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A bacterial extracellular proteinase degrading silk fibroin
No full textThe bacterium Variovorax paradoxus, grown in a minimal medium in which silk fibroin represents the sole source of carbon and nitrogen, produces an extracellular protease that hydrolyzes fibroin as well as casein and, to a smaller extent, collagen and albumin. The optimal pH for activity was found to be in the acid range (optimum pH 5.8–6.4) and the enzyme activity was stimulated by the addition of divalent cations, either manganese or magnesium. Gel permeation chromatography and SDS-PAGE provided evidence that the native enzyme is a monomer with a Mr of ca. 21 kDa
Resistance to azetidin-2-carboxylic acid and sodium chloride tolerance in carrot cell cultures and Spirulina platensis.
No full textMutants of Spirulina platensis and of Daucus carota resistant to azetidine-2carboxylic acid were tested for NaCl tolerance. A positivr correlation was found between proline overproduction and osmotolerance. In carrot lines proline overproduction was not strictly proportional to NaCl tolerance insofar as cells chracterized by differences in proline overproduction showed similar osmotolerance, suggesting that pother factors could be involved
Identificazione dei geni codificanti per gli enzimi catalasi e acyl-carrier protein in Mycobacterium avium.
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