Effect of polyol osmolytes on the structure-function integrity and aggregation propensity of catalase: A comprehensive study based on spectroscopic and molecular dynamic simulation measurements

Ali, Fasil; Manzoor, Usma; Khan, Faez Iqbal; Lai, Dakun; Khan, Md. Khurshid Alam; Chandrashekharaiah, K. S.; Singh, Laishram Rajendrakumar; Dar, Tanveer Ali

doi:10.1016/j.ijbiomac.2022.04.013

Cited by 9 publications

(4 citation statements)

References 42 publications

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“…However, the study of ternary mixtures, including proteins, water, and cosolvents, is more challenging than that of the binary system. Previous studies mainly focused on the impact of cosolvents on the structure, − dynamics, − stability, − and function , of proteins. Additionally, investigations have addressed the distribution of water and cosolvents on proteins, ,, along with the dynamics of water , in the ternary system.…”

Section: Introductionmentioning

confidence: 99%

Direct Observation of the Mutual Coupling Effect in the Protein–Water–Glycerol Mixture by Combining Neutron Scattering and Selective Deuteration

Ye,

Zheng,

Hong

et al. 2024

J. Phys. Chem. B

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Numerous studies have discussed the impact of cosolvents on the structure, dynamics, and stability of proteins in aqueous solutions. However, the dynamics of cosolvents in the protein−water−cosolvent ternary system is largely unexplored in experiments due to technical difficulty. Consequently, a comprehensive understanding of the interplay among proteins, water, and cosolvents is still lacking. Here, we employed selective deuteration and neutron scattering techniques to characterize the individual motions of each component in the protein/water/glycerol (GLY) mixture across various temperatures. The consistent dynamic onset temperatures and the correlation between the MSD of the protein and the viscosity of solvents revealed the mutual coupling effects among the three components. Furthermore, our experimental and simulation results showed that the hydrogen bond relaxation energy barrier in the ternary system is ∼43 kJ/ mol, whereas in the protein−water binary system it is merely ∼35 kJ/mol. Therefore, we suggest that GLY can enhance hydrogen bond interactions in the ternary system through the mutual coupling effect, thereby serving as one of the protective mechanisms of protein preservation by GLY.

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Section: Introductionmentioning

confidence: 99%

Direct Observation of the Mutual Coupling Effect in the Protein–Water–Glycerol Mixture by Combining Neutron Scattering and Selective Deuteration

Ye,

Zheng,

Hong

et al. 2024

J. Phys. Chem. B

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“…[28][29][30] Since catalases have the ability to decompose H 2 O 2 into water and oxygen, they are often employed for the elimination of H 2 O 2 in widespread industries, such as food, bioremediation, textile, biomedical, pharmaceutical, agricultural, detergent, and biosensor technology. [31][32][33][34][35][36] Catalase is employed to remove H 2 O 2 which can inhibit bacterial cultures required in cheese production. 37 It is used with glucose oxidase to eliminate glucose from egg white before drying for use in the baking industry.…”

Section: Introductionmentioning

confidence: 99%

“…Catalases are heme‐containing metalloenzymes existing in plants and animal tissues, and each catalase protein having ferriporphyrin as a prosthetic group in each of its four subunits 28–30 . Since catalases have the ability to decompose H 2 O 2 into water and oxygen, they are often employed for the elimination of H 2 O 2 in widespread industries, such as food, bioremediation, textile, biomedical, pharmaceutical, agricultural, detergent, and biosensor technology 31–36 . Catalase is employed to remove H 2 O 2 which can inhibit bacterial cultures required in cheese production 37 .…”

Section: Introductionmentioning

confidence: 99%

Metal ion‐mediated immobilization of catalase on poly(ε‐caprolactone)/polyethyleneimine electrospun nanofibers

Çetin

2023

J of Applied Polymer Sci

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A common industrial byproduct known as hydrogen peroxide, which is an essential intermediate, is associated with oxidative damage to brain cells and a number of neurodegenerative disorders. Although catalases are enzymes capable of decomposing hydrogen peroxide into water and oxygen, the low stability of free enzymes limits their industrial use. In the current study, poly(ε‐caprolactone)/polyethyleneimine nanofibers were fabricated using the electrospinning process and catalase was subsequently immobilized via coordination of Cu2+ ions. The characterization of the catalase‐immobilized nanofibers and their catalytic activity for hydrogen peroxide decomposition was evaluated by comparing the free catalase. The studies conducted in the pH range of 5.0–8.5 revealed that the catalase‐immobilized nanofibers had their highest levels of enzyme activity at pH 7.0. When compared to free catalase, it was shown that the thermal stability and storage stability of catalase‐immobilized nanofibers were significantly improved. Catalase‐immobilized nanofibers showed significant reusability, where activity was maintained by around 60% after five repeating cycles. The findings showed that catalase‐immobilized PCL/PEI‐Cu2+ nanofibers had a high potential for various industrial applications as a substitute for the existing techniques.

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“…Catalases are enzymes used by cells to remove excess cytoplasmic hydrogen peroxide by converting them to water and molecular oxygen. However, if the concentration of H 2 O 2 increases due to disease, radiation exposure, and certain chemicals and medications that exceed the capacity of catalase, H 2 O 2 begins to accumulate and cause cell damage [5][6][7][8]. On the other hand, the activity of the catalase enzyme can be affected by different environmental conditions, such as ionic strength, pH, and temperature (T), or due to the presence of compounds that inhibit its activity [9,10].…”

Section: Introductionmentioning

confidence: 99%

Catalase Like-Activity of Metal NPs–Enzyme Biohybrids

et al. 2022

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In this work, an efficient synthesis of bionanohybrids as artificial metalloenzymes (Cu, Pd, Ag, Mn) based on the application of an enzyme as a scaffold was described. Here we evaluated the effect of changing the metal, pH of the medium, and the amount of enzyme in the synthesis of these artificial metalloenzymes, where changes in the metal species and the size of the nanoparticles occur. These nanozymes were applied in the degradation of hydrogen peroxide for their evaluation as mimetics of catalase activity, the best being the Mn@CALB-H2O, which presented MnO2 nanostructures, with three-fold improved activity compared to Cu2O species, CuNPs@CALB-P, and free catalase.

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Effect of polyol osmolytes on the structure-function integrity and aggregation propensity of catalase: A comprehensive study based on spectroscopic and molecular dynamic simulation measurements

Cited by 9 publications

References 42 publications

Direct Observation of the Mutual Coupling Effect in the Protein–Water–Glycerol Mixture by Combining Neutron Scattering and Selective Deuteration

Direct Observation of the Mutual Coupling Effect in the Protein–Water–Glycerol Mixture by Combining Neutron Scattering and Selective Deuteration

Metal ion‐mediated immobilization of catalase on poly(ε‐caprolactone)/polyethyleneimine electrospun nanofibers

Catalase Like-Activity of Metal NPs–Enzyme Biohybrids

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