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Evaluation the enzymatic activites of Candida albicans and Candida parapasilosis isolated from bovine mastitis in Basrah Province Iraq by API ZYM test

The aim of the study is to evaluate the enzymatic activities of Candida albicans and Candida parapasilosis isolated from bovine mastitis. Two hundred and fifty milk samples were isolated from cows with mastitis in Basrah province were collected and examined using rapid diagnostic tests. Candida Spp...

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Bibliographic Details
Main Authors: AL-abedi, Hawrra Faysal Hasab Allh, AL-Attraqchi, Azhar A. F., Khudaier, Bassam Yasein
Format: Conference Proceeding
Language:English
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Summary:The aim of the study is to evaluate the enzymatic activities of Candida albicans and Candida parapasilosis isolated from bovine mastitis. Two hundred and fifty milk samples were isolated from cows with mastitis in Basrah province were collected and examined using rapid diagnostic tests. Candida Spp were identified as proportion of 116/250 (46.4%). Based on conventional method and ID - Yst card system Vitek 2, C. albicans was the predominant 60/116 (51.7%), followed by C.parapasilosis as 15/116 (12.9%). Some randomly chosen isolates of C. albicans and C. parapasilosis were used for detection of their enzymatic activities by API ZYM test. In case of C. albicans (n=30) the isolates produced n-acetylo-B-glucosyloaminidase strongly when the percentage was 30/30 (100%), esterase and valine arylamidase (C4) 29/30 (96.6%), leucine arylamidase 28/30 (93.3%), esterase lipase (C8) and naphthol-AS-BI- phosphohydrolase 25/30 (83.3%), α-glucosidase 23(76.6%), β-glucosidase 22 (73.3%), α-mannosidase 4 (13.3%), with a lowest activity of cystine arylamidase 1(3.3%). Regarding C. parapasilosis (n=10) the isolates showed a highest activity of leucine arylamidase, acid phosphatase, naphthol-AS-BI-phosphohydrolase and α-glucosidase which was 10/10 (100%) for each, followed by esterase lipase (C8) 9/10 (90%), valine arylamidase and alkaline phosphatase 8/10 (80%) for both and esterase (C4) 7/10 (70%).
ISSN:0094-243X
1551-7616
DOI:10.1063/5.0027653