Relationship Between Extracellular Neutral Protease Production and Appearance of Bleb-Like Evaginations in Pseudomonas fragi

1985 ◽  
Vol 48 (12) ◽  
pp. 1067-1070 ◽  
Author(s):  
S. S. THOMPSON ◽  
Y. M. NAIDU ◽  
J. J. PESTKA
Keyword(s):  
Cell Wall ◽  
Protease Activity ◽  
Bacterial Population ◽  
Proteolytic Enzymes ◽  
Brain Heart Infusion ◽  
Brain Heart Infusion Broth ◽  
Protease Production ◽  
Ultrastructural Examination ◽  
Pseudomonas Fragi ◽  
Extracellular Protease Activity

Pseudomonas fragi is one of several pseudomonads known to produce proteolytic enzymes. During growth of P. fragi in brain heart infusion broth (BHI) at 10°C, the bacterial population increased from 107 to over 1010 CFU/ml after 130 h, with a concurrent increase in pH from 7.4 to 8.5. Maximal extracellular protease activity occurred after 60 to 72 h. Ultrastructural examination of cells grown in BHI showed the presence of bleb-like evaginations of the cell wall. Similar structures were not detected when P. fragi was grown in Koser citrate broth, a medium which was unsuitable for supporting protease production by P. fragi.

scholarly journals Canola Cake as a Potential Substrate for Proteolytic Enzymes Production by a Selected Strain of Aspergillus oryzae: Selection of Process Conditions and Product Characterization

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Adriana C. Freitas ◽  
Ruann J. S. Castro ◽  
Maria A. Fontenele ◽  
Antonio S. Egito ◽  
Cristiane S. Farinas ◽  
...  
Keyword(s):  
Aspergillus Oryzae ◽  
Protease Activity ◽  
Incubation Temperature ◽  
Initial Conditions ◽  
Proteolytic Enzymes ◽  
Inoculum Size ◽  
Protease Production ◽  
Process Conditions ◽  
Enzymatic Extract ◽  
Technological Advances

Oil cakes have excellent nutritional value and offer considerable potential for use in biotechnological processes that employ solid-state fermentation (SSF) for the production of high value products. This work evaluates the feasibility of using canola cake as a substrate for protease production by a selected strain of Aspergillus oryzae cultivated under SSF. The influences of the following process parameters were considered: initial substrate moisture content, incubation temperature, inoculum size, and pH of the buffer used for protease extraction and activity analysis. Maximum protease activity was obtained after cultivating Aspergillus oryzae CCBP 001 at 20°C, using an inoculum size of 107 spores/g in canola cake medium moistened with 40 mL of water to 100 g of cake. Cultivation and extraction under selected conditions increased protease activity 5.8-fold, compared to the initial conditions. Zymogram analysis of the enzymatic extract showed that the protease molecular weights varied between 31 and 200 kDa. The concentrated protease extract induced clotting of casein in 5 min. The results demonstrate the potential application of canola cake for protease production under SSF and contribute to the technological advances needed to increase the efficiency of processes designed to add value to agroindustrial wastes.

scholarly journals Production of extracellular protease by a Brazilian strain of Beauveria bassiana reactivated on coffee berry borer, Hypothenemus hampei

2007 ◽  
Vol 50 (2) ◽  
pp. 217-223 ◽  
Author(s):  
Eliana Tiemi Ito ◽  
Geni Varéa-Pereira ◽  
Dalva Tomoe Miyagui ◽  
Maria Helena Pimenta Pinotti ◽  
Pedro Manoel Oliveira Janeiro Neves
Keyword(s):  
Beauveria Bassiana ◽  
Protease Activity ◽  
Extracellular Protease ◽  
Protease Production ◽  
Hypothenemus Hampei ◽  
Coffee Berry ◽  
Active Growth ◽  
Lag Period ◽  
Extracellular Protease Activity ◽  
The Stability

Studies were carried out on extracellular protease production by Beauveria bassiana CG432 in liquid medium containing glucose and yeast extract. B. Bassiana presented active growth after lag period of 24 h., produced 80% of the total of the extracellular protease activity in 48 h which was maximum on the 5th culture day. The extracellular protease presented optimum activity at 60ºC, was stable up to 1M Cl-, maintained the stability during 15 day at 4ºC and -18ºC, but was not stable if frozen repeatedly.

THE EFFECT OF "COMPETASE" ON DNA UPTAKE IN PROVOKED TRANSFORMATION OF A STREPTOCOCCUS

1965 ◽  
Vol 11 (5) ◽  
pp. 823-827 ◽  
Author(s):  
R. Pakula ◽  
A. H. W. Hauschild
Keyword(s):  
Deoxyribonucleic Acid ◽  
Brain Heart Infusion ◽  
Streptomycin Resistance ◽  
Brain Heart Infusion Broth ◽  
Dna Uptake ◽  
Retarding Effect ◽  
Competence Factor ◽  
Effect On Growth

The competence-provoking factor produced by the highly transformable group H streptococcus, strain Challis, was used to provoke efficient transformability in the poorly transformable group H streptococcus, strain Wicky. Transformations to streptomycin resistance were carried out with C14-labelled DNA which was extracted from bacteria fed with thymidine-2-C14.When cultures of strain Wicky were grown in Difco brain–heart infusion broth, supplemented with serum, and treated with competence factor and deoxyribonucleic acid, 25 to 40% of viable units were transformed while no transformation occurred without the factor. At the same time, the incorporation of C14 into cells treated with competence factor was higher than incorporation of C14 into untreated cells.Crude preparations of the competence factor had a retarding effect on growth of the streptococcus, irrespective of whether DNA was added.

Influence of Neurosecretory Cells and of Corpus Allatum on Intestinal Protease Activity in the Adult Calliphora Erythrocephala MEIG

1963 ◽  
Vol 40 (2) ◽  
pp. 301-321
Author(s):  
ELLEN THOMSEN ◽  
IB MØLLER
Keyword(s):  
Protein Synthesis ◽  
Protease Activity ◽  
Proteolytic Enzymes ◽  
Specific Protein ◽  
Neurosecretory Cells ◽  
Corpus Allatum ◽  
Minor Effect ◽  
Calliphora Erythrocephala ◽  
Sugar Water ◽  
The Mean

1. The protease activity of the adult Calliphora female measured on the first 5 days after emergence was found to be highly influenced by the diet, the activity of females fed on sugar, water and meat (meat-flies) being much higher than that of females fed only on sugar and water (sugar-flies). 2. The development of the enzyme(s) was found to be controlled by the medial neurosecretory cells (m.n.c.), the mean protease activity of females deprived of their m.n.c. only amounting to one-quarter to one-third of the maximum values for the meat-flies. 3. Implantation of corpora cardiaca-allata (presumably containing m.n.c. hormone) into females without m.n.c. raised the protease activity of these significantly, showing that the influence of the implanted organs must be hormonal. 4. The corpus allatum was found to have a certain, if minor, effect on the protease activity. 5. It is concluded that in Calliphora the eating of meat exerts its effect on the production of protease mainly indirectly by causing liberation of m.n.c. hormone into the blood. 6. As proteases are themselves proteins, the effect of the m.n.c. hormone on the production of proteolytic enzymes by the gut cells must be regarded as an effect on the specific protein synthesis of these cells. There is some evidence that the m.n.c. hormone might be involved in the regulation of protein synthesis in general.

Toxin Production by Psychrotrophic Bacillus spp. Present in Milk

1990 ◽  
Vol 53 (9) ◽  
pp. 790-792 ◽  
Author(s):  
M. W. GRIFFITHS
Keyword(s):  
Bacillus Cereus ◽  
Brain Heart Infusion ◽  
Bacterial Count ◽  
Toxin Production ◽  
Latex Agglutination ◽  
Brain Heart Infusion Broth ◽  
Agglutination Assay ◽  
Bacillus Spp ◽  
Latex Agglutination Assay

Using a reversed passive latex agglutination assay, about 85% of psychrotrophic Bacillus spp. tested were shown to produce diarrhoegenic toxin during growth on brain heart infusion broth at 25°C. The majority of these strains were identified as Bacillus cereus or cereus-related strains. However, a number of other species was capable of synthesizing the toxin. Further investigation of four psychrotrophic Bacilli showed that the toxin was produced during growth in milk at temperatures ranging from 6 to 21°C. Toxin production increased with increasing temperatures and was not synthesized in appreciable quantities until the bacterial count exceeded 1 × 107 cfu/ml.

Production and characterisation of thermostable alkaline protease from Bacillus subtilis isolated from LA hot spring, Terengganu

2021 ◽  
Vol 16 (7) ◽  
pp. 84-91
Author(s):  
Maslinda Alias ◽  
Hakim Che Harun Mohammad ◽  
Ashraf Razali Nurul ◽  
Jasnizat Saidin ◽  
Nazaitulshila Rasit ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Alkaline Protease ◽  
Protease Activity ◽  
Hot Spring ◽  
Skim Milk ◽  
Industrial Applications ◽  
Protease Production ◽  
Significant Activity ◽  
Original Activity ◽  
Optimum Ph

This research aims to produce thermostable alkaline protease from Bacillus subtilis isolated from La Hot Spring, Terengganu, Malaysia. The study was also conducted to determine the optimum conditions for protease production and stability by considering several parameters including pH, temperature and salt concentration. All seven bacteria were screened on skim milk agar overnight at 37 °C. Three strains with the highest proteolytic activity were identified in protease specific medium. The thermostable alkaline protease had an optimum temperature of 60 °C which achieved 85.73, 82.90 and 83.05 U/mL of protease activity for the three strains respectively. Furthermore, the strains exhibited significant activity of more than 90% from their original activity. Meanwhile, the optimum pH for protease production was pH 9 with the protease activity of 76.76, 79.71 and 88.39 U/mL for TB4, TB6 and TB9 strains, respectively. Proteases were found stable at pH 9 where the loss did not exceed 30% of its original activity. Collectively, all of the data emphasised that proteases from B. subtilis were alkaline thermostable proteases in accordance with a recent report. The finding highlights the viability of the proteases for biotechnological and industrial applications.

Purification and characterization of exocellular proteases produced by a clinical isolate and a laboratory strain of Pseudomonas aeruginosa

1980 ◽  
Vol 26 (1) ◽  
pp. 77-86 ◽  
Author(s):  
S. E. Jensen ◽  
L. Phillippe ◽  
J. Teng Tseng ◽  
G. W. Stemke ◽  
J. N. Campbell
Keyword(s):  
Molecular Weight ◽  
Pseudomonas Aeruginosa ◽  
Clinical Isolate ◽  
Protease Activity ◽  
Gel Filtration ◽  
Laboratory Strain ◽  
Exchange Chromatography ◽  
The Other ◽  
Protease Production ◽  
Peptide Bonds

Exocellular protease production was examined in two separate strains of Pseudomonas aeruginosa, one a clinical isolate and the other a laboratory strain. Both strains produced two separate proteases (proteases 1 and 2) which were indistinguishable from one strain to the other. The two proteases were purified by a two-step procedure of gel filtration chromatography followed by ion-exchange chromatography. Proteases 1 and 2 were shown to be distinct serologically and unrelated by physicochemical parameters examined. Protease 1 was the major exocellular protein produced and contributed about 95% of the total protease activity of the culture. It was estimated to have a molecular weight of 34 850 and was also shown to contain 10% glucosamine by weight. Protease 2, in contrast, had an estimated molecular weight of 52750 and contained no detectable carbohydrate. Proteases 1 and 2 were both stimulated by Ca2+, and Mg2+ and inhibited by Co2+Zn2+, and 1,10-o-phenanthroline. Protease 1 was also inhibited by EDTA. In addition to protease activity, both proteases 1 and 2 demonstrated elastase activity as well as a limited collagenase activity. Specificity of the two proteases against synthetic peptides was, however, quite different. Protease 1, but not protease 2, showed a preference for peptide bonds in which the amino group was contributed by an amino acid with a hydrophobic R group.

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