%0 Journal Article %A Li, Zusheng S. %A Beveridge, Terry J. %A Betts, Joanna %A Clarke, Anthony J. %T Partial characterization of a major autolysin from Mycobacterium phlei %D 1999 %J Microbiology, %V 145 %N 1 %P 169-176 %@ 1465-2080 %R https://doi.org/10.1099/13500872-145-1-169 %K autolysin %K β-glycosidase %K Mycobacterium phlei %I Microbiology Society, %X Summary: Autolytic enzyme profiles of fast- and slow-growing mycobacteria were examined using SDS-PAGE zymography with incorportated mycobacterial peptidoglycan sacculi as substrate. Each species tested (Mycobacterium phlei, Mycobacterium smegmatis, Mycobacterium aurum, Mycobacterium fortuitum and Mycobacterium kansasii) appeared to produce a different set of enzymes on the basis of differing number and molecular masses. A major autolysin from M. phlei was purified to apparent homogeneity by DEAE-cellulose chromatography, preparative gel electrophoresis and Mono Q FPLC. This enzyme had an estimated molecular mass of 38 kDa, an isoelectric point of 5·5 and a pH optimum of pH 7·5. Digestion of purified peptidoglycan by the enzyme resulted in the appearance of reducing sugars, suggesting that the 38 kDa autolysin is a β-glycosidase. Partial internal amino acid sequence of the autolysin was determined and should facilitate identification, cloning and overexpression of the encoding gene. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/13500872-145-1-169