Purification and Characterization of Cell Wall-associatedN-Acetylmuramyl-L-alanine Amidase from AlkaliphilicBacillus lentusC-125 | Zendy

Rikizo Aono | Zendy; Sanada Takafumi | Zendy; Horikoshi Koki | Zendy

Open Access

Purification and Characterization of Cell Wall-associatedN-Acetylmuramyl-L-alanine Amidase from AlkaliphilicBacillus lentusC-125

Author(s) -

Rikizo Aono,

Sanada Takafumi,

Horikoshi Koki

Publication year - 1996

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.60.1140

Subject(s) - amidase , peptidoglycan , enzyme , molecular mass , chemistry , cell wall , biochemistry , alanine , chromatography , amino acid

Cells of the facultative alkaliphile Bacillus sp. C-125 grown at neutral pH autolyze rapidly in alkaline buffers of pH 9-10. Alkaline autolytic activity has been found mainly in the cell wall fraction. A peptidoglycanlytic enzyme was extracted from the cell wall fraction suspended in 4M LiCl. The enzyme was identified as N-acetylmuramyl-L-alanine amidase, with a molecular mass of 58kDa. At low salinity, the enzyme formed an aggregate of high molecular mass. The peptidoglycan lytic reaction of this enzyme happened at pH 9.0-10.5 at 37°C. Optimum pH for the reaction was 9.7-10.0. The enzyme was most active at 60°C when assayed at pH 9.0.

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