Heavy metal-induced oxidative stress and alteration in secretory proteins in yeast isolates.

In the recent years, yeasts have evolved as potent bioremediative candidates for the detoxification of xenobiotic compounds found in the natural environment. Candida sp. are well-studied apart from Saccharomyces sp. in heavy metal detoxification mechanisms. In the current study, Candida parapsilosis strain ODBG2, Candida sp. strain BANG3, and Candida viswanathii strain ODBG4 were isolated from industrial effluents and contaminated ground water, and were studied for their metal tolerance. Among these three isolates, the metal tolerance was found to be more towards Lead (Pb 2 mM), followed by Cadmium (Cd 1.5 mM) and Chromium [Cr(VI), 1 mM]. On further exploring the involvement of primary defensive enzymes in these isolates towards metal tolerance, the anti-oxidative enzyme superoxide dismutase was found to be prominently high (25% with respect to the control) during first 24 h of metal-isolate interaction. The Catalase enzyme assay was observed to have increased enzyme activity at 48 h. It also triggered the activity of peroxidases, which lead to the increase in reduced glutathione in the organism by 0.87-1.9-fold as a metal chelator and also as a second-line defensive molecule. The exoproteome profile showed the early involvement (exponential growth phase) of secreted proteins (low-molecular-weight) of about ~ 40-45 kDa under Cd and Pb stress (0.5 mM). The exoproteome profiling under heavy metal stress in Candida parapsilosis strain ODBG2 and Candida viswanathii strain ODBG4 is the first report.