Fluorimetric assay of mycobacterial group-specific hydrolase enzymes.
Fluorigenic substrates prepared from 4-methylumbelliferone provide a simple, convenient method for detecting and assaying group-specific hydrolase activity in small quantities of whole mycobacteria. Physico-chemical properties of the enzymes such as pH dependence and heat stability may also be studied. A technique is described for studying glycosidase, hexosaminidase, acid phosphatase, and acyl esterase activity in seven mycobacterial species. Such techniques will be a useful aid to the taxonomy, identification, and quantification of mycobacteria, especially slowly growing strains in which biochemical properties are very difficult to detect by other techniques.
D000135:Acid Phosphatase / Q000378:metabolism; D004950:Esterases / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism; D006596:Hexosaminidases / Q000378:metabolism; D006867:Hydrolases / Q000378:metabolism*; D009161:Mycobacterium / Q000201:enzymology*; D013045:Species Specificity; D013050:Spectrometry, Fluorescence
D006867:Hydrolases; D004950:Esterases; D000135:Acid Phosphatase; D006026:Glycoside Hydrolases; D006596:Hexosaminidases