Recycling by-design of plastic through formulation with thermally protected enzymes in layered double hydroxide structures

Romano, Angela; Rosato, Antonella; Totaro, Grazia; Zanaroli, Giulio; Celli, Annamaria; Sisti, Laura

doi:10.1016/j.jclepro.2022.135517

Cited by 11 publications

(15 citation statements)

References 38 publications

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“…Zou and Planck [8,9] reported the use of Na 2 SO 4 0.08 M for the release of cellulase from LDH. Therefore, preliminary kinetics studies (up to 12 h) were carried out on MgAl/cutinasebased LDH in sulfate solution and water, and the findings were reported by Romano et al [4]. Briefly, most of the cutinase was released in Na 2 SO 4 in the first 4 h, and after this time, the release profile tended to reach a plateau.…”

Section: Effect Of Medium On the Release Of Enzyme From The Ldh Struc...mentioning

confidence: 90%

“…The first release experiments of several Mg/Al LDH/cutinase, containing different amounts of enzyme, have been previously reported [4]: the findings demonstrated that the best option in terms of protein recovered and immobilization efficiency is the sample containing a 2/1 ratio of cutinase with respect to Al; therefore, in the current study, the best triggering conditions are evaluated in terms of medium, pH, and concentration.…”

Section: Introductionmentioning

confidence: 90%

“…On the other hand, the release of cutinase in water was negligible, reaching 10% in 4 h. After 12 h, the total activity recovered was 67% in sulfate solution and 14% in water. Moreover, kinetic release studies in Na 2 SO 4 0.08 M on several LDH/Cut samples with different loadings of cutinase (ranging from 3.4/1 to 0.5/1 in terms of molar ratio with respect to Al 3+ ), demonstrated that the 2/1 loading is the optimum balance in terms of immobilization efficiency (80%) and higher protein release (60%), without a loss of activity in the enzyme recovered [4].…”

Section: Effect Of Medium On the Release Of Enzyme From The Ldh Struc...mentioning

confidence: 96%

“…The LDH was prepared according to the procedure reported by Romano et al [4]. Briefly, Mg(NO 3 ) 2 •6H 2 O (0.209 g, 8.16 × 10 −4 mol) and Al(NO 3 ) 3 •9H 2 O (0.153 g, 4.08 × 10 −4 mol) were mixed with deionized and decarbonated water (50 mL) and added dropwise to a water solution (100 mL) containing cutinase (5.6 mL, 20 mg/mL, corresponding to 0.102 g and 8.36 × 10 −4 mol of enzyme).…”

Section: Immobilization Of Cutinase On Ldhmentioning

confidence: 99%

“…Among several enzymes, cutinase is a highly degrading polyester hydrolytic enzyme: biopolymers such as poly(butylene succinate) (PBS), poly(butylene succinate-co-adipate) (PBSA), and poly(caprolactone) are successfully degraded by cutinase [1][2][3]. The immobilization of cutinase in inorganic host structures such as layered double hydroxides (LDH) has been demonstrated as an effective approach to thermally protect the enzyme [4]. LDH, whose general formula is [M II 1−x M III x (OH) 2 ] x + (A n− ) x/n mH 2 O wherein M II , M III , and A n− denote divalent cations (Mg 2+ , Ca 2+ , Zn 2+ , Cu 2+ , Co 2+ , Ni 2+ , etc.…”

Section: Introductionmentioning

confidence: 99%

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Triggering of Polymer-Degrading Enzymes from Layered Double Hydroxides for Recycling Strategies

Romano

Rosato

Bianchi

et al. 2023

IJMS

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The use of degrading enzymes in polymer formulation is a very attractive strategy to manage the end-of-life of plastics. However, high temperatures cause the denaturation of enzymes and the loss of their catalytic activity; therefore, protection strategies are necessary. Once protected, the enzyme needs to be released in appropriate media to exert its catalytic activity. A successful protection strategy involves the use of layered double hydroxides: cutinase, selected as a highly degrading polyester hydrolytic enzyme, is thermally protected by immobilization in Mg/Al layered double hydroxide structures. Different triggering media are here evaluated in order to find the best releasing conditions of cutinase from LDH. In detail, phosphate and citrate–phosphate buffers, potassium carbonate, sodium chloride, and sodium sulfate solutions are studied. After the comparison of all media in terms of protein release and activity retained, phosphate buffer is selected as the best candidate for the release of cutinase from LDH, and the effect of pH and concentration is also evaluated. The amount of the enzyme released is determined with the Lowry method. Activity tests are performed via spectrophotometry.

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Section: Effect Of Medium On the Release Of Enzyme From The Ldh Struc...mentioning

confidence: 90%

Section: Introductionmentioning

confidence: 90%

Section: Effect Of Medium On the Release Of Enzyme From The Ldh Struc...mentioning

confidence: 96%

Section: Immobilization Of Cutinase On Ldhmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Triggering of Polymer-Degrading Enzymes from Layered Double Hydroxides for Recycling Strategies

Romano

Rosato

Bianchi

et al. 2023

IJMS

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Effect of functional fillers in solvent‐free polyurethane adhesives: Processing and characterization

Khemakhem,

Le Rouzic,

Brosset

et al. 2024

Polymer Engineering & Sci

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The present work is focused on the study of polyurethane adhesives in the presence of functional fillers (encapsulated enzymes) intended to make them degradable. This is part of a general strategy aiming to recycle multilayer films for packaging, at their end of life, by means of separating the constituent layers as a result of adhesives degradation. Primarily, it was found that the presence of small quantities of functional filler greatly affects both, the quality of the coating process and the kinetics of the adhesive curing. The former, because of the dependency on particle size distribution, leads to high variations in thickness and mechanical properties of multilayers and, the latter, because of a significant catalytic effect (higher curing rates). Indeed, an assessment of the adhesives' kinetics by rheology showed that the pot‐life and the cross‐over point (G′ = G″) for the enzyme‐containing system were obtained three times faster in comparison to the control formulation. These findings were also confirmed by differential scanning calorimetry measurements. On the other hand, by reducing and homogenizing the filler's particle size using separated sieved material (≤50 μm), improvements in coating control as well as in the quality and final properties of the multilayers were evidenced.Highlights Recycling multilayer plastic films for flexible packaging. Encapsulated enzymes to degrade the polyurethane adhesive in specific conditions. The presence of functional fillers affects the coating process. Process optimization to ensure the coating quality control.

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Mechanistic Insights into Cellular and Molecular Basis of Protein‐Nanoplastic Interactions

Naidu,

Nagar,

Poluri

2023

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Plastic waste is ubiquitously present across the world, and its nano/sub‐micron analogues (plastic nanoparticles, PNPs), raise severe environmental concerns affecting organisms’ health. Considering the direct and indirect toxic implications of PNPs, their biological impacts are actively being studied; lately, with special emphasis on cellular and molecular mechanistic intricacies. Combinatorial OMICS studies identified proteins as major regulators of PNP mediated cellular toxicity via activation of oxidative enzymes and generation of ROS. Alteration of protein function by PNPs results in DNA damage, organellar dysfunction, and autophagy, thus resulting in inflammation/cell death. The molecular mechanistic basis of these cellular toxic endeavors is fine‐tuned at the level of structural alterations in proteins of physiological relevance. Detailed biophysical studies on such protein‐PNP interactions evidenced prominent modifications in their structural architecture and conformational energy landscape. Another essential aspect of the protein‐PNP interactions includes bioenzymatic plastic degradation perspective, as the interactive units of plastics are essentially nano‐sized. Combining all these attributes of protein‐PNP interactions, the current review comprehensively documented the contemporary understanding of the concerned interactions in the light of cellular, molecular, kinetic/thermodynamic details. Additionally, the applicatory, economical facet of these interactions, PNP biogeochemical cycle and enzymatic advances pertaining to plastic degradation has also been discussed.

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Recycling by-design of plastic through formulation with thermally protected enzymes in layered double hydroxide structures

Cited by 11 publications

References 38 publications

Triggering of Polymer-Degrading Enzymes from Layered Double Hydroxides for Recycling Strategies

Triggering of Polymer-Degrading Enzymes from Layered Double Hydroxides for Recycling Strategies

Effect of functional fillers in solvent‐free polyurethane adhesives: Processing and characterization

Mechanistic Insights into Cellular and Molecular Basis of Protein‐Nanoplastic Interactions

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