Structural studies of Myceliophthora Thermophila Laccase in the presence of deep eutectic solvents

Chan, Jou Chin; Zhang, Bixia; Martínez, Michael J.; Kuruba, Balaganesh; Brozik, James A.; Kang, ChulHee; Zhang, Xiao

doi:10.1016/j.enzmictec.2021.109890

Cited by 18 publications

(18 citation statements)

References 64 publications

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“…Hence, one can conclude that both HBAs and HBDs reduce the catalytic activity because they affect the affinity of the enzyme for the substrate (maintained or lower K m values). As indicated before, this behavior could be attributed to the effect of the DES components on the enzyme structure, as well as to the fact that the nature of each DES causes changes in some physicochemical properties, such as polarity and viscosity of the reaction medium, which in turn could affect the enzyme activity and/or the ability of the substrate to reach the active site of the enzyme [ 55 , 60 , 61 , 62 ].…”

Section: Resultsmentioning

confidence: 99%

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Tyrosinase Magnetic Cross-Linked Enzyme Aggregates: Biocatalytic Study in Deep Eutectic Solvent Aqueous Solutions

et al. 2023

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In the field of biocatalysis, the implementation of sustainable processes such as enzyme immobilization or employment of environmentally friendly solvents, like Deep Eutectic Solvents (DESs) are of paramount importance. In this work, tyrosinase was extracted from fresh mushrooms and used in a carrier-free immobilization towards the preparation of both non-magnetic and magnetic cross-linked enzyme aggregates (CLEAs). The prepared biocatalyst was characterized and the biocatalytic and structural traits of free tyrosinase and tyrosinase magnetic CLEAs (mCLEAs) were evaluated in numerous DES aqueous solutions. The results showed that the nature and the concentration of the DESs used as co-solvents significantly affected the catalytic activity and stability of tyrosinase, while the immobilization enhanced the activity of the enzyme in comparison with the non-immobilized enzyme up to 3.6-fold. The biocatalyst retained the 100% of its initial activity after storage at −20 °C for 1 year and the 90% of its activity after 5 repeated cycles. Tyrosinase mCLEAs were further applied in the homogeneous modification of chitosan with caffeic acid in the presence of DES. The biocatalyst demonstrated great ability in the functionalization of chitosan with caffeic acid in the presence of 10% v/v DES [Bet:Gly (1:3)], enhancing the antioxidant activity of the films.

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Section: Resultsmentioning

confidence: 99%

“…Apart from the shift in λ max , changes in the intensity of the fluorescence emission were observed and were most pronounced in the case of Chol DHP:Gly and Bet:Gly (1:3); this points to general changes in the microenvironment of the aromatic amino acids [ 60 ].…”

Section: Resultsmentioning

confidence: 99%

Tyrosinase Magnetic Cross-Linked Enzyme Aggregates: Biocatalytic Study in Deep Eutectic Solvent Aqueous Solutions

et al. 2023

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“…There are few studies in the literature that compare the kinetic characteristics of laccase from the ascomycete M. thermophila at different temperatures. Typically, studies tend to be conducted at the optimal operating temperature enzyme (50–60 °C). ,, To better understand the catalytic activity of laccase in the presence of NADES, we performed kinetic experiments at the enzyme’s optimal temperature (50 °C) and at a lower temperature (20 °C), to reduce the total energy of the process in practical applications. The kinetic parameters of laccase in the presence of different concentrations of NADES (10% (w/w)), in acetate buffer at pH 5, were evaluated against a range of concentrations of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) (Figure and Table ).…”

Section: Resultsmentioning

confidence: 99%

Eutectic Mixtures As Green Solvents for Laccase-Catalyzed Reactions

Freitas,

Rocha,

Noro

et al. 2023

ACS Sustainable Chem. Eng.

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“…Copper ions of laccase, which are involved in the catalytic activity of the enzyme, are present in β-sheets, which are mainly composed of conserved polar amino acids 82 . The stability and activity of laccase have been reported to be increased when the content of α-helix increased and β-sheets decreased 20 , 60 , 83 . A more rigid protein structure aligned with increasing in α-helix content could explain the higher stability of laccase HNFs than the free enzyme 20 .…”

Section: Resultsmentioning

confidence: 99%

Instantaneous synthesis and full characterization of organic–inorganic laccase-cobalt phosphate hybrid nanoflowers

Vojdanitalab

Jafari-Nodoushan

Mojtabavi

et al. 2022

Sci Rep

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A novel approach termed the "concentrated method" was developed for the instant fabrication of laccase@Co3(PO4)2•hybrid nanoflowers (HNFs). The constructed HNFs were obtained by optimizing the concentration of cobalt chloride and phosphate buffer to reach the highest activity recovery. The incorporation of 30 mM CoCl2 and 160 mM phosphate buffer (pH 7.4) resulted in a fast anisotropic growth of the nanomaterials. The purposed method did not involve harsh conditions and prolonged incubation of precursors, as the most reported approaches for the synthesis of HNFs. The catalytic efficiency of the immobilized and free laccase was 460 and 400 M−1S−1, respectively. Also, the enzymatic activity of the prepared biocatalyst was 113% of the free enzyme (0.5 U mL−1). The stability of the synthesized HNFs was enhanced by 400% at pH 6.5–9.5 and the elevated temperatures. The activity of laccase@Co3(PO4)2•HNFs declined to 50% of the initial value after 10 reusability cycles, indicating successful immobilization of the enzyme. Structural studies revealed a 32% increase in the α-helix content after hybridization with cobalt phosphate, which improved the activity and stability of the immobilized laccase. Furthermore, the fabricated HNFs exhibited a considerable ability to remove moxifloxacin as an emerging pollutant. The antibiotic (10 mg L−1) was removed by 24% and 75% after 24 h through adsorption and biodegradation, respectively. This study introduces a new method for synthesizing HNFs, which could be used for the fabrication of efficient biocatalysts, biosensors, and adsorbents for industrial, biomedical, and environmental applications.

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Structural studies of Myceliophthora Thermophila Laccase in the presence of deep eutectic solvents

Cited by 18 publications

References 64 publications

Tyrosinase Magnetic Cross-Linked Enzyme Aggregates: Biocatalytic Study in Deep Eutectic Solvent Aqueous Solutions

Tyrosinase Magnetic Cross-Linked Enzyme Aggregates: Biocatalytic Study in Deep Eutectic Solvent Aqueous Solutions

Eutectic Mixtures As Green Solvents for Laccase-Catalyzed Reactions

Instantaneous synthesis and full characterization of organic–inorganic laccase-cobalt phosphate hybrid nanoflowers

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