PURIFICATION AND PROPERTIES OF A PROTEASE FROM PENICILLIUM CYANEO-FULVUM

1960 ◽  
Vol 38 (1) ◽  
pp. 969-980 ◽  
Author(s):  
Kartar Singh ◽  
S. M. Martin
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
Proteolytic Enzyme ◽  
Ethylenediaminetetraacetic Acid ◽  
Alkaline Proteases ◽  
Plasma Albumin ◽  
Metal Chelating ◽  
Bovine Plasma ◽  
Purification And Properties ◽  
Optimum Ph

A proteolytic enzyme present in culture filtrates of Penicillium cyaneo-fulvum was purified approximately 100-fold. In the ultracentrifuge the enzyme behaved as a homogeneous protein, but on electrophoresis some contamination was apparent. The molecular weight of the enzyme was estimated to be about 45,000.The protease hydrolyzed casein and denatured haemoglobin, gelatin, and native bovine plasma albumin but not native or denatured ovalbumin. It also coagulated milk. The optimum pH for caseolysis was 9.5 to 11.0. Metal chelating- and sulphydryl-reagents did not affect enzyme activity but zinc and mercurous ions inhibited the enzyme, the inhibition being reversed with ethylenediaminetetraacetic acid (EDTA). Soybean trypsin inhibitor was without effect on the enzyme whereas ovomucoid inhibited the enzyme. Although it is similar in some respects to other alkaline proteases, the P. cyaneo-fulvum enzyme does not appear to be identical with any one of them.

PURIFICATION AND PROPERTIES OF A PROTEASE FROM PENICILLIUM CYANEO-FULVUM

1960 ◽  
Vol 38 (9) ◽  
pp. 969-980 ◽  
Author(s):  
Kartar Singh ◽  
S. M. Martin
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
Proteolytic Enzyme ◽  
Ethylenediaminetetraacetic Acid ◽  
Alkaline Proteases ◽  
Plasma Albumin ◽  
Metal Chelating ◽  
Bovine Plasma ◽  
Purification And Properties ◽  
Optimum Ph

A proteolytic enzyme present in culture filtrates of Penicillium cyaneo-fulvum was purified approximately 100-fold. In the ultracentrifuge the enzyme behaved as a homogeneous protein, but on electrophoresis some contamination was apparent. The molecular weight of the enzyme was estimated to be about 45,000.The protease hydrolyzed casein and denatured haemoglobin, gelatin, and native bovine plasma albumin but not native or denatured ovalbumin. It also coagulated milk. The optimum pH for caseolysis was 9.5 to 11.0. Metal chelating- and sulphydryl-reagents did not affect enzyme activity but zinc and mercurous ions inhibited the enzyme, the inhibition being reversed with ethylenediaminetetraacetic acid (EDTA). Soybean trypsin inhibitor was without effect on the enzyme whereas ovomucoid inhibited the enzyme. Although it is similar in some respects to other alkaline proteases, the P. cyaneo-fulvum enzyme does not appear to be identical with any one of them.

CHARACTERISTICS OF AN EXTRACELLULAR PROTEINASE FROM MICROCOCCUS FREUDENREICHII

1958 ◽  
Vol 4 (3) ◽  
pp. 237-242 ◽  
Author(s):  
I. Husain ◽  
I. J. McDonald
Keyword(s):  
Enzyme Activity ◽  
Extracellular Proteinase ◽  
Plasma Albumin ◽  
Cheese Ripening ◽  
Bovine Plasma ◽  
Optimum Ph ◽  
Β Lactoglobulin

An extracellular proteinase from Micrococcus freudenreichii is described. The enzyme hydrolyzes casein and crystalline β-lactoglobulin rapidly and crystalline bovine plasma albumin very slowly. The enzyme is most active at 50 °C. but is essentially inactivated in 15 minutes at 60 °C. The optimum pH for enzyme activity is 5.5 to 6.4. The possible role of the proteinase in cheese ripening is discussed.

An extracellular proteolytic enzyme from Scopulariopsis brevicaulis. 1. Purification and properties

1971 ◽  
Vol 17 (8) ◽  
pp. 1029-1042 ◽  
Author(s):  
Kartar Singh ◽  
Claude Vézina
Keyword(s):  
Proteolytic Enzyme ◽  
Deae Cellulose ◽  
Alkaline Proteases ◽  
Casein Hydrolysis ◽  
Purification And Properties ◽  
Optimum Ph ◽  
Sh Reagents ◽  
Extracellular Proteolytic Enzyme ◽  
Scopulariopsis Brevicaulis ◽  
Insulin Chains

A proteolytic enzyme present in culture filtrates of Scopulariopsis brevicaulis was purified about 200-fold by (NH4)2SO4 and ethanol fractionations followed by chromatography on DEAE-cellulose, DEAE-Sephadex, and hydroxylapatite. Ultracentrifugation of the purified enzymes showed only one sedimenting component and its molecular weight was estimated to be about 24 000. The protease hydrolyzed casein, urea-denatured hemoglobin, gelatin, fibrinogen, fibrin, insulin chains A and B, but not human serum albumin or ovalbumin. It also coagulated milk. The enzyme had no action on the various peptides tested and showed low esterase activity. Optimum pH for casein hydrolysis was 10.5 to 11; for hemoglobin hydrolysis 7.0–9.5, and for gelatin hydrolysis, 6.0–8.0. The enzyme activity was unaffected by most metal ions, SH-reagents, and some natural trypsin inhibitors. The protease was strongly inhibited by diisopropylfluorophosphate and phenylmethanesulfonyl fluoride. Although similar in some respects to CA-7, the enzyme isolated from Aspergillus oryzae, and other alkaline proteases, the S. brevicaulis protease does not appear to be identical with any one of them.

Extracellular alkaline phosphatase from marine bacteria: purification and properties of extracellular phosphatase from a marine Pseudomonas sp.

1980 ◽  
Vol 26 (7) ◽  
pp. 833-838 ◽  
Author(s):  
Hiromi Kobori ◽  
Nobuo Taga
Keyword(s):  
Molecular Weight ◽  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Marine Bacteria ◽  
Divalent Cations ◽  
Maximal Activity ◽  
Pseudomonas Sp ◽  
Purification And Properties ◽  
Extracellular Alkaline Phosphatase ◽  
Increased Pressure

Extracellular alkaline phosphatase produced by a marine Pseudomonas was purified to electrophoretic homogeneity. The molecular weight of the enzyme was estimated to be 100 000. The enzyme had maximal activity at pH 11.5. The enzyme was completely inhibited by 1 mM EDTA. However, divalent cations reversed the enzyme inhibition and their order of effectiveness on the reaction was Zn2+ > Ca2+ > Mn2+ > Mg2+ > Sr2+ > Co2+. The enzyme activity was affected by the species of anion whose order of effectiveness was demonstrated to follow the lyotrophic series, Cl− > Br− > NO3−> ClO4− > SCN−. The activity of phosphatase was accelerated linearly by increased pressure until up to 1000 atm (1 atm = 101.325 kPa), and the enzyme activity at 1000 atm was 3.2 times higher than that at 1 atm.

Characterisation of a Neutral Protease Produced by Micrococcus luteus

1996 ◽  
Vol 51 (5-6) ◽  
pp. 429-431 ◽  
Author(s):  
M.O. Ilori ◽  
O.O. Amund ◽  
O. Omidiji
Keyword(s):  
Molecular Weight ◽  
Citric Acid ◽  
Proteolytic Enzyme ◽  
Micrococcus Luteus ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Optimum Temperature ◽  
Optimum Ph

Abstract A proteolytic enzyme produced by a cassava-ferment­ing strain of Micrococcus luteus was extracted and puri­fied 50-fold by gel filtration and ion exchange chromatography. The optimum pH for the enzyme was 7.0, the optimum temperature 25 °C, the apparent molecular weight 42 kDa and the Km value, 0.45 mg ml-1 with casein as substrate. The enzyme was stimulated by Ca2+ and Mg2+ but inhibited by Zn2+ and Co2+ ions. Other inhibitors were EDTA, KCN, citric acid and L-cysteine indicating the enzyme to be a metalloprotease.

Purification and properties of an exocellular β-glucosidase of Candida molischiana (Zikes) Meyer and Yarrow capable of hydrolyzing soluble cellodextrins

1985 ◽  
Vol 63 (11) ◽  
pp. 1160-1166 ◽  
Author(s):  
Pierre Gondé ◽  
Robert Ratomahenina ◽  
Alain Arnaud ◽  
Pierre Galzy
Keyword(s):  
Molecular Weight ◽  
Ion Exchange ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Optimum Temperature ◽  
Purification And Properties ◽  
Optimum Ph

The exocellular enzyme β-glucosidase of Candida molischiana was studied. This strain is able to ferment soluble cellodextrins. The enzyme was partially purified by ion-exchange chromatography and gel filtration. The molecular weight of this enzyme was 120 000; its optimum pH was between 4 and 4.5 and its optimum temperature was 60 °C. This enzyme was active against different soluble glucosides and was inhibited by p-chloromercuribenzoate, gluconolactone, and glucose. A "glucosyltransferase" activity appeared in the presence of ethanol. The biosynthesis of the enzyme was constitutive but repressed by glucose.

scholarly journals THE NUMBER OF POLYPEPTIDE CHAINS IN BOVINE PLASMA ALBUMIN

1956 ◽  
Vol 34 (2) ◽  
pp. 160-169 ◽  
Author(s):  
M. E. Reichmann ◽  
J. Ross Colvin
Keyword(s):  
Molecular Weight ◽  
Light Scattering ◽  
Sodium Chloride ◽  
Sedimentation Velocity ◽  
Performic Acid ◽  
Sedimentation Equilibrium ◽  
Plasma Albumin ◽  
Disulphide Bonds ◽  
Bovine Plasma ◽  
Polypeptide Chains

The molecular weight of performic acid oxidized bovine plasma albumin, dispersed in 0.08 M borate +0.2 M sodium chloride buffer, pH 7.4, was estimated as 30,000 by light-scattering and sedimentation equilibrium methods, 19,000 by osmotic pressure. Sedimentation velocity analyses and electrophoresis showed that the component polypeptide chains of the material are similar in mass and charge density so the polydispersity must be attributed to labile aggregates. The results indicate that here are at least three and probably four similar polypeptide chains in the molecule of native bovine plasma albumin, held together by disulphide bonds.

scholarly journals The Comparative Study of Papain Enzyme from Papaya Fruits California variant and Indonesian Local variant

2018 ◽  
Vol 19 (2) ◽  
pp. 42-48
Author(s):  
Diah Ratna Ningrum ◽  
Wawan Kosasih ◽  
Sri Priatni
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
Proteolytic Enzyme ◽  
Enzyme Properties ◽  
Specific Enzyme ◽  
Specific Enzyme Activity ◽  
Local Variant ◽  
Papaya Latex ◽  
Almost All ◽  
The Comparative Study

Papain (E.C.3.4.22.2) is a proteolytic enzyme which has important role due toits diverse uses in textile, pharmaceutics, cosmetics and food industries.Papain enzyme can be found in almost all parts of the papaya plant and mostof the stem and fruit. The objective of this study is to compare the Californiavar. and Indonesian local var. of papaya fruits, in papain production and alsoto characterize the enzyme properties. Results showed that the highest yield ofcrude papain was obtained from local papaya latex (24.87%) whichprecipitated by ethanol with ratio of 1:2. The highest of activity enzyme,soluble protein and specific enzyme activity obtained from the local papayawere 3154 ± 11.31unit/mL, solubility protein of 0.94± 0.08 mg/mL andspesific enzyme activity of 3355.32 unit/mg protein, respectively. The activityof enzyme fraction F7 obtained from purification by DEAE sepharose columnwas 202.33 U/mL dan the molecular weight of this fraction was between 17-28 kDa.© 2

scholarly journals PREPARATION, PURIFICATION AND PROPERTIES OF LIPASE FROM HEPATOPANCREAS OF TRA (PANGASIUS) CATFISH

2011 ◽  
Vol 14 (3) ◽  
pp. 5-11
Author(s):  
Thy Bao Vuong ◽  
Lam Bich Tran ◽  
Duan Luu
Keyword(s):  
Heavy Metals ◽  
Molecular Weight ◽  
Enzyme Activity ◽  
Crude Extract ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Purification And Properties ◽  
Temperature Optima

Lipase from the hepatopancreas of Tra (Pangasius) catfish was purified by ammonium sulfate fractionation, followed by ion-exhange chromatography on DEAE Cellulose and gel filtration Sephadex G-75. The preparation was homogeneous on polyacrylamide disc gel electrophoresis. The specific activity of the purified enzyme was 37.95 times higher than that of the crude extract. The enzyme showed a molecular weight of 57000 Da. The pH and temperature optima of purified lipase were 8 and 500C respectively. Enzyme activity was enhanced by Ca2+ but inhibited by heavy metals Zn2+, Cd2+, Mg2+.

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