Expression of transaminase enzymes and effect of potassium iodide on its production in mycelial form of Sporothrix schenckii

Abstract

Sporotrichosis is chronic, pyogranulomatous fungal infection of cutaneous or subcutaneous. It is caused by the dimorphic fungus (S. schenckii).This study describes the in-vitro effect of potassium iodide (KI) on the transaminases enzymes, aspartate aminotransferase (AST) and alanine aminotransferase (ALT) produced by the filamentous form of .A master culture of was prepared in YNB (Yeast nitrogen base) medium and was incubated at 25ºC (mould). KI was added into the YNB medium in increasing concentrations. One mL suspension of master culture was inoculated into each bottle and incubated at 25ºC for different time period, 4 day (early-log period), 9 day (mid-log period) and 14 day (peak of growth) respectively. After centrifuging, a 5% homogenate was prepared that was used for transaminases enzyme assay. The mean aspartate aminotransferase level of control specimen was 12.4 ± 3.30, 22.4 ± 3.69 and 53.6 ± 8.46 IU on day 4, 9 and 14 respectively. The mean aspartate aminotransferase level of test specimen was ranged from 3.5 ± 0.80 (KI 6.4 gram %) to 12.4 ± 4.66 IU (KI 0.1 gram %), 2.6 ± 0.21 (KI 6.4 gram %) to 29.5 ± 7.31 IU (KI 0.05 gram %) and 2.5 ± 0.23 (KI 6.4 gram %) to 42.3 ±3.70 IU (KI 0.2 gram %) on day 4, 9 and 14 respectively. The mean alanine aminotransferase level of control specimen was 17.5 ± 5.93, 24.6 ± 3.59 and 32.6 ± 7.54 IU on day 4, 9 and 14 respectively. The mean alanine aminotransferase level of test specimen was ranged from 2.2 ± 0.00 (KI 6.4 gram %) to 15.4 ± 2.36 IU (KI 0.1 gram %), 2.7 ± 0.81 (KI 6.4 gram %) to 29.5 ± 2.75 IU (KI 1.6 gram %) and 3.5 ± 1.37 (KI 6.4 gram %) to 29.6 ± 2.82 IU (KI 0.2 gram %) on day 4, 9 and 14 respectively.At the entire test concentrations mean value was lower as compared to control. The low activity of the transaminases enzymes indicates that KI has inhibitory effect on the growth of (mould) and has led to decrease in the activity of these enzymes.