Achromopeptidase, Crude, Lytic Enzyme

Achromopeptidase, originally isolated from the soil bacterium discovered by Masaki, et al., has a broad bacteriolytic spectrum, and its bacteriolytic activity is more potent and its bacteriolytic spectrum wider than those of albumen lysozyme. It can be also used for preparation of protoplasts from actinomycetes, etc.

Activity: 900 ~ 1500 units/mg
Diluent: Lactose as necessary
Optimum ion strength for enzyme action: 0.01 mol/L NaCl [0.01 mol/L Tris-HCl buffer (pH 8.0)]
Unit Definition
One unit of enzyme is defined as that which when present in 1 mL of substrate suspension of lyophilized Micrococcus lysodeikticus IFO 3333 in Tris-HCl buffer causes turbidity ( absorbance at 600 nm) to decrease at the rate of 0.001 per minute at pH 8.0 and 37 degrees C.
Source: Bacteria

Originally, the source of this product was indicated as "Achromobacter lyticus" based on the physiological and morphological properties of the bacteria. However, we confirmed that the 16SrDNA sequence was highly homologous to that of Lysobacter.
References

1. Hiroshi, O. et al.: Sci. Reports of Meiji Seika Kaisha, 21, 52 (1982)


2. Hiroshi, O. et al.: J. Antibiotics, 36, 184 (1983)


3. Keiji, N. et al.: Agr. Biol. Chem., 37, 2667 (1973)


4. Sueharu, H., et al.: Agric. Biol. Chem., 41, 2487 (1977)


5. Hiroshi, O. et al.: J. Antibiotics, 36, 1040 (1983)