scholarly journals Cow Dung Is a Novel Feedstock for Fibrinolytic Enzyme Production from Newly Isolated Bacillus sp. IND7 and Its Application in In Vitro Clot Lysis

2016 ◽  
Vol 7 ◽  
Author(s):  
Ponnuswamy Vijayaraghavan ◽  
Arumugaperumal Arun ◽  
Samuel Gnana Prakash Vincent ◽  
Mariadhas Valan Arasu ◽  
Naif Abdullah Al-Dhabi
Keyword(s):  
Enzyme Production ◽  
Fibrinolytic Enzyme ◽  
Clot Lysis ◽  
Cow Dung ◽  
Bacillus Sp

scholarly journals Novel Sequential Screening and Enhanced Production of Fibrinolytic Enzyme byBacillussp. IND12 Using Response Surface Methodology in Solid-State Fermentation

2017 ◽  
Vol 2017 ◽  
pp. 1-13 ◽  
Author(s):  
Ponnuswamy Vijayaraghavan ◽  
P. Rajendran ◽  
Samuel Gnana Prakash Vincent ◽  
Arumugaperumal Arun ◽  
Naif Abdullah Al-Dhabi ◽  
...  
Keyword(s):  
Response Surface Methodology ◽  
Solid State ◽  
Response Surface ◽  
Solid State Fermentation ◽  
Enzyme Production ◽  
Blood Clot ◽  
Fibrinolytic Enzyme ◽  
Surface Model ◽  
Cow Dung ◽  
Enhanced Production

Fibrinolytic enzymes have wide applications in clinical and waste treatment. Bacterial isolates were screened for fibrinolytic enzyme producing ability by skimmed milk agar plate using bromocresol green dye, fibrin plate method, zymography analysis, and goat blood clot lysis. After these sequential screenings,Bacillussp. IND12 was selected for fibrinolytic enzyme production.Bacillussp. IND12 effectively used cow dung for its growth and enzyme production (687±6.5 U/g substrate). Further, the optimum bioprocess parameters were found out for maximum fibrinolytic enzyme production using cow dung as a low cost substrate under solid-state fermentation. Two-level full-factorial experiments revealed that moisture, pH, sucrose, peptone, and MgSO4were the vital parameters with statistical significance (p<0.001). Three factors (moisture, sucrose, and MgSO4) were further studied through experiments of central composite rotational design and response surface methodology. Enzyme production of optimized medium showed4143±12.31 U/g material, which was more than fourfold the initial enzyme production (978±36.4 U/g). The analysis of variance showed that the developed response surface model was highly significant (p<0.001). The fibrinolytic enzyme digested goat blood clot (100%), chicken skin (83±3.6%), egg white (100%), and bovine serum albumin (29±4.9%).

scholarly journals IN VITRO ASSESSMENT OF POTENTIAL PROBIOTIC MICROORGANISMS FOR APPLICATION IN ANIMAL FEEDING

2018 ◽  
Vol 54 (4A) ◽  
pp. 250 ◽  
Author(s):  
Le Thi Hong Van
Keyword(s):  
Enzyme Production ◽  
Animal Feed ◽  
Digestive Enzyme ◽  
Saccharomyces Boulardii ◽  
Bacillus Sp ◽  
Acid Generation ◽  
Gastrointestinal Conditions ◽  
Animal Feeding ◽  
In Vitro Assessment

This study aimed to evaluate and to select potential probiotic microorganisms. The obtained results would be further studied for application in production of animal feed. A total of 16 strains of microorganisms including 11 strains of Lactobacillus, four strains of Bacillus and a yeast strain Saccharomyces boulardii PLCP were investigated for acid production, digestive enzyme production and antimicrobial activity as well as their survival when exposed to simulated gastrointestinal conditions. The results showed that all 11 strains of Lactobacillus bacteria were capable of acid generation (in the range from 18.05 – 19.04 g/l). All four strains of Bacillus bacteria were capable of producing protease. Only Bacillus sp D7 strain was capable of producing three digestive enzymes (protease, amylase, cellulase) with hydrolyzed hollows ranged from 15.5–18.5 mm. The antibacterial activity of 9/16 test strains was positive against Salmonella Typhimurium, Staphylococcus aureus and Escherichia coli. Survivability of 15 test microorganisms in simulated gastrointestinal conditions was relatively high (c.a. 80 %). Three strains of L. acidophilus VAST, S. boulardii PLCP and Bacillus sp D7 when in mixture demonstrated a great potential as probiotics for animal.

scholarly journals Statistical Optimization of Fibrinolytic Enzyme Production Using Agroresidues byBacillus cereusIND1 and Its Thrombolytic ActivityIn Vitro

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Ponnuswamy Vijayaraghavan ◽  
Samuel Gnana Prakash Vincent
Keyword(s):  
Enzyme Production ◽  
Blood Clot ◽  
Exchange Chromatography ◽  
Fibrinolytic Enzyme ◽  
Dihydrogen Phosphate ◽  
Sodium Dihydrogen Phosphate ◽  
Beef Extract ◽  
Diethylaminoethyl Cellulose ◽  
Sodium Dihydrogen

A potent fibrinolytic enzyme-producingBacillus cereusIND1 was isolated from the Indian food, rice. Solid-state fermentation was carried out using agroresidues for the production of fibrinolytic enzyme. Among the substrates, wheat bran supported more enzyme production and has been used for the optimized enzyme production by statistical approach. Two-level full-factorial design demonstrated that moisture, supplementation of beef extract, and sodium dihydrogen phosphate have significantly influenced enzyme production (P<0.05). A central composite design resulted in the production of 3699 U/mL of enzyme in the presence of 0.3% (w/w) beef extract and 0.05% (w/w) sodium dihydrogen phosphate, at 100% (v/w) moisture after 72 h of fermentation. The enzyme production increased fourfold compared to the original medium. This enzyme was purified to homogeneity by ammonium sulfate precipitation, diethylaminoethyl-cellulose ion-exchange chromatography, Sephadex G-75 gel filtration chromatography, and casein-agarose affinity chromatography and had an apparent molecular mass of 29.5 kDa. The optimum pH and temperature for the activity of fibrinolytic enzyme were found to be 8.0 and 60°C, respectively. This enzyme was highly stable at wide pH range (7.0–9.0) and showed 27% ± 6% enzyme activity after initial denaturation at 60°C for 1 h.In vitroassays revealed that the enzyme could activate plasminogen and significantly degraded the fibrin net of blood clot, which suggests its potential as an effective thrombolytic agent.

Activated Protein C Increases Fibrin Clot Lysis by Neutralization of Plasminogen Activator Inhibitor No Evidence for a Cofactor Role of Protein S

1988 ◽  
Vol 60 (02) ◽  
pp. 328-333 ◽  
Author(s):  
N J de Fouw ◽  
Y F de Jong ◽  
F Haverkate ◽  
R M Bertina
Keyword(s):  
Plasminogen Activator ◽  
Protein C ◽  
Blood Platelets ◽  
Plasminogen Activator Inhibitor ◽  
Protein S ◽  
Tissue Type ◽  
Clot Lysis ◽  
Activator Inhibitor ◽  
Pai 1

summaryThe effect of purified human activated protein G (APC) on fibrinolysis was studied using a clot iysis system consisting of purified glu-plasminogen, tissue-type plasminogen activator, plasminogen activator inhibitor (released from endothelial cells or blood platelets), fibrinogen, 125T-fibrinogen and thrombin. All proteins were of human origin.In this system APC could increase fibrinolysis in a dose dependent way, without affecting fibrin formation or fibrin crosslinking. However, this profibrinolytic effect of APC could only be observed when plasminogen activator inhibitor (PAI-l) was present. The effect of APC was completely quenched by pretreatment of APC with anti-protein C IgG or di-isopropylfluorophosphate. Addition of the cofactors of APC:protein S, Ca2+-ions and phospholipid-alone or in combination did not enhance the profibrinolytic effect of APC. These observations indicate that human APC can accelerate in vitro clot lysis by the inactivation of PAI-1 activity. However, the neutralization of PAI-1 by APC is independent of the presence or absence of protein S, phospholipid and Ca2+-ions.

Anti-thrombotic Effect of a PAI-1 Inhibitor in Rats Given Endotoxin

1996 ◽  
Vol 75 (01) ◽  
pp. 118-126 ◽  
Author(s):  
T Abrahamsson ◽  
V Nerme ◽  
M Strömqvist ◽  
B Åkerblom ◽  
A Legnehed ◽  
...  
Keyword(s):  
Plasminogen Activator Inhibitor ◽  
Rat Plasma ◽  
Clot Lysis ◽  
Fibrin Deposition ◽  
Plasminogen Activator Inhibitor 1 ◽  
Fab Fragment ◽  
Dose Dependent Decrease ◽  
Pai 1

SummaryThe aim of this study was to investigate the anti-thrombotic effects of an inhibitor of the plasminogen activator inhibitor-1 (PAI-1) in rats given endotoxin. In studies in vitro, PRAP-1, a Fab-fragment of a polyclonal antibody against human PAI-1, was shown to inhibit PAI-1 activity in rat plasma as well as to stimulate clot-lysis of the euglobulin fraction derived from rat plasma. Endotoxin administered to anaesthetised rats produced a marked increase in plasma PAI-1 activity. To study fibrin formation and lysis in vivo after intravenous (i. v.) injection of the coagulant enzyme batroxobin, 125I-fibrinogen was administered to the animals. The thrombi formed by batroxobin were rapidly lysed in control animals, while the rate of lysis was markedly attenuated in rats given endotoxin. PRAP-1 was administered i.v. (bolus + infusion) to rats given endotoxin and batroxobin and the PAI-1 inhibitor caused a dose-dependent decrease in the 125I-fibrin deposition in the lungs. An immunohistochemical technique was used to confirm this decrease in density of fibrin clots in the tissue. Furthermore, PRAP-1 decreased plasma PAI-1 activity in the rats and this reduction was correlated to the decrease in lung 125I-fibrin deposition at the corresponding time point. It is concluded that in this experimental model the PAI-1 antibody PRAP-1 may indeed inhibit thrombosis in animals exposed to endotoxin.

The Effects of Brinolase (Fibrinolytic Enzyme from Aspergillus Oryzae) on Platelet Aggregation of Dog and Man

1972 ◽  
Vol 28 (01) ◽  
pp. 031-048 ◽  
Author(s):  
W. H. E Roschlau ◽  
R Gage
Keyword(s):  
Platelet Aggregation ◽  
Aspergillus Oryzae ◽  
Degradation Products ◽  
Blood Platelet ◽  
Human Platelets ◽  
Fibrinolytic Enzyme ◽  
Inhibitory Effects ◽  
Blood Platelet Aggregation

SummaryInhibition of blood platelet aggregation by brinolase (fibrinolytic enzyme from Aspergillus oryzae) has been demonstrated with human platelets in vitro and with dog platelets in vivo and in vitro, using both ADP and collagen as aggregating stimuli. It is suggested that the optimal inhibitory effects of brinolase occur indirectly through the generation of plasma fibrinogen degradation products, without compromising platelet viability, rather than by direct proteolysis of platelet structures.

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