Purification and Properties of Autolytic Endo- -N-acetylglucosaminidase and the N-Acetylmuramyl-L-alanine Amidase from Bacillus subtilis Strain 168

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Abstract
.beta.-N-acetylglucosaminidase was purified from the walls of B. subtilis 168 and compared with the other known autolysin, N-acetylmuramyl-L-alanine amidase (amidase). The .beta.-N-acetylglucosaminidase was a dimer in LiCl buffers with a subunit MW of 90,000 and a pH optimum of .apprx. 5.0. It was very sensitive to proteolytic enzymes and was critically activated by 0.1-0.2 M LiCl. It was insoluble in concentrations of LiCl lower than 0.05-0.1 M. It was less strongly bound to walls than was the amidase, which was a monomer of MW 30,000-40,000 in LiCl buffers. The .beta.-N-acetylglucosaminidase is an endoenzyme and showed no exo-activity. Lysozyme-like enzyme (muramidase) activity was undetectable in the wall extracts examined.