Properties of adenosine deaminase from Candida albicans

Citation
A. Challa et al., Properties of adenosine deaminase from Candida albicans, J BASIC MIC, 39(2), 1999, pp. 97-101
Citations number
11
Categorie Soggetti
Microbiology
Journal title
JOURNAL OF BASIC MICROBIOLOGY
ISSN journal
0233111X → ACNP
Volume
39
Issue
2
Year of publication
1999
Pages
97 - 101
Database
ISI
SICI code
0233-111X(1999)39:2<97:POADFC>2.0.ZU;2-0
Abstract
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 system ic disease, candidiasis, in immunosuppressed humans. The fungus was grown a s a yeast form in LEE's synthetic medium, pH 4.5, at room temperature for v arious growth periods. Adenosine deaminase (ADA) activity was determined fr om the cell free extract by measuring the change in absorbance 265 nm resul ting from the deamination of adenosine. In yeast form, maximum growth and A DA activity were found at 72 and 24 hours, respectively, whereas in the myc elial form both the growth and ADA activity were maximum after 48 hours. Am ong the three media tested, tryptic soy broth supported maximum growth and enzyme production, compared to LEE synthetic medium or SABOURAUD dextrose b roth. The enzyme was active over the pH range 4-8 and the optimum temperatu re for ADA activity was found to be 37 degrees C.