Studies on peroxidase production and detection of Sporotrichum thermophile-like catalase-peroxidase gene in a Bacillus species isolated from Hogsback forest reserve, South Africa

Abstract

A B S T R A C TThis study sought to determine the process conditions for optimum peroxidase production by a Bacillus species (Bacillus sp. FALADE-1-KX640922) isolated from Hogsback forest reserve in South Africa and characterize the peroxidase gene in the bacteria. We optimized peroxidase production by manipulating the environmental and nutritional parameters under submerged fermentation. Subsequently, the gene encoding heme-peroxidase was determined through nested polymerase chain reaction and Sanger DNA sequencing. The studied bacteria had maximum peroxidase production at pH 8, 30 C and 150 rpm. The addition of guaiacol to lignin fermentation medium enhanced peroxidase production by over 100 % in the studied bacteria. However, the other lignin monomers (veratryl alcohol, vanillin, vanillic acid and ferulic acid) repressed the enzyme activity. Modification of the fermentation medium with ammonium sulphate gave the maximum peroxidase yield (8.87 U mL À1 ). Under the predetermined culture conditions, Bacillus sp. FALADE-1 expressed maximum specific peroxidase activity at 48 h (8.32 U mg À1 ). Interestingly, a search of the sequenced gene in PeroxiBase showed 100% similarity to Sporotrichum thermophile catalase-peroxidase gene (katG), as well, the deduced protein sequence clustered with bacterial catalase-peroxidases and had a molecular weight of about 11.45 kDa with 7.01 as the estimated isoelectric point. Subsequently, the nucleotide sequence was deposited in the National Center for Biotechnology Information (NCBI) repository with the accession number MF407314. In conclusion, Bacillus sp. FALADE-1 is a promising candidate for improved peroxidase production.

Response to Cold Adaption in Acinetobacter johnsonii XY27 from Spoiled Bigeye Tuna (Thunnus obesus): Membrane Protein Composition and Protein Biomarker Identification by Proteomics

“…Besides, catalase-peroxidase 1 was significantly upregulated in the evolution and transfer process of the horizontal gene, causing peroxidase activity expression in A. johnsonii XY27 under cold stress, which was corroborated by Falade, Mabinya, Okoh, and Nwodo (2019) . Microorganisms respond to low temperatures by differential expression of cold-induced proteins, which result in the negative expression of DNA .…”

“…39 Besides, catalase-peroxidase 1 was significantly upregulated in the evolution and transfer process of the horizontal gene, causing peroxidase activity expression in A. johnsonii XY27 under cold stress, which was corroborated by Falade, Mabinya, Okoh, and Nwodo (2019). 40 Microorganisms respond to low temperatures by differential expression of cold-induced proteins, which result in the negative expression of DNA. 41 In this study, A0A510X9K9, D0SFF5, A0A3Q8XCC7, A0A0U3I7Y6, A0A380U3B7, N9CZ07, and A0A654RM88 significantly downregulated under cold were shown to facilitate the DNA biological process of degrading machinery.…”

Biodegradation improvement of bioinspired crosslinked and noncrosslinked polyvinyl alcohol nanocomposites with cellulose nanocrystals extracted from rice straw through natural soil burial exposure

“…family were proven to be able to produce peroxidase enzyme. [ 47,48 ] In this study, PVOH degrading bacteria of Bacillus cereus CCM 2010 and Bacillus cereus ATCC 14579 that were identified as PVOH degraders in Section 4.6 had contributed to the biodegradation of PVOH.…”

Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin

“…Catalase-peroxidase ( KatG ) belongs to class I peroxidases of the PCAT superfamily. The corresponding gene ( KatG ) encodes a bifunctional enzyme with predominant catalase and peroxidase activity in an organism [49] .…”