production ◽  
Dry Cell

The study aimed to determine the effectiveness of docosahexaenoic acid (DHA) production by Schizochytrium sp. biomass fed with waste glycerol depending on the concentration of extracellular polymeric substances (EPS) in the culture medium and medium aeration effectiveness. The microalgae from the genus Schizochytrium sp. were proved to be capable of producing EPS composed of glucose, galactose, mannose, fucose, and xylose. The highest EPS concentration, reaching 8.73 ± 0.09 g/dm3, was determined at the stationary growth phase. A high EPS concentration caused culture medium viscosity to increase, contributing to diminished oxygen availability for cells, lower culture effectiveness, and reduced waste glycerol conversion to DHA. The Schizochytrium sp. culture variant found optimal in terms of the obtained technological effects and operating costs was performed at the volumetric oxygen mass transfer coefficient of kLa = 600 1/h, which enabled obtaining dry cell weight (DCW) of 147.89 ± 4.77 g/dm3, lipid concentration of 69.44 ± 0.76 g/dm3, and DHA concentration in the biomass reaching 29.44 ± 0.36 g/dm3. The effectiveness of waste glycerol consumption in this variant reached 3.76 ± 0.31 g/dm3·h and 3.16 ± 0.22 g/gDCW.

Sign in / Sign up

Export Citation Format

Share Document