Extracellular proteinases ofCandidaspecies pathogenic yeasts

2018 ◽  
Vol 33 (2) ◽  
pp. 113-124 ◽  
Author(s):  
M. Rapala-Kozik ◽  
O. Bochenska ◽  
D. Zajac ◽  
J. Karkowska-Kuleta ◽  
M. Gogol ◽  
...  
Keyword(s):  
Extracellular Proteinases

Secretion of Extracellular Proteinases Active against Fibrillar Proteins by Micromycetes

2017 ◽  
Vol 72 (4) ◽  
pp. 206-210
Author(s):  
E. A. Popova ◽  
D. M. Bednenko ◽  
A. A. Osmolovskiy ◽  
V. G. Kreyer ◽  
I. B. Kotova ◽  
...  
Keyword(s):  
Extracellular Proteinases

scholarly journals Heterogeneity of metallo and serine extracellular proteinases in oral clinical isolates ofCandida albicansin HIV-positive and healthy children from Rio de Janeiro, Brazil

2003 ◽  
Vol 38 (2) ◽  
pp. 173-180 ◽  
Author(s):  
Edja Maria Melo de Brito Costa ◽  
André Luis Souza Santos ◽  
Abel Silveira Cardoso ◽  
Maristela Barbosa Portela ◽  
Celina Monteiro Abreu ◽  
...  
Keyword(s):  
Rio De Janeiro ◽  
Clinical Isolates ◽  
Hiv Positive ◽  
Healthy Children ◽  
Extracellular Proteinases

Extracellular proteinases from the phytopathogenic fungus Fusarium culmorum

2006 ◽  
Vol 42 (3) ◽  
pp. 298-303 ◽  
Author(s):  
E. V. Ievleva ◽  
T. A. Revina ◽  
N. N. Kudryavtseva ◽  
A. V. Sof’in ◽  
T. A. Valueva
Keyword(s):  
Fusarium Culmorum ◽  
Phytopathogenic Fungus ◽  
Extracellular Proteinases

Aspergillus ochraceus micromycetes—producers of extracellular proteinases—protein C activators of blood plasma

2012 ◽  
Vol 48 (5) ◽  
pp. 488-492 ◽  
Author(s):  
A. A. Osmolovskiy ◽  
V. G. Kreier ◽  
A. V. Kurakov ◽  
N. . Baranova ◽  
N. S. Egorov
Keyword(s):  
Blood Plasma ◽  
Protein C ◽  
Aspergillus Ochraceus ◽  
Extracellular Proteinases

Purification and Characterization of Three Extracellular Proteinases Produced by Pseudomonas fluorescens INIA 745, an Isolate from Ewe's Milk

1999 ◽  
Vol 62 (5) ◽  
pp. 543-546 ◽  
Author(s):  
J. FERNÁNDEZ ◽  
A. F. MOHEDANO ◽  
P. GAYA ◽  
M. MEDINA ◽  
M. NUÑEZ
Keyword(s):  
Pseudomonas Fluorescens ◽  
Culture Medium ◽  
Inhibitory Effect ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Purification And Characterization ◽  
Ph Optimum ◽  
Extracellular Proteinases ◽  
Ewe's Milk

Three proteinases were isolated from culture medium of Pseudomonas fluorescens INIA 745 and purified to homogeneity by a combination of Phenyl-Sepharose, DEAE-Sepharose, and Sephadex G-100 chromatography. Optimal temperature for enzymatic activity was 45°C for all three proteinases. The pH optimum of proteinases I and II was found to be 7.0, while that of proteinase III was 8.0. Divalent metal ions like Cu2+, Co2+, Zn2+, Fe2+, and Hg2+ were inhibitory to proteinase activity while Ca2+, Mg2+, and Mn2+ had little or no inhibitory effect. The three enzymes were strongly inhibited by EDTA and 1,10-phenantroline and partially by cysteine. The three enzymes are metalloproteinases since they were inhibited by chelators and reactivated by Co2+, Mn2+, Cu2+, and Zn2+. The Km values of proteinases I, II, and III for casein were calculated to be 3.2, 2.6, and 5.2 mg/ml, respectively. Proteinases II and III rapidly degraded β-casein, with preference to αs1-casein, whereas proteinase I hydrolyzed both casein fractions at a slow rate.

Defense peptides: recent developments

2015 ◽  
Vol 6 (4) ◽  
pp. 237-251 ◽  
Author(s):  
Małgorzata Cytryńska ◽  
Agnieszka Zdybicka-Barabas
Keyword(s):  
De Novo ◽  
Current Knowledge ◽  
Membrane Lipid ◽  
Factors Affecting ◽  
Natural Defense ◽  
Secreted Factors ◽  
Recent Developments ◽  
Extracellular Proteinases ◽  
Defense Peptides ◽  
Conventional Antibiotics

AbstractDefense peptides are small amphipathic molecules that exhibit antimicrobial, antitumor, antiviral, and immunomodulatory properties. This review summarizes current knowledge on the mechanisms of antimicrobial activity of cationic and anionic defense peptides, indicating peptide-based as well as microbial cell-based factors affecting this activity. The peptide-based factors include charge, hydrophibicity, and amphipathicity, whereas the pathogen-based factors are membrane lipid composition, presence of sterols, membrane fluidity, cell wall components, and secreted factors such as extracellular proteinases. Since defense peptides have been considered very promising molecules that could replace conventional antibiotics in the era of drug-resistant pathogens, the issue of microbial resistance to antimicrobial peptides (AMPs) is addressed. Furthermore, selected approaches employed for optimization and de novo design of effective AMPs based on the properties recognized as important for the function of natural defense peptides are presented.

Studies on the Production of Extracellular Proteinases by a Non-pigmented Strain of Chromobacterium lividum Isolated from Abattoir Effluent

1978 ◽  
Vol 45 (1) ◽  
pp. 111-124 ◽  
Author(s):  
R. H. DAINTY ◽  
D. J. ETHERINGTON ◽  
B. G. SHAW ◽  
J. BARLOW ◽  
G. T. BANKS
Keyword(s):  
Extracellular Proteinases
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