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An inhibition enzyme-linked immunosorbent assay was developed to detect low levels of the proteases extracted from four strains of Pseudomonas fluorescens. The assay detected between 0.24 and 7.8 ng of protease per ml of ultrahigh-temperature-treated milk and could be completed within 6 h. It could be used as a framework for a test system for quantifying(More)
The labile non-allosteric form of phosphofructokinase (ATP:D-fructose-6-phosphate 1-phosphotransferase, EC was purified to a specific activity of 107 U/mg (2078-fold) from aerobic cultures of Escherichia coli K-12. The enzyme has an isoelectric point (pI) of 5.1, a native molecular weight of 67 000 +/- 3000 and a subunit weight of 34 000 +/- 400.(More)
The physicochemical properties of eight extracellular proteinases secreted by psychrotrophic bacteria of dairy origin have been studied. Seven of these proteinases were able to withstand ultra heat treatment (UHT) with D values at 140 degrees C ranging from 2 to 300 s. The six Pseudomonas fluorescens proteinases were glycoproteins of mol. wt 47000-49500.(More)
Eighty-seven proteolytic psychrotrophic micro-organisms were isolated from 11 bulk milk supplies of two Queensland factories from different climatic regions, before and after storage at 4 degrees C for 7 d. These isolates together with 15 reference strains formed the basis of a numerical taxonomic study involving 81 attributes. All but six isolates were(More)
In crude cell-free extracts of aerobically grown E. coli K-12, the non-allosteric form of 6-phosphofructokinase has a tetrameric molecular weight 140 000 with a low affinity (less than 5%) for the blue dextran chromophore--Cibacron Blue. The allosteric form has the same tetrameric molecular weight, but possesses a strong affinity for the blue dextran(More)
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