scholarly journals Purification and Characterization of an Extracellular Protease Produced by Pseudomonas fluorescens M3/6

1991 ◽  
Vol 74 (12) ◽  
pp. 4125-4136 ◽  
Author(s):  
K.L. Kohlmann ◽  
S.S. Nielsen ◽  
M.R. Ladisch
Keyword(s):  
Pseudomonas Fluorescens ◽  
Extracellular Protease ◽  
Purification And Characterization

scholarly journals Purification and characterization of an extracellular protease from Pseudomonas cepacia.

1989 ◽  
Vol 57 (3) ◽  
pp. 771-778 ◽  
Author(s):  
A I McKevitt ◽  
S Bajaksouzian ◽  
J D Klinger ◽  
D E Woods
Keyword(s):  
Extracellular Protease ◽  
Pseudomonas Cepacia ◽  
Purification And Characterization

Purification and characterization of an extracellular protease from Flavobacterium arborescen

1983 ◽  
Vol 132 (1) ◽  
pp. 41-49 ◽  
Author(s):  
George Boguslawski ◽  
Janice L. Shultz ◽  
Clifford O. Yehle
Keyword(s):  
Extracellular Protease ◽  
Purification And Characterization

Purification and Characterization of Three Extracellular Proteinases Produced by Pseudomonas fluorescens INIA 745, an Isolate from Ewe's Milk

1999 ◽  
Vol 62 (5) ◽  
pp. 543-546 ◽  
Author(s):  
J. FERNÁNDEZ ◽  
A. F. MOHEDANO ◽  
P. GAYA ◽  
M. MEDINA ◽  
M. NUÑEZ
Keyword(s):  
Pseudomonas Fluorescens ◽  
Culture Medium ◽  
Inhibitory Effect ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Purification And Characterization ◽  
Ph Optimum ◽  
Extracellular Proteinases ◽  
Ewe's Milk

Three proteinases were isolated from culture medium of Pseudomonas fluorescens INIA 745 and purified to homogeneity by a combination of Phenyl-Sepharose, DEAE-Sepharose, and Sephadex G-100 chromatography. Optimal temperature for enzymatic activity was 45°C for all three proteinases. The pH optimum of proteinases I and II was found to be 7.0, while that of proteinase III was 8.0. Divalent metal ions like Cu2+, Co2+, Zn2+, Fe2+, and Hg2+ were inhibitory to proteinase activity while Ca2+, Mg2+, and Mn2+ had little or no inhibitory effect. The three enzymes were strongly inhibited by EDTA and 1,10-phenantroline and partially by cysteine. The three enzymes are metalloproteinases since they were inhibited by chelators and reactivated by Co2+, Mn2+, Cu2+, and Zn2+. The Km values of proteinases I, II, and III for casein were calculated to be 3.2, 2.6, and 5.2 mg/ml, respectively. Proteinases II and III rapidly degraded β-casein, with preference to αs1-casein, whereas proteinase I hydrolyzed both casein fractions at a slow rate.

PURIFICATION AND CHARACTERIZATION OF AN ENDOPEPTIDASE FROM PSEUDOMONAS FLUORESCENS ATCC 948

1998 ◽  
Vol 22 (1) ◽  
pp. 17-35 ◽  
Author(s):  
MARCO GOBBETTI ◽  
EMANUELE SMACCHI ◽  
LESZEK STEPANIAK ◽  
FRANCESCA CREA ◽  
PATRICK F. FOX
Keyword(s):  
Pseudomonas Fluorescens ◽  
Purification And Characterization
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