Purification and Characterization of a Dipeptidase from Pseudomonas fluorescens ATCC 948

Purification and characterization of a proteinaceous compound from Pseudomonas fluorescens ATCC 948 with inhibitory activity against some Gram-positive and Gram-negative bacteria of dairy interest

Purification and Characterization of a Dipeptidase from Streptococcus cremoris Wg2.

A dipeptidase was purified to homogeneity from a crude cell extract of Streptococcus cremoris Wg2 by DEAE-Sephacel column chromatography followed by preparative disc gel electrophoresis. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme showed a single protein band with a molecular weight of 49,000. The dipeptidase is capable of hydrolyzing a range of dipeptides, ...

Purification and properties of nucleoside hydrolase from Pseudomonas fluorescens.

An enzyme which catalyzes the hydrolytic cleavage of various ribonucleosides to free base and ribose components has been obtained from cells of Pseudomonas fluorescens and purified about 300-fold by fractionation with protamine sulfate, ammonium sulfate, alumina Cy, and diethylaminoethyl cellulose. The preparation thus purEed catalyzes the hydrolysis of about 50 moles of uridine per min per mg ...

Purification and characteristics of aspartate transcarbamylase from Pseudomonas fluorescens.

Aspartate transcarbamylase from a Pseudomonas fluerescens has been purified to homogeneity. The enzyme has a molecular weight of 360,000. It is composed of 2 apparently identical subunits with molecular weights of 180,000. Activity can be recovered from the enzyme denatured with mercaptoethanol and sodium dodecyl sulfate when the dodecyl sulfate is dialyzed away. The renatured enzyme has the mo...

Purification and Characterization of a Thermostable Neutrophilic Metalloprotease from Pseudomonas sp. DR89

A novel neutrophilic metalloprotease was isolated from Pseudomonas sp. DR89 isolate which was identified ina mineral spring in Iran. The enzyme was purified from the isolate to 21-folds in a three-step procedure involving ammonium sulfate precipitation, Q-Sepharose ionic exchange and Sephadex G-100 gel filtrationchromatography. Resuts showed that the enzyme was active at high temper...