scholarly journals Synergistic caseinolytic activity and differential fibrinogenolytic action of multiple proteases of Maclura spinosa (Roxb. ex Willd.) latex

2015 ◽  
Vol 11 (44) ◽  
pp. 457 ◽  
Author(s):  
SNanjunda Swamy ◽  
BK Venkatesh ◽  
RaghuRam Achar ◽  
P Sharanappa ◽  
BS Priya
Keyword(s):  
Caseinolytic Activity

The Plasmin Inhibitors of Plasma

1964 ◽  
Vol 12 (01) ◽  
pp. 119-125 ◽  
Author(s):  
Y Shamash ◽  
A Rimon
Keyword(s):  
Human Plasma ◽  
New Method ◽  
Normal Amount ◽  
Caseinolytic Activity ◽  
Before And After ◽  
Plasmin Inhibitors

SummaryA new method for the assay of plasmin inhibitors in human plasma is described. The method consists of determination of the caseinolytic activity of a standard plasmin solution before and after incubation with the inhibitor, with lysine added to the mixture as a stabilizer of plasmin. Using this method, it was found that plasma contains enough inhibitors to inactivate 30 caseinolytic units of plasmin, or 10 times the normal amount of plasminogen in human plasma.

Partial characterization of cheese-ripening proteinases produced by the yeastKluyveromyces lactis

1983 ◽  
Vol 50 (4) ◽  
pp. 469-480 ◽  
Author(s):  
Paul A. Grieve ◽  
Barry J. Kitchen ◽  
John R. Dulley ◽  
John Bartley
Keyword(s):  
Molecular Weight ◽  
Kluyveromyces Lactis ◽  
Apparent Molecular Weight ◽  
Aminopeptidase Activity ◽  
Carboxypeptidase Y ◽  
Casein Hydrolysis ◽  
Cheese Ripening ◽  
Caseinolytic Activity ◽  
Proteinase A

SUMMARYAn extract ofKluyveromyces lactis416 and a β-galactosidase preparation (Maxilact 40000) contaminated with proteinase, showed similar pH profiles of caseinolytic activity. Similar modes of casein hydrolysis (κ-, > αs-, ≥ β-) were observed at pH 5·0 (the pH of Cheddar cheese), without detection of bitterness. The contaminated Maxilact preparation contained similar proteinase types to those detected in an autolysate ofK. lactis. Both the autolysate and the Maxilact preparation contained acid endopeptidase (proteinase A), serine endopeptidase (proteinase B) and serine exopeptidase (carboxypeptidase Y) activities. Some aminopeptidase activity was also detected in both preparations. There were some differences in apparent molecular weight and charge properties between proteinase A and B and carboxypeptidase Y from the 2 proteinase sources.

Isolation and properties of a collagenase with caseinolytic activity from a Pseudomonas sp.

1989 ◽  
Vol 68 (6) ◽  
pp. 399-403 ◽  
Author(s):  
Tomohiro Hisano ◽  
Shiro Abe ◽  
Michio Wakashiro ◽  
Akira Kimura ◽  
Kousaku Murata
Keyword(s):  
Pseudomonas Sp ◽  
Caseinolytic Activity

Effect of the addition of extracts of thermophilic lactobacilli on acid production byStreptococcus thermophilusin milk

1981 ◽  
Vol 48 (1) ◽  
pp. 139-148 ◽  
Author(s):  
Denis H. Hemme ◽  
Véronique Schmal ◽  
Jean E. Auclair
Keyword(s):  
Acid Production ◽  
Streptococcus Thermophilus ◽  
Lactobacillus Helveticus ◽  
Caseinolytic Activity ◽  
Hard Cheese

SummarySoluble extracts of 20 strains of thermophilic lactobacilli (Lactobacillus helveticus, L.lactisand L.bulgaricus) were prepared and added to milk for the culture of 10 strains ofStreptococcus thermophilus. Acid production was stimulated in 64·5% of cases for 9 of these 10 strains. The L.helveticusextracts were the most stimulatory, but the same extracts did not always strongly stimulate each strain ofStr. thermophilus. The stimulatory effects observed varied with the volume of extract and the strain ofStr. thermophilus. The exception wasStr. thermophilus385, which was never stimulated. The stimulatory effects observed were due to aminopeptidases present in the lactobacillus extracts and were not related to a general caseinolytic activity. The possible addition of such extracts to milk for cooked hard cheese is discussed.

scholarly journals Nonplasminogen-dependent protease in human plasma

Blood ◽  
1979 ◽  
Vol 54 (3) ◽  
pp. 607-613
Author(s):  
JA Marcum ◽  
DL Kline
Keyword(s):  
Ionic Strength ◽  
Human Plasma ◽  
Trypsin Inhibitor ◽  
Fibrinolytic Activity ◽  
Coagulation Factors ◽  
Contact Activation ◽  
Ph Optimum ◽  
Salt Addition ◽  
Caseinolytic Activity ◽  
Pancreatic Trypsin Inhibitor

Abstract Equal volumes of plasma and 0.3 M K2HPO4, pH 7.4, were mixed, diluted 20-fold, and adjusted to pH 5.2. After incubation at 37 degrees C for 30 min, the euglobulin percipitate, redissolved in 0.1 M K2HPO4, pH 7.4, developed caseinolytic activity (0.05 CTA U/ml). Na2HPO4 or NaCl of similar ionic strength could replace K2HPO4. The pH optimum of the protease was 6.5, activity falling off sharply below pH 6.0 and above 7.4. The proteolytic activity was inhibited by diisopropylphosphofluoridate and by pancreatic trypsin inhibitor, but was not inhibited by soybean trypsin inhibitor. The activity was not due to plasmin, contact activation, or coagulation factors, since it was fully generated in plasminogen-depleted, factors XII, XI, VII deficient, and prekallikrein-deficient plasmas. Purified Cl-esterase was not caseinolytic in our system. Redissolved euglobulin precipitate prepared from normal plasma without salt addition could serve as starting material for the generation of caseinolytic activity, as could serum, indicating that the Hageman factor cofactor and thrombin are not required. The protease had no detectable procoagulant or fibrinolytic activity.

Staphylococcal Exfoliative Toxin Induces Caseinolytic Activity

1987 ◽  
Vol 156 (3) ◽  
pp. 508-509 ◽  
Author(s):  
I. Takiuchi ◽  
M. Kawamura ◽  
T. Teramaro ◽  
D. Higuchi
Keyword(s):  
Exfoliative Toxin ◽  
Caseinolytic Activity

Studies on plasminogen. VIII. Species specificity of streptokinase

1969 ◽  
Vol 47 (10) ◽  
pp. 927-932 ◽  
Author(s):  
R. J. Wulf ◽  
E. T. Mertz
Keyword(s):  
Gel Electrophoresis ◽  
Continuous Flow ◽  
Species Specificity ◽  
Starch Gel Electrophoresis ◽  
Plasminogen Activation ◽  
Caseinolytic Activity ◽  
Starch Gel

Continuous-flow electrophoresis was used to isolate purified plasminogens from the serums of 10 species. The ratios of esterolytic to caseinolytic activity in the purified plasminogens with urokinase as the activator for the following animals were: rat 9.8, cow 6.6, pig 5.7, cat 3.5, sheep 3.4, mouse 3.3, rabbit 2.7, man 2.2, monkey 2.0, and dog 1.4. Plasminogen activation with streptokinase divides the species into three groups: (a) activated with small amounts of streptokinase (man, cat, monkey), (b) activated with large amounts of streptokinase (dog, rabbit), and (c) not activated (cow, sheep, pig, mouse, and rat). Streptokinase – human globulin mixture and urokinase activated all plasminogens equally well When the euglobulin fractions of the serums of nine of the ten species were subjected to starch gel electrophoresis at pH 2.5, groups a and b gave two major plasminogen bands, whereas c gave only one.

scholarly journals Improving the Thermostability and Activity of a Thermophilic Subtilase by Incorporating Structural Elements of Its Psychrophilic Counterpart

2015 ◽  
Vol 81 (18) ◽  
pp. 6302-6313 ◽  
Author(s):  
Bi-Lin Xu ◽  
Meihong Dai ◽  
Yuanhao Chen ◽  
Dongheng Meng ◽  
Yasi Wang ◽  
...  
Keyword(s):  
Industrial Applications ◽  
Amino Acid Residues ◽  
Structural Elements ◽  
Wild Type ◽  
Scanning Calorimetry ◽  
Thermostable Enzymes ◽  
Variable Regions ◽  
Enzyme Thermostability ◽  
Caseinolytic Activity ◽  
Important Challenge

ABSTRACTThe incorporation of the structural elements of thermostable enzymes into their less stable counterparts is generally used to improve enzyme thermostability. However, the process of engineering enzymes with both high thermostability and high activity remains an important challenge. Here, we report that the thermostability and activity of a thermophilic subtilase were simultaneously improved by incorporating structural elements of a psychrophilic subtilase. There were 64 variable regions/residues (VRs) in the alignment of the thermophilic WF146 protease, mesophilic sphericase, and psychrophilic S41. The WF146 protease was subjected to systematic mutagenesis, in which each of its VRs was replaced with those from S41 and sphericase. After successive rounds of combination and screening, we constructed the variant PBL5X with eight amino acid residues from S41. The half-life of PBL5X at 85°C (57.1 min) was approximately 9-fold longer than that of the wild-type (WT) WF146 protease (6.3 min). The substitutions also led to an increase in the apparent thermal denaturation midpoint temperature (Tm) of the enzyme by 5.5°C, as determined by differential scanning calorimetry. Compared to the WT, PBL5X exhibited high caseinolytic activity (25 to 95°C) and high values ofKmandkcat(25 to 80°C). Our study may provide a rational basis for developing highly stable and active enzymes, which are highly desired in industrial applications.

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