Skip to main content
Log in

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

  • Original Paper
  • Published:
Archives of Microbiology Aims and scope Submit manuscript

Abstract

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5

Similar content being viewed by others

Abbreviations

Pb:

Lead

Cd:

Cadmium

mM:

Millimolar

SOD:

Superoxide dismutase

CAT:

Catalase

GSH:

Glutathione

YPDA:

Yeast peptone dextrose agar

HM:

Heavy metal (s)

MIC:

Minimal inhibitory concentration

ITS:

Internal transcribe sequences

PCR:

Polymerase chain reaction

TBE:

Tris–borate EDTA

BLAST:

Basic local alignment search tool

MEGA:

Molecular evolutionary genetics analysis

PMSF:

Phenylmethylsulfonyl fluoride

H2O2 :

Hydrogen peroxide

DTNB:

5, 5′-Dithiobis(2-nitrobenzoic acid)

SDS-PAGE:

Sodium dodecyl sulphate polyacrylamide gel electrophoresis

CHAPS:

3-Cholamidopropyl dimethylammonio 1-propanesulfonate

DTT:

Dithiothreitol

References

Download references

Acknowledgements

Authors are thankful for Department of Studies in Biotechnology, University of Mysore, Mysuru for facilities provided. The authors also extend their thanks to facilities available at Laboratory of Plant Healthcare and Diagnostics, PG Department of Biotechnology and Microbiology, Karnatak University, Dharwad.

Funding

The authors received no financial support for this research work.

Author information

Authors and Affiliations

Authors

Contributions

Supervision of research work: NG and SJ. Bench work: GB. Data validation: GB, NG, KH, and SJ. Figures and charts: GB, NG, and SJ. Contributed reagents/chemicals: NG. Wrote the original manuscript: GB, NG, and SJ. All the authors read and approved the manuscript.

Corresponding authors

Correspondence to Sudisha Jogaiah or Nagaraja Geetha.

Ethics declarations

Conflict of interest

The authors do not have any competing interest in the submitted work.

Additional information

Communicated by Erko Stackebrandt.

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Supplementary Information

Below is the link to the electronic supplementary material.

Supplementary file1 (DOCX 487 KB)

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Bhavya, G., Hiremath, K.Y., Jogaiah, S. et al. Heavy metal-induced oxidative stress and alteration in secretory proteins in yeast isolates. Arch Microbiol 204, 172 (2022). https://doi.org/10.1007/s00203-022-02756-6

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • DOI: https://doi.org/10.1007/s00203-022-02756-6

Keywords

Navigation