Thermophilic iron containing type superoxide dismutase from Cohnella sp. A01

Shahi, Zahra Karimi Mazraeh; Takalloo, Zeinab; Mohamadzadeh, Jahangir; Sajedi, Reza H.; Haghbeen, Kamahldin; Aminzadeh, Saeed

doi:10.1016/j.ijbiomac.2021.07.150

Cited by 5 publications

(6 citation statements)

References 59 publications

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“…ΔG shows the catalytic reaction’s spontaneity. ΔH and ΔS shows the transition state’s (TS) efficiency ( Sharma et al, 2020 ; Shahi et al, 2021 ) In general, KRLr1 had lower values of E a ‡ , ΔG ‡ , and ΔG ‡ E–T compared to ΔH ‡ , ΔS ‡ , and ΔG ‡ E–S for the thermodynamic parameters of ES complex formation. These findings suggested that the KRLr1 reaction possesses an effective transition state and is probably quicker.…”

Section: Discussionmentioning

confidence: 99%

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Biochemical and molecular characterization of novel keratinolytic protease from Bacillus licheniformis (KRLr1)

et al. 2023

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The keratin-degrading bacterium Bacillus licheniformis secretes a keratinase with potential industrial interest. Here, the Keratinase gene was intracellularly expressed in Escherichia coli BL21(DE3) using pET-21b (+) vector. Phylogenetic tree analysis showed that KRLr1 is closely related to Bacillus licheniformis keratinase that belongs to the serine peptidase/subtilisin-like S8 family. Recombinant keratinase appeared on the SDS-PAGE gel with a band of about 38 kDa and was confirmed by western blotting. Expressed KRLr1 was purified by Ni-NTA affinity chromatography with a yield of 85.96% and then refolded. It was found that this enzyme has optimum activity at pH 6 and 37°C. PMSF inhibited the KRLr1 activity and Ca2+ and Mg2+ increased the KRLr1 activity. Using keratin 1% as the substrate, the thermodynamic values were determined as Km 14.54 mM, kcat 912.7 × 10−3 (S−1), and kcat/Km 62.77 (M−1 S−1). Feather digestion by recombinant enzyme using HPLC method, showed that the amino acids cysteine, phenylalanine, tyrosine and lysine had the highest amount compared to other amino acids obtained from digestion. Molecular dynamics (MD) simulation of HADDOCK docking results exhibited that KRLr1 enzyme was able to interact strongly with chicken feather keratine 4 (FK4) compared to chicken feather keratine 12 (FK12). These properties make keratinase KRLr1 a potential candidate for various biotechnological applications.

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Section: Discussionmentioning

confidence: 99%

“…A variety of keratin substrate concentrations (10–70 mM) and the activity optimum temperature were used to measure the keratinase activity. Assays were carried out in triplicate and with 0.6 mg/mL of the purified KRLr1 ( Shahi et al, 2021 ).…”

Section: Methodsmentioning

confidence: 99%

Biochemical and molecular characterization of novel keratinolytic protease from Bacillus licheniformis (KRLr1)

et al. 2023

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“…Superoxide dismutases (SODs) are well-known antioxidant enzymes that play critical roles in the cellular defenses of living organisms against harmful superoxide radicals during oxidative stress ( Pedone et al, 2020 ; Shahi et al, 2021 ). The most common iso-enzymes of SODs include copper-zinc SOD (Cu, ZnSOD), iron SOD (FeSOD), nickel SOD (NiSOD), and manganese SOD (MnSOD) ( Ranawat and Rawat, 2017 ; Shahi et al, 2021 ). Recently, several novel SOD genes from various prokaryotic and eukaryotic organisms have been identified and characterized ( Shahi et al, 2021 ).…”

Section: Oxidative Stress In Thermophilesmentioning

confidence: 99%

“…The most common iso-enzymes of SODs include copper-zinc SOD (Cu, ZnSOD), iron SOD (FeSOD), nickel SOD (NiSOD), and manganese SOD (MnSOD) ( Ranawat and Rawat, 2017 ; Shahi et al, 2021 ). Recently, several novel SOD genes from various prokaryotic and eukaryotic organisms have been identified and characterized ( Shahi et al, 2021 ). For example, the thermophile isolates Thermus thermophilus (HB27) isolated from thermal environment show excellent stability and activity under high temperatures, and also it is halotolerant ( Chen N. W. et al, 2021 ).…”

Section: Oxidative Stress In Thermophilesmentioning

confidence: 99%

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Adaptive Response of Thermophiles to Redox Stress and Their Role in the Process of dye Degradation From Textile Industry Wastewater

2022

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Release of dye-containing textile wastewater into the environment causes severe pollution with serious consequences on aquatic life. Bioremediation of dyes using thermophilic microorganisms has recently attracted attention over conventional treatment techniques. Thermophiles have the natural ability to survive under extreme environmental conditions, including high dye concentration, because they possess stress response adaptation and regulation mechanisms. Therefore, dye detoxification by thermophiles could offer enormous opportunities for bioremediation at elevated temperatures. In addition, the processes of degradation generate reactive oxygen species (ROS) and subject cells to oxidative stress. However, thermophiles exhibit better adaptation to resist the effects of oxidative stress. Some of the major adaptation mechanisms of thermophiles include macromolecule repair system; enzymes such as superoxide dismutase, catalase, and glutathione peroxidase; and non-enzymatic antioxidants like extracellular polymeric substance (EPSs), polyhydroxyalkanoates (PHAs), etc. In addition, different bacteria also possess enzymes that are directly involved in dye degradation such as azoreductase, laccase, and peroxidase. Therefore, through these processes, dyes are first degraded into smaller intermediate products finally releasing products that are non-toxic or of low toxicity. In this review, we discuss the sources of oxidative stress in thermophiles, the adaptive response of thermophiles to redox stress and their roles in dye removal, and the regulation and crosstalk between responses to oxidative stress.

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A novel highly thermostable and stress resistant ROS scavenging metalloprotein from Paenibacillus

Zhang,

Li,

Gong

et al. 2024

Archives of Biochemistry and Biophysics

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Thermophilic iron containing type superoxide dismutase from Cohnella sp. A01

Cited by 5 publications

References 59 publications

Biochemical and molecular characterization of novel keratinolytic protease from Bacillus licheniformis (KRLr1)

Biochemical and molecular characterization of novel keratinolytic protease from Bacillus licheniformis (KRLr1)

Adaptive Response of Thermophiles to Redox Stress and Their Role in the Process of dye Degradation From Textile Industry Wastewater

A novel highly thermostable and stress resistant ROS scavenging metalloprotein from Paenibacillus

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