Use of zeolite to controlBacillus megaterium extracellular proteinase production

1998 ◽  
Vol 43 (6) ◽  
pp. 613-616 ◽  
Author(s):  
J. Votruba ◽  
J. Pazlarová ◽  
J. Chaloupka
Keyword(s):  
Extracellular Proteinase ◽  
Proteinase Production

Regulation of extracellular proteinase production in an ectomycorrhizal fungusHebeloma crustuliniforme

Mycologia ◽  
1994 ◽  
Vol 86 (2) ◽  
pp. 227-234 ◽  
Author(s):  
Hong Zhu ◽  
Bruce P. Dancik ◽  
Kenneth O. Higginbotham
Keyword(s):  
Extracellular Proteinase ◽  
Proteinase Production

Extracellular proteinase production and the pathogenicity of Nocardiae

1989 ◽  
Vol 281 (1) ◽  
pp. 78-80 ◽  
Author(s):  
R. Tsuboi ◽  
T. Yamaguchi ◽  
K. Matsuda ◽  
H. Ogawa
Keyword(s):  
Extracellular Proteinase ◽  
Proteinase Production

Inhibition by chelating agents of the formation of active extracellular proteinase byPseudomonas fluorescens32A

1985 ◽  
Vol 52 (1) ◽  
pp. 91-100 ◽  
Author(s):  
Robin C. Mckeller ◽  
Hilaire Cholette
Keyword(s):  
Gel Electrophoresis ◽  
Protein Concentration ◽  
Chelating Agents ◽  
Polyacrylamide Gel Electrophoresis ◽  
Skim Milk ◽  
Staining Intensity ◽  
Protein Band ◽  
Enzyme Synthesis ◽  
Extracellular Proteinase ◽  
Proteinase Production

SUMMARYThe effect of chelating agents on extracellular proteinase production byPseudomonas fluorescens32A was examined. Increasing concentrations of orthophosphate slightly stimulated growth while inhibiting proteinase synthesis. Fifty percent inhibition was found at 35 and 28 mM-orthophosphate at 5 and 20 °C respectively. Extracellular protein concentration was reduced by 30% when cells were grown with 100 mM-orthophosphate. Polyacrylamide gel electrophoresis of the cell-free supernatants suggested that reduced enzyme synthesis had taken place as evidenced by the decrease in staining intensity of the protein band corresponding to the proteinase. Other phosphate compounds could replace orthophosphate as an inhibitor. Extent of inhibition was related to chain length; polyphosphates with 4–6 or 13–18 phosphorus atoms were the most effective inhibitors. EDTA (0·5 mM) completely inhibited proteinase synthesis. This inhibition could be partly reversed by Ca2+and, to a lesser extent, Mn2+. Proteinase production at 5 °C in skim milk was completely inhibited by phosphate glass (P13–P18). Control experiments showed that loss of activity with chelators was not due to inhibition of preformed enzyme. The results suggest a possible role for polyphosphates in controlling proteinase production in stored milk.

REGULATION OF PROTEINASE FORMATION IN A SPECIES OF MICROCOCCUS

1966 ◽  
Vol 12 (6) ◽  
pp. 1175-1185 ◽  
Author(s):  
I. J. McDonald ◽  
Alice K. Chambers
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Carbon Source ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Synthetic Medium ◽  
Carbon Sources ◽  
Extracellular Proteinase ◽  
Proteinase Production

Micrococcus sp. ATCC No. 407 (M. freudenreichii) produced relatively large amounts of extracellular proteinase in synthetic medium containing methionine, thiamine, biotin, NH4Cl, NaHCO3, NaCl, MgSO4, and FeSO4, with aspartic acid, asparagine, glutamic acid, or glutamine as the carbon source. The organism produced relatively small amounts of proteinase with succinate, malate, fumarate, maltose, maltotriose, or maltotetraose as the carbon source. In synthetic medium containing maltose, any one of several amino acids stimulated growth and proteinase production. The results indicated that the organism is a partial constitutive strain with respect to proteinase production and suggested that proteinase formation is controlled by a form of end-product induction. In the presence of inducer, carbon sources such as succinate or maltose caused suppression of proteinase formation, suggesting control by metabolic repression as well. Because extracellular proteinase formation is induced by amino acids and suppressed by carbon sources such as succinate or maltose, and because the organism can utilize amino acids as carbon sources for growth, it. is suggested that the function of extracellular proteinase in this organism is to ensure a supply of carbon for growth rather than a supply of amino acids for protein synthesis.

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