Disease relevance of BCE_3037

• Unusual chromatographic behaviour and one-step purification of a novel membrane proteinase from Bacillus cereus [1].
• Purified CCMP is a member of the metalloproteinase family with a pH optimum in the neutral range and a temperature optimum of 40 degrees C, whose properties differ from the serine-type membrane proteinase of Bacillus subtilis described by Shimizu et al [1].

High impact information on BCE_3037

• Exudate activity was freely dialyzable and was not measurably affected by a broad-spectrum protease (proteinase K), by autoclaving at 121 degrees C, or by freezing and thawing [2].
• Therefore it was assumed that the difference in thermostability between B. cereus neutral proteinase and thermolysin is not caused by different metal binding properties, or differences in the active site, but by changes within the rest of the molecule [3].
• The complete amino-acid sequence of a neutral proteinase, produced by Bacillus cereus, was determined by protein sequencing [3].

Analytical, diagnostic and therapeutic context of BCE_3037

• Antimicrobial activity was lost after treatment with proteinase K [4].
• Entomocin 9 retained more than 72% of activity after incubation for 20 min at 121 degrees C. Activity was lost after proteinase K treatment, it was stable in a pH range between 3 and 9, and resistant to lyophilization [5].

References