Purification and characterization of an antibiotic substance produced from Rhizopus oligosporus IFO 8631.
We obtained a purified antibiotic protein from the submerged cultivation broth of Rhizopus oligosporus IFO 8631 by using CM-Cellulofine chromatography and HPLC. The antibiotic did not show a broad spectrum of activity, but it was very active against some of the Bacillus species, especially against Bacillus subtillis (B. natto) at a very low concentration (less than 1 ppm). It also showed activity against other gram-positive bacteria, including Staphylococcus aureus and Streptococcus cremoris. The purified antibiotic was a simple protein of about 5,500 in molecular weight, the amino acid component being characteristically high in cystine content. This high cystine content contributed to the stability of the antibiotic over a wide pH range and against strong heating (50% of the activity remained after boiling for 1 hr).
Kobayasi
S
S
National Research Institute of Brewing, Tokyo, Japan.
Okazaki
N
N
Koseki
T
T
D000596:Amino Acids / Q000032:analysis; D000900:Anti-Bacterial Agents / Q000096:biosynthesis / Q000302:isolation & purification* / Q000494:pharmacology; D001412:Bacillus subtilis / Q000187:drug effects; D002851:Chromatography, High Pressure Liquid; D006094:Gram-Positive Bacteria / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D012233:Rhizopus / Q000378:metabolism*; D013696:Temperature
D000596:Amino Acids; D000900:Anti-Bacterial Agents