Open AccessCharacterization of a metalloprotease from psychrophilic Xanthomonas maltophilia
Author(s) -
Margesin Rosa,
Schinner Franz
Publication year - 1991
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1991.tb04538.x
Subject(s) - psychrophile , xanthomonas , microbiology and biotechnology , stenotrophomonas maltophilia , biology , chemistry , bacteria , pseudomonas aeruginosa , genetics
Summary An extracellular protease from psychrophilic Xanthomonas maltophilia isolated from alpine environment was purified and characterized. In spite of a comparable growth at 10°C and 20°C, protease excretion occured only at 10°C. The enzyme was a 21‐kDa protein with an isoelectric point higher than 9.5. The optimum pH and temperature for azocaseinolytic activity were 8.0 and 50°C respectively. The enzyme was stable up to 40°C but became inactive after 10 min at 60°C. The energy of activation was comparable to that of enzymes from mesophilic sources. Sensitivity to EDTA indicates that X. maltophilia protease is a metalloprotease.