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Catalase - Springer Nature

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Last Updated: 10 January 2023

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Lactate oxidase/catalase-displaying nanoparticles efficiently consume lactate in the tumor microenvironment to effectively suppress tumor growth

Increased glucose uptake and excess anaerobic glycolysis are often required for tumor cell proliferation, resulting in the production and concealment of a peculiar tumor microenvironment. To properly absorb lactate in the TME, lactate oxidase, and catalase, Aquifex aeolicus synthase protein nanoparticles were embedded onto Aeolicus lumazine synthase protein nanoparticles, forming either AaLS/LOX/CAT or AaLS/LOX/CAT. Both normoxic and hypoxic conditions were used by these complexes to consume lactate produced by CT26 murine colon carcinoma cells. Although mice death was caused by AaLS/LOX/CAT's local government, AaLAS/LOX/CAT's Aalist/LOX/CAT's treatment of the tumor site also reduced tumor formation with no dramatic side effects, no significant side effects were present. These results, taken collectively, showed that modular functionalization of protein nanoparticles with multiple metabolic enzymes may be able to produce new enzyme complex-based therapeutic tools that can control cancer metabolism.

Source link: https://doi.org/10.1186/s12951-022-01762-6


A thermostable bacterial catalase-peroxidase oxidizes phenolic compounds derived from lignins

The production of aromatics from lignin's biological valorization necessitates the development of ligninolytic peroxidases and laccases produced by fungi and bacteria. Hence, the finding of strong ligninolytic enzymes with high stability is a promising route for lignin biorefining. Our goal is to produce strong and thermostable ligninolytic enzymes using the thermophilic bacterium Thermobacillus xylanilyticus's enzymatic capability to produce durable and thermostable ligninolytic enzymes. The catalase-peroxide from T. xylanilyticus is thermostable, and the manganese peroxidase activity is shown in our analysis. The enzyme's ability was shown by electrochemical characterization using intermittent pulse amperometry, which demonstrated the enzyme's ability to oxidize small aromatic compounds derived from lignins. u2022 Production and analysis of a new thermostable bacterial catalase peroxide is expected to produce several phenolic monomers isolated from lignins. u2022 Intermittent pulse amperometry is promising to screen ligninolytic enzymes.

Source link: https://doi.org/10.1007/s00253-022-12263-9


Genomic analysis of Paenibacillus sp. MDMC362 from the Merzouga desert leads to the identification of a potentially thermostable catalase

Microorganisms in hot deserts face heat and other environmental conditions, such as desiccation, UV radiation, or poor nutrient availability. The genome of Paenibacillus sp. is included in this study. A catalase extracted from genomic annotation files by molecular dynamics was sequenced to reveal its genetic basis, its survival strategy's genetic basis, and to determine the thermostability of a catalase isolated from genomic annotation files using molecular dynamics. Paenibacillus sp. We also investigated the genetic constituents of the UvrABC system and additional DNA repair procedures, which help prevent UV radiation damage. These results indicate a potential thermostability of the enzyme. The protein exhibited stability and saved its compactness at temperatures up to 373. 15 K. Temperature preservation in Paenibacillus sp. Since the studied protein is a primary protein, thermostability could be preserved in Paenibacillus sp. Both MDMC362 closely related strains have a slight advantage in protein stability; however, bacteria from harsh environments may have a slight advantage over protein stability;.

Source link: https://doi.org/10.1007/s10482-022-01793-x


Decolorization and detoxication of plant-based proteins using hydrogen peroxide and catalase

The existing meat supply chain and its predicted future demand is expanding, prompting the desire to produce plant-based meat analogs. Despite continuing technological advancements, one of plant-based meat analogs' unsolved challenges is to safely and effectively decolor plant proteins that first appear yellow,u2013brown or strong brown color. This research was designed to produce an effective and safe decoloring system for soy-based protein products using food-grade hydrogen peroxide and catalase. Using catalase, the first, soy-based protein isolate and textured vegetable protein were treated with hydrogen peroxide, and then the remaining hydrogen peroxide was degraded.

Source link: https://doi.org/10.1038/s41598-022-26883-8

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions