Production and regulation of a thermostable protease by Pseudomonas sp. B45.
A Pseudomonas sp. produced an extracellular thermostable protease which required induction by peptone. Growth of the organism and the production of protease was optimum at 30 degrees C. The enzyme was subjected to catabolite repression by glucose. Both chloramphenicol and rifamycin completely abolished protease production indicating de novo synthesis of the enzyme. Leucine, lysine, histidine and glycine enhanced the protease production considerably and they were the most effective when added during the active period of production. Glucose repression could not be relieved by addition of leucine.
Chakraborty
R
R
Central Leather Research Institute, Biochemistry Laboratory, Adyar, Madras, India.
Srinivasan
M
M
D000596:Amino Acids / Q000494:pharmacology; D002701:Chloramphenicol / Q000494:pharmacology; D010450:Endopeptidases / Q000096:biosynthesis* / Q000302:isolation & purification; D004790:Enzyme Induction / Q000187:drug effects; D004794:Enzyme Repression / Q000187:drug effects; D004795:Enzyme Stability; D015971:Gene Expression Regulation, Enzymologic / Q000187:drug effects; D005947:Glucose / Q000494:pharmacology; D006358:Hot Temperature; D011549:Pseudomonas / Q000201:enzymology* / Q000302:isolation & purification; D012294:Rifamycins / Q000494:pharmacology; D013633:Tanning
D000596:Amino Acids; D012294:Rifamycins; D002701:Chloramphenicol; D010450:Endopeptidases; D005947:Glucose