Acidic extracellular proteases from microrganisms of fairly acidic niche.
The protein population secreted from three wine-contaminant microorganisms was studied by two-dimensional electrophoresis and screened for proteases. Proteolytic enzymes were electrophoretically purified and their activity, optimum pH and temperature determined. The protease of Acetobacter aceti maintained its activity over the range of pHs 3.0-5.0, thus being of potential biotechnological interest.
Bossi
Alessandra
A
Department of Science and Technology, University of Verona, Strada le Grazie 15, 37134 Verona, Italy. alessandra.bossi@univr.it
Bonizzato
Luca
L
Zapparoli
Giacomo
G
D000091:Acetobacter / Q000201:enzymology*; D001203:Ascomycota / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007778:Lactobacillus / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000502:physiology*
D010447:Peptide Hydrolases