IDEAS home Printed from https://ideas.repec.org/a/gam/jsusta/v15y2023i10p8287-d1150851.html
   My bibliography  Save this article

Differential Expression of Antioxidant Enzymes in Chlorine-Resistant Acinetobacter and Serratia spp. Isolated from Water Distribution Sites in Mumbai: A Study on Mechanisms of Chlorine Resistance for Sustainable Water Treatment Strategies

Author

Listed:
  • Santosh Jathar

    (Amity Institute of Biotechnology, Amity University Maharashtra, Mumbai-Pune Expressway, Bhatan, Panvel, Mumbai 410206, Maharashtra, India
    Municipal Laboratory, Municipal Corporation of Greater Mumbai, Dadar, Mumbai 400028, Maharashtra, India)

  • Sanabil Dakhni

    (Amity Institute of Biotechnology, Amity University Maharashtra, Mumbai-Pune Expressway, Bhatan, Panvel, Mumbai 410206, Maharashtra, India)

  • Disha Shinde

    (Amity Institute of Biotechnology, Amity University Maharashtra, Mumbai-Pune Expressway, Bhatan, Panvel, Mumbai 410206, Maharashtra, India)

  • Abigail Fernandes

    (Amity Institute of Biotechnology, Amity University Maharashtra, Mumbai-Pune Expressway, Bhatan, Panvel, Mumbai 410206, Maharashtra, India)

  • Pamela Jha

    (Sunandan Divatia School of Science, SVKM’S NMIMS University, Mumbai 400056, Maharashtra, India)

  • Neetin Desai

    (Sunandan Divatia School of Science, SVKM’S NMIMS University, Mumbai 400056, Maharashtra, India)

  • Tareeka Sonawane

    (Amity Institute of Biotechnology, Amity University Maharashtra, Mumbai-Pune Expressway, Bhatan, Panvel, Mumbai 410206, Maharashtra, India)

  • Renitta Jobby

    (Amity Institute of Biotechnology, Amity University Maharashtra, Mumbai-Pune Expressway, Bhatan, Panvel, Mumbai 410206, Maharashtra, India
    Amity Centre of Excellence in Astrobiology, Amity University Maharashtra, Mumbai-Pune Expressway, Bhatan, Panvel, Mumbai 410206, Maharashtra, India)

Abstract

Chlorination is a widely used process for disinfecting drinking water, but the emergence of chlorine-resistant bacteria has become a significant concern. While previous research has focused on identifying chlorine-resistant organisms, there has been limited investigation into the mechanisms behind chlorine resistance. Some bacterial isolates that display resistance to chlorine treatment may protect themselves using various mechanisms, including biofilm production, antibiotic resistance, horizontal transfer of antibiotic resistance genes, or producing antioxidant enzymes. Given that chlorination employs hypochlorous acid (HOCl), which is an extremely potent oxidizing agent, the most critical mechanism to investigate is antioxidant enzymes. This study investigated the antioxidant profile of eight chlorine-resistant isolates (three of the Serratia sp. and five of the Acinetobacter) after chlorine exposure. The profiles, both between and within species, were noticeably different. Among the isolates, Acinetobacter junii NA 3-2 showed a significant increase in the specific activity of superoxide dismutase, catalase, and ascorbate peroxidase after exposure to 20 ppm chlorine. In the guaiacol peroxidase (GPX) assay, only isolates belonging to Serratia marcescens showed GPX activity, and Serratia marcescens 3929-1 showed significant increase after exposure to 20 ppm of chlorine. None of the isolates belonging to Acinetobacter spp. showed GPX activity. Additionally, almost all control samples exhibited some enzyme activity, which may explain their survival against chlorine treatment in reservoirs. Principal component analysis revealed no strain-dependent similarities, while the balance of scavenging enzymes changed, as demonstrated in the heat map. Thus, this study suggests that antioxidant enzymes may be one mechanism of protection for some bacterial species against oxidative stress from chlorination, resulting in chlorine resistance. Understanding the mechanism of chlorine resistance is critical to identifying potential solutions. This study highlights the need to consider more modern approaches to disinfecting drinking water.

Suggested Citation

  • Santosh Jathar & Sanabil Dakhni & Disha Shinde & Abigail Fernandes & Pamela Jha & Neetin Desai & Tareeka Sonawane & Renitta Jobby, 2023. "Differential Expression of Antioxidant Enzymes in Chlorine-Resistant Acinetobacter and Serratia spp. Isolated from Water Distribution Sites in Mumbai: A Study on Mechanisms of Chlorine Resistance for ," Sustainability, MDPI, vol. 15(10), pages 1-11, May.
  • Handle: RePEc:gam:jsusta:v:15:y:2023:i:10:p:8287-:d:1150851
    as

    Download full text from publisher

    File URL: https://www.mdpi.com/2071-1050/15/10/8287/pdf
    Download Restriction: no

    File URL: https://www.mdpi.com/2071-1050/15/10/8287/
    Download Restriction: no
    ---><---

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:gam:jsusta:v:15:y:2023:i:10:p:8287-:d:1150851. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: MDPI Indexing Manager (email available below). General contact details of provider: https://www.mdpi.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.