Pancreatic pseudocyst fluid–a mixture of plasma proteins and pancreatic juice possessing a high proteolytic activity

1989 ◽  
Vol 49 (5) ◽  
pp. 403-412
Author(s):  
A. R. Lasson ◽  
J. Göuransson ◽  
K. Ohlsson
2010 ◽  
Vol 28 (No. 4) ◽  
pp. 280-289 ◽  
Author(s):  
P. Miller ◽  
M.E. Haveroen ◽  
K. Solichová ◽  
R. Merkl ◽  
L.M. McMullen ◽  
...  

During a 15-month period, samples of commercially pasteurised liquid whole egg (LWE) were tested for the presence of spoilage microflora. The total bacterial counts were 2.2 ± 0.6 log CFU/g and total lactic acid bacteria (LAB) counts were 1.9 ± 0.6 log CFU/g. Enterobacteriaceae were detected in 2 samples. Out of the tested samples, 45 LAB were isolated and identified, with 30 strains identified as Enterococcus faecium, 12 as Enterococcus faecalis, and 3 as Lactobacillus paracasei subsp. paracasei. All strains, except 6 strains of E. faecium, possessed lipolytic activity. All the E. faecalis strains and one strain of E. faecium showed a high proteolytic activity, while moderate proteolytic activity was shown by 3 lactobacilli strains. Minimum inhibitory concentration (MIC) of nisin and Micocin X was measured against groups of isolated strains, and ranged from 10.4 µg/ml to 41.7 µg/ml for nisin and from 0.2 mg/ml to 1.6 mg/ml for Micocin X. The LWEs supplemented with 6.25 mg/l of nisin or with 500 mg/ml of Micocin X were pasteurised at 65°C for 2.5 minutes. The shelf life of LWE with the addition of nisin or Micocin X stored under refrigerator conditions was extended by a minimum of 5 weeks.


Parasitology ◽  
1960 ◽  
Vol 50 (3-4) ◽  
pp. 531-550 ◽  
Author(s):  
R. A. Neal

The proteolytic activity of extracts ofEntamoeba histolyticahas been further investigated. Casein and gelatin, but not haemaglobin, were hydrolysed. Activity was observed in the pH range 5·8 to 8·5 with optimal activity at pH 7·5 to 7·9. Activity was optimal at 37° C. and sulphydryl groups were not required. Concomitant bacteria showed no proteolytic activity. Hyaluronidase, collagenase and lecithinase could not be detected.An inhibitor of proteolytic enzyme was present in sera of all animals tested and in egg yolk. All culture media prepared from eggs were inhibitory, but inspissation or dilution of serum inactivated the serum inhibitor. Purified trypsin inhibitors from lima and soy bean were not active against the amoebic enzyme. Proteolytic enzymes were not secreted extracellularlyin vitro.High proteolytic activity was found in two out of five invasive, freshly isolated, strains ofE. histolyticaand after two series of liver passages of a single strain. The significance of these observations is discussed. It is concluded that the present evidence does not convincingly demonstrate that high proteolytic activity is required for tissue invasion by amoebae, but may accompany another factor.


Author(s):  
O. K. Dzhalalova ◽  
V. A. Aleinik ◽  
M. A. Zhuraeva ◽  
S. M. Babich ◽  
Sh. Kh. Khamrakulov

The effect of various concentrations of fat hydrolysis products on the pancreatic and gastric juices OPA using casein-fat emulsion (casein + tributyrin, casein + sunflower oil) was studied. It is concluded that the hydrolysis products of sunflower oil, contributes to a significant decrease in pancreatic juice OPA, which are less pronounced under the influence of tributyrin hydrolysis products.The hydrolysis products of both sunflower oil and tributyrinare less pronounced in an acidic environment to reduce the gastric juice OPA. An increase in the concentration of both sunflower oil and tributyrin in the emulsion with casein contributes to a significant increase in pancreatic juice OPA. At the same time, the effect of tributyrinis less pronounced than when using sunflower oil. At the same time, an increase in the concentration of both tributyrin and sunflower oil to a lesser extent affects the increase in the gastric juice gastric arteries.


2012 ◽  
Vol 52 (3) ◽  
pp. 368-373 ◽  
Author(s):  
Maryam Ajamhassani ◽  
Arash Zibaee ◽  
Jalal Sendi ◽  
Hassan Askary ◽  
Nasser Farrar

Proteolytic Activity in the Midgut of the Crimson Speckled MothUtethesia PulchellaL. (Lepidoptera: Arctiidae)Samples were prepared from the midgut of 4th instar larvae of the crimson speckled mothUtethesia pulchellaL. to find proteolytic activity and properties. Result revealed the presence of high proteolytic activity in the midgut when taking into account specific proteinases including trypsin-like, chymotrypsin-like, elastase and two exopeptidase (aminopeptidase and carboxipeptidase). The optimal pH of general protease was 8 and 7 when using azocasein and hemoglobin as general substrates, respectively. The optimal temperature of the total proteolytic activity in the midgut ofU. pulchellawas 25°C and 30°C when using azocasein and hemoglobin, respectively. Proteolytic activity was inhibited significantly by soybean trypsin inhibitor (SBTI), phenylmethylsulfonyl fluoride (PMSF), trypsin inhibitor (TLCK), chymotrypsin inhibitor (TPCK) and Phenanthroline. These results provide evidences for the presence of serine proteinases as the major proteases in the midgut ofU. pulchella;a key rangeland pest in warm climates. The interaction between digestive proteases and protease inhibitors have potentially important consequences for pest management programs.


1971 ◽  
Vol 25 (2) ◽  
pp. 235-241 ◽  
Author(s):  
S. Lepkovsky ◽  
F. Furuta ◽  
Mildred K. Dimivk

1. One reason, based on indirect evidence, advanced in explanation of the low nutritional value of raw soya bean (RS) is that it stimulates the pancreas to secrete massive amounts of protein which are ultimately lost in the faeces. This theory has been investigated directly.2. The expected outpouring of pancreatic protein did not occur when the secretion of enzymes and protein in pancreatic juice from chickens and rats given successively heated soya bean (HS) and RS diets was measured directly.3. It is suggested that RS, acting upon intestinal proteins, forms trypsin inhibitor-protein complexes which, in spite of adequate proteolytic activity, escape digestion and are lost with the faeces, thus decreasing the nutritional value of the diet.


1974 ◽  
Vol 53 (2) ◽  
pp. 502-502 ◽  
Author(s):  
I. Ishikawa ◽  
T. Noguchi ◽  
S. Kinoshita

2019 ◽  
Vol 49 (2) ◽  
pp. 77-84 ◽  
Author(s):  
V. G. Vertiprakhov ◽  
K. V. Borisenko

The paper presents the results of feeding crossbred laying hens of Hisex White breed, one year of age, suffering from chronic fistulae of the main pancreatic duct, on the wheat-soya diet supplemented with exogenous protease. The scope of the study covered the effect of enzymatic preparation Axtra Pro® on exocrine pancreatic function of hens, diet nutrients digestibility, digestive enzyme activity and blood biochemical values. Enzymatic activity of1 gof preparation Axtra Pro® amounted to 897 ± 47.5 mg of casein split during 1 minute (mg/(ml per min), which is 77.6% higher compared to preparation Pancreatine. Supplementing feed with the preparation Axtra Pro® (100g/t of feed) did not affect the amount of pancreatic juice, there were no changes in secretory enzymatic activity. The analysis of postprandial enzyme secretion dynamics made it possible to conclude that when laying hens were fed on the wheat-soya diet supplemented with exogenous protease, there was a decrease in proteolytic activity of the pancreatic juice during the first 60 min after the feed intake. After 150 min, i.e. during the neurohumoral phase of the regulation of pancreatic enzyme secretion, there was a rise in proteolytic activity. At the same time protease activity did not undergo insignificant changes during the experiment; digestibility of protein increased by 1.2% compared to the control group. Supplementing diet with the preparation Axtra Pro® (100 g/t of feed) led to the decrease in the activity of alkaline phosphatase in hens’ blood plasma by 47.8%, and glucose concentration by 9.2% compared to the control group, which proves a positive effect of the preparation on the function of digestive glands.


Parasitology ◽  
1990 ◽  
Vol 101 (1) ◽  
pp. 57-60 ◽  
Author(s):  
P. Bózner ◽  
P. Demeš ◽  
J. Štefanovič

SUMMARYCell extracts of an entero-invasive protozoon of squirrel monkeys,Tritrichomonas mobilensis, contained relatively high proteolytic activity, measured on hide powder azure (HPA). Multiple proteinase forms, optimally active at pH 5–7, were detected by electrophoretic analysis in gelatin-containing polyacrylamide gels. Three major proteinase bands of apparent low molecular weights,Mr18, 23 and 30 kDa, were seen on gels. Inhibition-activation studies suggest that only cysteine proteinases were involved in HPAase and gelatinolytic activities ofT. mobilensiscell extracts.


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