The bacterium Variovorax as paradoxus, grown in a minimal medium in which s
ilk 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 pll For activity was foun
d 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 magnesi
um. Gel permeation chromatography and SDS-PAGE provided evidence that the n
ative enzyme is a monomer with a M-r of ca. 21 kDa. (C) 2001 Elsevier Scien
ce Ltd. All rights reserved.