Purification and characterization of the extracellular proteinase of Pseudomonas fluorescens NCDO 2085

The Journal of Dairy Research
D J Fairbairn, B A Law

Abstract

Pseudomonas fluorescens NCDO 2085 produced a single heat-stable extracellular proteinase in Na caseinate medium at 20 degrees C and pH 7.0. The proteinase was purified to electrophoretic homogeneity using chromatofocusing, gel filtration and ion-exchange chromatography. The purification procedure resulted in a 158-fold increase in the specific activity and a yield of 3.5% of the original activity. The enzyme is a metalloproteinase containing Zn and Ca, with an isoelectric point at 5.40 +/- 0.05 and a mol. wt of 40 200 +/- 2100. It is heat-stable having D-values at 74 and 140 degrees C of 1.6 and 1.0 min respectively; 40 and 70% of the original activity remained after HTST (74 degrees C/17 s) and ultra high temperature (140 degrees C/4 s) treatments respectively. The amino acid composition of the proteinase was determined and compared with those from other Pseudomonas spp.

References

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Jun 24, 1975·Biochimica Et Biophysica Acta·L Carrick, R S Berk
Dec 1, 1977·Journal of General Microbiology·B Wretlind, T Wadström
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Citations

May 1, 1993·The Journal of Dairy Research·H KumuraZ Saito
Sep 6, 2000·Journal of Applied Microbiology·R Koka, B C Weimer
Feb 1, 1987·The Journal of Applied Bacteriology·D J Fairbairn, B A Law

Related Concepts

Molecular Sieve Chromatography
SDS-PAGE
Isoelectric Point
Endopeptidases
Pseudomonas fluorescens

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