Bienzymatic Supramolecular Complex of Catalase Modified with Cyclodextrin‐Branched Carboxymethylcellulose and Superoxide Dismutase: Stability and Anti‐Inflammatory Properties

Valdivia, Aymara; Pérez, Y.; Cao, Roberto; Baños, Maysa; García, Ariel; Villalonga, Reynaldo

doi:10.1002/mabi.200600166

Cited by 15 publications

(10 citation statements)

References 17 publications

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“…An original supramolecular-based strategy was used to prepare a bienzymatic conjugate of catalase and SOD, by assembling adamantane-modified SOD with catalase previously cross-linked with CD-branched CMC. 102 The anti-inflamma- Low molecular weight dextrans, previously functionalized with a carboxylate or amino group at its reducing end residue, were chemically attached to catalase via a carbodiimide coupling reaction. 84,121 Significantly, the catalytic activity of catalase increased after modification with the monoaminated dextran, while the conjugate with the monocarboxylated polysaccharide retained 77% of the original activity.…”

Section: Neoglycoenzymes For Biomedical Applicationmentioning

confidence: 99%

“…Enzyme amino groups can be acylated with carbohydrate-containing carboxylic acid groups giving amide derivatives by using a water-soluble carbodiimide as coupling agent via the formation of an intermediary O -acylisourea active ester derivative (Figure ). − Enzyme–carbohydrate conjugates can be prepared by one-pot synthetic procedures in slightly acid aqueous solutions (pH 4.8–6.0), through coupling reactions that usually involve N -ethyl- N ′-(3-dimethylaminopropyl) carbodiimide (EDC) as coupling agent and long reaction times. − ,− ,− Two-step procedures have been also reported to acylate enzyme amino groups with sugars containing carboxylic acid groups. In such strategies, the carboxylic groups in saccharides are first activated with EDC in acidic or neutral solutions, and further reacted with the amino groups on the enzyme surface. − , …”

Section: Strategies For Preparing Artificial Glycoenzymesmentioning

confidence: 99%

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Neoglycoenzymes

et al. 2014

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Section: Neoglycoenzymes For Biomedical Applicationmentioning

confidence: 99%

Section: Strategies For Preparing Artificial Glycoenzymesmentioning

confidence: 99%

Neoglycoenzymes

et al. 2014

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“…In another paper, a catalase was chemically glycosilated with cyclodextrin-branched carboxymethylcellulose and them associated with superoxide dismutase modified with 1-adamantane carboxylic acid [265]. Following this strategy, superooxide dismutase was remarkably resistant to inactivation by H 2 O 2 and its anti-inflammatory activity was 4.5-fold increased after supramolecular association with the modified catalase form.…”

Section: Chemical Modificationmentioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

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Hydrogen peroxide is a substrate or side-product in many enzyme-catalyzed reactions. For example, it is a side-product of oxidases, resulting from the re-oxidation of FAD with molecular oxygen, and it is a substrate for peroxidases and other enzymes. However, hydrogen peroxide is able to chemically modify the peptide core of the enzymes it interacts with, and also to produce the oxidation of some cofactors and prostetic groups (e.g., the hemo group). Thus, the development of strategies that may permit to increase the stability of enzymes in the presence of this deleterious reagent is an interesting target. This enhancement in enzyme stability has been attempted following almost all available strategies: site-directed mutagenesis (eliminating the most reactive moieties), medium engineering (using stabilizers), immobilization and chemical modification (trying to generate hydrophobic environments surrounding the enzyme, to confer higher rigidity to the protein or to generate oxidation-resistant groups), or the use of systems capable of decomposing hydrogen peroxide under very mild conditions. If hydrogen peroxide is just a side-product, its immediate removal has been reported to be the best solution. In some cases, when hydrogen peroxide is the substrate and its decomposition is not a sensible solution, researchers coupled one enzyme generating hydrogen peroxide "in situ" to the target enzyme resulting in a continuous supply of this reagent at low concentrations thus preventing enzyme inactivation.This review will focus on the general role of hydrogen peroxide in biocatalysis, the main mechanisms of enzyme inactivation produced by this reactive and the different strategies used to prevent enzyme inactivation caused by this "dangerous liaison". Outlook

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“…The most important discovery is that the pretreatment of DNLE significantly increased the activities of SOD and CAT in H 2 O 2 ‐damaged cells, which meant the eliminating of intracellular H 2 O 2 could be accelerated by DNLE. There were already evidence has pointed out that combination of SOD and CAT was more effective than the action of either single enzyme in cell protection against oxidative stress (Luangwattananun et al., 2016; Valdivia et al., 2007). Thus, the cellular oxidative damage caused by H 2 O 2 could be greatly attenuated by the increasing of SOD and CAT activities.…”

Section: Discussionmentioning

confidence: 99%

Dendrobiumliquor eliminates free radicals and suppresses cellular proteins expression disorder to protect cells from oxidant damage

et al. 2020

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Dendrobium liquor obtained by soaking Dendrobium in Chinese liquor is considered as a health drink in China. Here, we found the pretreatment of extract of Dendrobium nobile Lindl. liquor (DNLE) attenuated the oxidative damage to cells caused by H 2 O 2 , while the abilities of DNLE of eliminating extracellular free radicals and promoting the activities of intracellular antioxidant enzymes were observed. Quantitative proteomics identified 375 differentially expressed proteins caused by H 2 O 2 treatment in 293T cells. However, only 12 differentially expressed proteins were found in DNLEpretreated cells which under the same oxidative damage. This suggested that the pretreatment of DNLE could suppress the disorder of protein expressions caused by oxidative stress which could induce cell death. Besides, DNLE was helpful for avoiding the unfolded protein response (UPR) and cell cycle disorder caused by oxidative stress. Taken together, these results demonstrated that Dendrobium liquor could be a healthy herbal drink with antioxidant function. Practical applications Dendrobium is used as an edible herb and a tonic food in traditional Chinese medicine. Dendrobium liquor obtained by soaking Dendrobium with Chinese liquor is also regarded as a nourishing health drink. However, there is rare research data on biological activity of Dendrobium liquor. Our current results demonstrated that the extract of Dendrobium nobile Lindl. liquor (DNLE) possessed the ability of eliminating free radicals in/out the human cells. More importantly, DNLE could help cells to resist the interference on cell life activities caused by oxidative stress. Since many evidences suggested that oxidative stress is linked to human disease and aging, and chemical antioxidant has some side effects on health, Dendrobium liquor can serve as a natural health drink with antioxidant function. Furthermore, the active ingredients in DNLE also possess the potential to be developed as natural antioxidant additive in food and cosmetics.

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Bienzymatic Supramolecular Complex of Catalase Modified with Cyclodextrin‐Branched Carboxymethylcellulose and Superoxide Dismutase: Stability and Anti‐Inflammatory Properties

Cited by 15 publications

References 17 publications

Neoglycoenzymes

Neoglycoenzymes

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Dendrobiumliquor eliminates free radicals and suppresses cellular proteins expression disorder to protect cells from oxidant damage

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