Investigating the Role of Conformational Effects on Laccase Stability and Hyperactivation under Stress Conditions

Ferrario, Virgilio F.; Chernykh, A.M.; Fiorindo, Federica; Kolomytseva, M. P.; Sinigoi, Loris; Myasoedova, N. M.; Fattor, Diana; Ebert, Cynthia; Golovleva, Ludmila; Gardossi, Lucia

doi:10.1002/cbic.201500339

Cited by 11 publications

(5 citation statements)

References 48 publications

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“…Nevertheless, there are various abundant natural materials, including lignin and rubber, which are quite resistant to biodegradation in most natural environments because of their function in nature, which requires high chemical stability and scarce reactivity of the bonds connecting their monomers [ 38 ]. As a consequence, they undergo biodegradation only under certain conditions and when attacked by specific enzymes, such as laccases in the case of lignin [ 39 ].…”

Section: Resultsmentioning

confidence: 99%

Understanding Marine Biodegradation of Bio-Based Oligoesters and Plasticizers

et al. 2023

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The study reports the enzymatic synthesis of bio-based oligoesters and chemo-enzymatic processes for obtaining epoxidized bioplasticizers and biolubricants starting from cardoon seed oil. All of the molecules had MW below 1000 g mol−1 and were analyzed in terms of marine biodegradation. The data shed light on the effects of the chemical structure, chemical bond lability, thermal behavior, and water solubility on biodegradation. Moreover, the analysis of the biodegradation of the building blocks that constituted the different bio-based products allowed us to distinguish between different chemical and physicochemical factors. These hints are of major importance for the rational eco-design of new benign bio-based products. Overall, the high lability of ester bonds was confirmed, along with the negligible effect of the presence of epoxy rings on triglyceride structures. The biodegradation data clearly indicated that the monomers/building blocks undergo a much slower process of abiotic or biotic transformations, potentially leading to accumulation. Therefore, the simple analysis of the erosion, hydrolysis, or visual/chemical disappearance of the chemical products or plastic is not sufficient, but ecotoxicity studies on the effects of such small molecules are of major importance. The use of natural feedstocks, such as vegetable seed oils and their derivatives, allows the minimization of these risks, because microorganisms have evolved enzymes and metabolic pathways for processing such natural molecules.

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Section: Resultsmentioning

confidence: 99%

Understanding Marine Biodegradation of Bio-Based Oligoesters and Plasticizers

et al. 2023

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“…17 A shift to a lower wavelength of the negative band accompanied with the disappearance of the positive peak at around 188 nm was observed for the spectrum of NPs-LC, which might arise from perturbations of β-sheet domains and attendant formation of random coil configurations. 40 To gain further details of the conformational changes of protein, a proportion of the secondary structure was quantified by DICHROWEB, as presented in Table 1. The results showed that the α-helix content in WPI increased significantly and yet the amounts of β-sheet, β-turn, and random coil were reduced upon conjugation, showing the secondary structural changes induced by covalent grafting with dextran.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…Samples with TG treatment showed a remarkably increasing CD intensity in both positive and negative ellipticities along with the red shift of the positive peak compared with Control, suggesting the increasing α-helix structure . A shift to a lower wavelength of the negative band accompanied with the disappearance of the positive peak at around 188 nm was observed for the spectrum of NPs-LC, which might arise from perturbations of β-sheet domains and attendant formation of random coil configurations . To gain further details of the conformational changes of protein, a proportion of the secondary structure was quantified by DICHROWEB, as presented in Table .…”

Section: Resultsmentioning

confidence: 99%

Mild Enzyme-Induced Gelation Method for Nanoparticle Stabilization: Effect of Transglutaminase and Laccase Cross-Linking

Liu

Cui

Muhoza

et al. 2021

J. Agric. Food Chem.

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Low-environment-sensitive nanoparticles were prepared by enzymatic cross-linking of electrostatic complexes of dextran-grafted whey protein isolate (WPI-Dextran) and chondroitin sulfate (ChS). The effect of transglutaminase (TG) and laccase cross-linking on nanoparticle stability was investigated. Covalent TG cross-linking and grafted dextran cooperatively contributed to the stability of nanoparticles against dissociation and aggregation under various harsh environmental conditions (sharply varying pH, high ionic strength, high temperature, and their combined effects). However, fragmentation induced by laccase treatment did not promote nanoparticle stability. Structural characterization showed that the compact structure promoted by TG-induced covalent isopeptide bonds repressed dissociation against varying environmental conditions and thermal-induced aggregation. Furthermore, the increasing α-helix and decreasing random coil contents benefited the formation of disulfide bonds, further contributing to the enhanced stability of nanoparticles cross-linked by TG, whereas weak hydrophobic interactions and hydrogen bonding as evidenced by the increase in β-sheet and microenvironmental changes were not able to maintain the stability of nanoparticles treated with laccase. Encapsulated cinnamaldehyde presented sustained release from TG-cross-linked nanoparticles, and the bioaccessibility was considerably enhanced to 50.7%. This research developed a novel mild strategy to enhance nanoparticle stability in harsh environments and digestive conditions, which could be an effective delivery vehicle for hydrophobic nutrients and drug applications in food and pharmaceutical industries.

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“…On the other hand, Christensen and Kepp (2013a , b ), exhaustively studied the isoforms of the laccase of Tramentes versicolor by molecular dynamics and other computational techniques in which they predict and rationalize a laccase to provide stability to mutations of multiple sites in its structure, showing that it is possible to generate stable mutants through computational studies, although to carry it out it turned out to be expensive. Ferrario et al (2015) , tested a thermal treatment with simulations of molecular dynamics on a laccase enzyme, observed that the enzyme conserved its geometry even making conformational changes in the labile parts. In contrast to our research in which through the protocol used to increase the thermal stability of Lacc 6 based on a rational approach by means of multiple methods including phylogenetic analysis, comparison with homologous proteins (particularly thermophilic), optimization of charged interactions (saline bridges and hydrogen bonds), optimization of waste and loops that show unfavorable Ramachandran angles as well as high B factors and computational design based on the structure, suggest a fast and inexpensive computational alternative.…”

Section: Discussionmentioning

confidence: 99%

In silico Design of Laccase Thermostable Mutants From Lacc 6 of Pleurotus Ostreatus

et al. 2018

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Fungal laccase enzymes have a great biotechnological potential for bioremediation processes due to their ability to degrade compounds such as ρ-diphenol, aminophenols, polyphenols, polyamines, and aryldiamines. These enzymes have activity at different pH and temperature values, however, high temperatures can cause partial or total loss of enzymatic activity, so it is appropriate to do research to modify their secondary and/or tertiary structure to make them more resistant to extreme temperature conditions. In silico, a structure of the Lacc 6 enzyme of Pleurotus ostreatus was constructed using a laccase of Trametes versicolor as a template. From this structure, 16 mutants with possible resistance at high temperature due to ionic interactions, salt bridges and disulfide bonds were also obtained in silico. It was determined that 12 mutants called 4-DB, 3-DB, D233C-T310C, F468P, 3-SB, L132T, N79D, N372D, P203C, P203V, T147E, and W85F, presented the lowest thermodynamic energy. Based on the previous criterion and determining the least flexibility in the protein structures, three mutants (4-DB, 3-DB, and P203C) were selected, which may present high stability at high temperatures without affecting their active site. The obtained results allow the understanding of the molecular base that increase the structural stability of the enzyme Lacc 6 of Pleurotus ostreatus, achieving the in silico generation of mutants, which could have activity at high temperatures.

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Investigating the Role of Conformational Effects on Laccase Stability and Hyperactivation under Stress Conditions

Cited by 11 publications

References 48 publications

Understanding Marine Biodegradation of Bio-Based Oligoesters and Plasticizers

Understanding Marine Biodegradation of Bio-Based Oligoesters and Plasticizers

Mild Enzyme-Induced Gelation Method for Nanoparticle Stabilization: Effect of Transglutaminase and Laccase Cross-Linking

In silico Design of Laccase Thermostable Mutants From Lacc 6 of Pleurotus Ostreatus

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