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Properties of adenosine deaminase from Candida albicans
Author(s) -
Challa Anjana,
Johnson Salynn,
Robertson Kesha,
Gunasekaran M.
Publication year - 1999
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/(sici)1521-4028(199905)39:2<97::aid-jobm97>3.0.co;2-n
Subject(s) - adenosine deaminase , adenosine , purine , mycelium , candida albicans , yeast , enzyme , purine nucleoside phosphorylase , enzyme assay , biochemistry , yeast extract , microbiology and biotechnology , chemistry , adenosine deaminase deficiency , biology , fermentation , botany
Adenosine deaminase (ADA; adenosine aminohydrolase, E.C. 3.5.4.4), a purine catabolic enzyme, was studied in Candida albicans , an opportunistic yeast that causes diseases ranging from superficial infections to the deep systemic disease, candidiasis, in immunosuppressed humans. The fungus was grown as a yeast form in L ee 's synthetic medium, pH 4.5, at room temperature for various growth periods. Adenosine deaminase (ADA) activity was determined from the cell free extract by measuring the change in absorbance 265 nm resulting from the deamination of adenosine. In yeast form, maximum growth and ADA activity were found at 72 and 24 hours, respectively, whereas in the mycelial form both the growth and ADA activity were maximum after 48 hours. Among the three media tested, tryptic soy broth supported maximum growth and enzyme production, compared to L ee synthetic medium or S abouraud dextrose broth. The enzyme was active over the pH range 4–8 and the optimum temperature for ADA activity was found to be 37 °C.