Influence of salts and metal nanoparticles on the activity and thermal stability of a recombinant chitinase from Stenotrophomonas maltophilia N4

Sosnowska, Malwina; Jankiewicz, Urszula; Kutwin, Marta; Chwalibog, A.; Gałązka, Agnieszka

doi:10.1016/j.enzmictec.2018.05.003

Cited by 7 publications

(4 citation statements)

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“…The optimum temperature for chitinolytic activity of the analysed enzyme was 37 °C. It is a lower value compared to literature data indicating an optimal temperature of 40 °C (Suma and Podile 2013), 45 °C (Jabeen et al 2018) or 50 °C (Sosnowska et al 2018) for chitinases from S. maltophilia. A similar result-an optimum in the range of 35-40 °C-was determined for Streptomyces luridiscabiei U05 (Swiontek Brzezinska et al 2019).…”

Section: Discussioncontrasting

confidence: 71%

Purification, characterization and cloning of a chitinase from Stenotrophomonas rhizophila G22

et al. 2019

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In the presented research the extracellular chitinase of Stenotrophomonas rhizophila G22 was biochemically and molecularly characterized. The studied enzyme was purified from a 72-h bacterial culture about 14 times, with a recovery of 63%. The molecular weight of the purified protein was estimated at 50 kDa by SDS-PAGE. The enzyme showed high activity against colloidal chitin. Significantly lower activities were observed with native chitin powder and chitosan. Adsorption of the enzyme to colloidal chitin and to powdered chitin at the level of 75% and 37%, respectively, was observed after 30 min of reaction. Optimum temperature and pH were 37 °C and 5.9, respectively. The enzyme demonstrated higher activity against nitrophenyl-β d N, N′, N″-triacetylchitotriose and approx. 5 times lower activity for 4-nitrophenyl-N, N′-diacetylβ-d-chitobiose. The enzyme is an endochitinase, which is confirmed by the K m and V max values determined in the studies. S. rhizophila G22 endochitinase was inhibited in the presence of cysteine-specific inhibitors, which indicates the role of cysteine moieties in the mechanism of catalysis or in stabilisation of the enzyme molecule. Also Ca 2+ and Mn 2+ ions may stabilise the protein's spatial structure. SDS and ions: Fe 2+ , Cu 2+ , Co 2+ , Zn 2+ inhibited the activity of enzyme. A full-length (2109 bp) gene coding chitinase from S. rhizophila G22 was obtained. Four domains typical for glycoside hydrolase family 18 (GH 18) chitinases were identified: catalytic Gly_18, chitin-binding-ChtBD3, type-III fibronectin-FN3 and polycystic kidney disease domain-PKD domain.

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Section: Discussioncontrasting

confidence: 71%

Purification, characterization and cloning of a chitinase from Stenotrophomonas rhizophila G22

et al. 2019

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“…Similar to plants and bacteria, other studies on the interaction of AgNPs and fungi suggest that the size of AgNPs play a vital role in this interaction [ 25 , 103 , 106 ]. The presence of chitin gives a semipermeable structure to the fungal cell wall and reduces the penetration of larger size AgNPs into fungal cells [ 107 ]. In addition to soil bacteria and fungi, AgNPs can also affect decomposers.…”

Section: Environmental and Toxicological Effects Of Agnpsmentioning

confidence: 99%

Silver Nanoparticle’s Toxicological Effects and Phytoremediation

et al. 2021

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The advancement in nanotechnology has brought numerous benefits for humans in diverse areas including industry, medicine, and agriculture. The demand in the application of nanomaterials can result in the release of these anthropogenic materials into soil and water that can potentially harm the environment by affecting water and soil properties (e.g., soil texture, pH, organic matter, and water content), plants, animals, and subsequently human health. The properties of nanoparticles including their size, surface area, and reactivity affect their fate in the environment and can potentially result in their toxicological effects in the ecosystem and on living organisms. There is extensive research on the application of nano-based materials and the consequences of their release into the environment. However, there is little information about environmentally friendly approaches for removing nanomaterials from the environment. This article provides insight into the application of silver nanoparticles (AgNPs), as one of the most commonly used nanomaterials, their toxicological effects, their impacts on plants and microorganisms, and briefly reviews the possibility of remediation of these metabolites using phytotechnology approaches. This article provides invaluable information to better understand the fate of nanomaterials in the environment and strategies in removing them from the environment.

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“…Morphological and structural analyzes such as FTIR, SEM, and XRD obtained for immobilized phytase prove that the enzyme successfully binds to the ZnO surface (Arshi et al., 2020; Berini et al., 2019; Ismail et al., 2019; Preety & Hooda, 2014; Sosnowska et al., 2018).…”

Section: Discussionmentioning

confidence: 99%

Biochemical properties of phytase immobilized and its effect on growth parameters of tomato

Dikbaş,

Alım,

Uçar

et al. 2024

J. Plant Nutr. Soil Sci.

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BackgroundPhosphorus (P) is one of the nonrenewable resources of critical importance in agricultural production. P is present in soil in organic and inorganic forms. Phytate constitutes the majority of organic P in soil. Phytate binds strongly to the solid phase of the soil and becomes unavailable for use by plants. Therefore, the soluble phytate‐P ratio in soil is mostly at very low levels. Plants and associated microorganisms secrete organic acids and hydrolyzing enzymes such as phytase to dissolve phytate in the soil. Both the solubility of phytate and phytase activity are limiting properties for the uptake of phytate‐P by plants.AimsOur aim was to evaluate the effects of phytase immobilized on zinc oxide nanoparticles (ZnO Np) on tomato plant (Solanum lycopersicum) growth parameters. In this study, seedling period was analyzed.MethodsIn the study, phytase activity of 13 different bacteria was investigated, and phytase was purified from Lactobacillus kefiri, showing the highest activity, and its biochemical properties were determined. Phytase was immobilized on zinc oxide (ZnO) nanoparticles and characterized by X‐ray diffraction, Fourier transform infrared spectroscopy, and scanning electron microscopes analysis. The effects of ZnONps, immobilized phytase, and free phytase on the growth parameters of tomato plant were investigated. Tomato seeds were soaked with ZnONps, immobilized and free phytase for 30 min at room temperature and sown in pots containing suitable growing medium. Vegetative development of tomato plant, plant height, number of lateral branches, main stem diameter, distance between nodes, number of nodes, main root, and shoot length were determined.ResultsPhytase was partially purified with 7.60% recovery and specific activity of 1758.5 (EU mg−1 protein). Molecular mass of partially purified phytase was approx.72 kD, optimum pH and temperature values were determined as pH 5.0 and 70–80°C, respectively. Immobilized phytase caused a significant increase of 41.1% in plant height, 64.1% in main root, and 36.1% in shoot length in tomato plants compared to the control. In addition, a significant increase was observed in the number of side branches, main stem diameter, distance between nodes, number of nodes, and vegetative growth of the plant.ConclusionsThe results showed that the immobilized phytase enzyme has a positive effect on seedling growth in tomato and can be used in tomato cultivation in the future.

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Influence of salts and metal nanoparticles on the activity and thermal stability of a recombinant chitinase from Stenotrophomonas maltophilia N4

Cited by 7 publications

References 46 publications

Purification, characterization and cloning of a chitinase from Stenotrophomonas rhizophila G22

Purification, characterization and cloning of a chitinase from Stenotrophomonas rhizophila G22

Silver Nanoparticle’s Toxicological Effects and Phytoremediation

Biochemical properties of phytase immobilized and its effect on growth parameters of tomato

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