Identification and characterization of lignin depolymerization enzymes in Bacillus subtilis strain S11Y isolated from a tropical environment in Malaysia

Fatimah Azizah Riyadi, Nadia Farhana Azman, Fazrena Nadia Md Akhir, Nor’Azizi Othman, Hirofumi Hara

Research output: Contribution to journalArticlepeer-review

Abstract

Biological pretreatment using microbial enzymes appears to be the most promising pre-treatment technology for the breakdown of recalcitrant lignin structure. This research focuses on the identification and characterization of lignin-depolymerizing enzymes in Bacillus subtilis strain S11Y, previously isolated from palm oil wastes in Malaysia. The draft genome sequences of this highly lignin-depolymerizing strain revealed that the genome lacked any of the well-known dye-decolorizing per-oxidase or catalase-peroxidase that are commonly reported to be involved in lignin depolymerization by bacteria, indicating that strain S11Y has distinct sets of potential lignin depolymerization genes. The oxidative stress-related enzymes Cu/Zn type-superoxide dismutase (Sod2) and a heme-containing monofunctional catalase (Kat2) were identified in the genome sequences that are of interest. Their lignin-depolymerizing ability were evaluated by treating Alkali lignin (AL) with each enzyme and their degradation ability were evaluated using gel-permeation chromatography (GPC), ultra-high-pressure liquid chromatography–mass spec-trometry (UHPLC/MS), and gas chromatography– mass spectrometry (GC/MS), which successfully proved lignin depolymerizing ability. Successful evaluation of lignin depolymerizing enzymes can be applicable for lignin pre-treatment process in green energy production and generation of valuable chemicals in bio-refinery.

Original languageEnglish
Pages (from-to)278-286
Number of pages9
JournalJournal of General and Applied Microbiology
Volume69
Issue number5
DOIs
Publication statusPublished - 2023

Keywords

  • Bacillus subtilis strain S11Y
  • Cu/Zn type-superoxide dismutase
  • lignin depolymerization
  • monofunctional catalase

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