Proteolytic activity of a yeast cell wall lytic Arthrobacter species.
OBJECTIVE
To investigate properties of the proteolytic activity of a yeast cell wall lytic soil bacterium identified as an Arthrobacter species.


RESULTS
The organism was grown at pH 7.5 and 30 degrees C in shake flasks on media with different complex subtrates. Highest proteolytic activity assayed with azocaseine was detected in media with wheat gluten. In addition, l-leucine, l-alanine exopeptidase activity and esterase activity were found. The proteolytic activity showed stability up to pH 12, with a maximum at pH 11. The temperature optimum was at 55 degrees C, but there was a loss in enzyme activity of 50% within 2 h. The proteolytic activity was inhibited by 3,4-dichloroisocumarin, whereas there was little or no effect with EDTA, pepstatin A or E64.


CONCLUSIONS
The proteolytic activity is highly alkaline stable. The formation of the enzyme can be induced by media with high protein content.
Adamitsch
B F
BF
Institute of Chemical Engineering, Vienna University of Technology, Vienna, Austria. bernhard.adamitsch@tuwien.ac.at
Karner
F
F
Hampel
W
W
D001173:Arthrobacter / Q000254:growth & development / Q000378:metabolism*; D002364:Caseins / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D003470:Culture Media; D010450:Endopeptidases / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008666:Metalloendopeptidases / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D012988:Soil Microbiology; D013379:Substrate Specificity; D013696:Temperature
D002364:Caseins; D003470:Culture Media; C026018:azocasein; D010450:Endopeptidases; D008666:Metalloendopeptidases; C030895:caseinase