Multifunctional hydrophobin-like protein (HFB-NJ1): A versatile solution for wastewater treatment

  • Harshitha Kamath Miyar
  • , Neetha Nirupam Jathanna
  • , Raja Selvaraj
  • , Ramesh Vinayagam
  • , A. Pugazhendhi
  • , Louella Concepta Goveas*
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

As wastewater contains a variety of contaminating bacteria and oily residues, there is an urgent need for environmentally safe bactericidal agents and surfactants which can be applied for wastewater treatment. The present study emphasizes on the potential of hydrophobin-like protein (HFB-NJ1) extracted from sporulating mycelia of Aspergillus sp. NJ1 for wastewater treatment. The purified HFB-NJ1, depicted the presence of one single protein band of molecular size approximately 11–12 kDa on silver-stained SDS-PAGE gel. HFB-NJ1 also presented properties such as surface modification of glass and stable emulsification of sunflower oil. HFB-NJ1 depicted exceptional antibacterial activity against bacterial pathogens such as Bacillus subtilis and Pseudomonas aeruginosa at low MIC of 0.5 μg/mL and 0.75 μg/mL respectively. Additionally, HFB-NJ1 depicted enhanced emulsification of various vegetable and petroleum-based oils (E24 > 80%). HFB-NJ1 effectively reduced gold ions, producing nanospheres with a size of 15.33 nm – a recognized antimicrobial agent. This study underscores the multifunctional attributes of HFB-NJ1, highlighting its efficacy in removing pathogenic bacteria, emulsifying organic compounds from wastewater, and demonstrating a reduction ability for nanoparticle synthesis.

Original languageEnglish
Article number119139
JournalEnvironmental Research
Volume255
DOIs
Publication statusPublished - 15-08-2024

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • General Environmental Science

Fingerprint

Dive into the research topics of 'Multifunctional hydrophobin-like protein (HFB-NJ1): A versatile solution for wastewater treatment'. Together they form a unique fingerprint.

Cite this