scholarly journals Metaproteomics of cellulose methanisation under thermophilic conditions reveals a surprisingly high proteolytic activity

2013 ◽  
Vol 8 (1) ◽  
pp. 88-102 ◽  
Author(s):  
Fan Lü ◽  
Ariane Bize ◽  
Alain Guillot ◽  
Véronique Monnet ◽  
Céline Madigou ◽  
...  
Keyword(s):  
Proteolytic Activity ◽  
High Proteolytic Activity ◽  
Thermophilic Conditions

scholarly journals Shelf life extension of liquid whole eggs by heat and bacteriocin treatment

2010 ◽  
Vol 28 (No. 4) ◽  
pp. 280-289 ◽  
Author(s):  
P. Miller ◽  
M.E. Haveroen ◽  
K. Solichová ◽  
R. Merkl ◽  
L.M. McMullen ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Shelf Life ◽  
Proteolytic Activity ◽  
Inhibitory Concentration ◽  
Lipolytic Activity ◽  
Life Extension ◽  
High Proteolytic Activity ◽  
Liquid Whole Egg ◽  
Spoilage Microflora ◽  
Whole Egg

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.

Enzymic Proteolysis byEntamoeba histolytica; biochemical characteristics and relationship with invasiveness

Parasitology ◽  
1960 ◽  
Vol 50 (3-4) ◽  
pp. 531-550 ◽  
Author(s):  
R. A. Neal
Keyword(s):  
Proteolytic Activity ◽  
Culture Media ◽  
Proteolytic Enzymes ◽  
Egg Yolk ◽  
Single Strain ◽  
High Proteolytic Activity ◽  
Serum Inhibitor ◽  
Sulphydryl Groups ◽  
Ph Range

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.

scholarly journals Proteolytic Activity in the Midgut of the Crimson Speckled Moth Utethesia Pulchella L. (Lepidoptera: Arctiidae)

2012 ◽  
Vol 52 (3) ◽  
pp. 368-373 ◽  
Author(s):  
Maryam Ajamhassani ◽  
Arash Zibaee ◽  
Jalal Sendi ◽  
Hassan Askary ◽  
Nasser Farrar
Keyword(s):  
Pest Management ◽  
Protease Inhibitors ◽  
Proteolytic Activity ◽  
Trypsin Inhibitor ◽  
Serine Proteinases ◽  
Optimal Temperature ◽  
Phenylmethylsulfonyl Fluoride ◽  
Chymotrypsin Inhibitor ◽  
High Proteolytic Activity ◽  
Optimal Ph

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.

High Proteolytic Activity in the Periodontal Pocket

1974 ◽  
Vol 53 (2) ◽  
pp. 502-502 ◽  
Author(s):  
I. Ishikawa ◽  
T. Noguchi ◽  
S. Kinoshita
Keyword(s):  
Proteolytic Activity ◽  
Periodontal Pocket ◽  
High Proteolytic Activity

Proteolytic activity inTritrichomonas mobilensis

Parasitology ◽  
1990 ◽  
Vol 101 (1) ◽  
pp. 57-60 ◽  
Author(s):  
P. Bózner ◽  
P. Demeš ◽  
J. Štefanovič
Keyword(s):  
Proteolytic Activity ◽  
Electrophoretic Analysis ◽  
Squirrel Monkeys ◽  
Cysteine Proteinases ◽  
Polyacrylamide Gels ◽  
Molecular Weights ◽  
High Proteolytic Activity ◽  
Cell Extracts

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.

scholarly journals CRYSTALLINE PEPSIN

1933 ◽  
Vol 16 (4) ◽  
pp. 615-623 ◽  
Author(s):  
John H. Northrop
Keyword(s):  
Gastric Mucosa ◽  
Magnesium Sulfate ◽  
Gastric Juice ◽  
Proteolytic Activity ◽  
Optical Activity ◽  
Specific Activity ◽  
Crystalline Form ◽  
High Proteolytic Activity ◽  
Related Proteins

1. A method has been described for isolating a crystalline protein with high proteolytic activity from bovine gastric juice by means of precipitation with magnesium sulfate and fractionation of the precipitate with acetone and magnesium sulfate. 2. The crystalline protein obtained in this way has the same crystalline form, optical activity, and specific activity, as determined by a number of methods, as does the crystalline protein previously isolated from swine gastric mucosa. 3. The solubility of the two preparations, however, is additive so that they are different although very closely related proteins.

scholarly journals Hydrolyzing Ability of Protease of Enzyme Complex of Cholera Vibrio that is Proteovibrin for Protein Substrates

2008 ◽  
pp. 37-39
Author(s):  
I. A. Kuzmichenko ◽  
M. N. Kireev ◽  
O. V. Gromova ◽  
V. S. Bronnikova ◽  
S. A. Nizhegorodtsev
Keyword(s):  
Molecular Weight ◽  
Proteolytic Activity ◽  
Low Molecular Weight ◽  
Enzyme Complex ◽  
Cholera Vibrio ◽  
Protein Substrates ◽  
High Proteolytic Activity ◽  
Production Strain ◽  
The Way

The way of production of low-molecular weight enzyme complex of cholera vibrio (proteovibrin) with high proteolytic activity is described. Its prevailing accumulation in ultrafiltrate of cultural liquid of M41 production strain is shown. Proteovibrin protease doesn't yield to commercial trypsin in proteolytic activity as regards some protein substrates and can be used for enzymolysate preparation.

X-ray crystal structure of CMS1MS2: a high proteolytic activity cysteine proteinase from Carica candamarcensis

Amino Acids ◽  
2012 ◽  
Vol 43 (6) ◽  
pp. 2381-2391 ◽  
Author(s):  
Marco T. R. Gomes ◽  
Raphael D. Teixeira ◽  
Míriam T. P. Lopes ◽  
Ronaldo A. P. Nagem ◽  
Carlos E. Salas
Keyword(s):  
Crystal Structure ◽  
Proteolytic Activity ◽  
Cysteine Proteinase ◽  
X Ray ◽  
High Proteolytic Activity
Sign in / Sign up

Export Citation Format

Share Document