(Hydroxypropyl)methyl cellulose-chitosan film as a matrix for lipase immobilization: Operational and morphological study

Vassiliadi, Evdokia; Aridas, Anastasios; Schmitt, Véronique; Xenakis, Aristotelis; Zoumpanioti, Maria

doi:10.1016/j.mcat.2022.112252

Cited by 4 publications

(6 citation statements)

References 55 publications

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“…Furthermore, it was observed that when the enzyme is incorporated into the film, fewer crystals are visible. A similar result was observed via AFM in our previous study, where the enzyme seemed to level the roughness of the film [ 21 ]. To add to this, long, narrow channels appear across most of the surface of the film ( Figure 5 ).…”

Section: Resultssupporting

confidence: 88%

“…The purpose of the present study is to thoroughly describe the structure of a biocatalyst used successfully in a previous work [ 21 ]. In this work, the two polymers (namely, HPMC and chitosan) were combined in order to formulate a film on which Mucor miehei lipase was immobilized.…”

Section: Resultsmentioning

confidence: 99%

“…Loading the films with enzyme caused more water molecules to remain trapped within the matrix, as the unloaded film had 1.4% moisture content, while the moisture content increased for the loaded film to 2.7%. Water molecules trapped in the film structure provide the conditions for the enzyme to remain active, but when the moisture content was reduced to 0.9% for the HPMC–CS enzyme-loaded film after 35 uses, not only did the enzyme activity drop significantly [ 21 ], but those nonpolar and unfavorable for polysaccharides conditions also influenced the morphology of the film. Thus, the results suggest that extensive usage of the film indirectly causes changes in the chemical structure of the enzyme (chemical degradation or precipitation) as a result of the progression of dehydration of the polysaccharide-based film.…”

Section: Resultsmentioning

confidence: 99%

“…The present study is an attempt to understand the morphology and structure of a well-studied biocompatible film, in an effort to provide insight into the performance of the biocatalyst that has been proven to give good results [ 21 ]. Having already studied the optimal conditions in which the film as a biocatalyst could perform on the model reaction of propyl laurate synthesis, the first morphological results were obtained with the use of atomic force microscopy.…”

Section: Introductionmentioning

confidence: 99%

“…Having already studied the optimal conditions in which the film as a biocatalyst could perform on the model reaction of propyl laurate synthesis, the first morphological results were obtained with the use of atomic force microscopy. The results triggered the interest to perform a deeper analysis on this easily reusable biocatalyst [ 21 ]. Therefore, the aim of the present study is to structurally characterize a biocatalyst based on the blend of two polymers, namely, (hydroxypropyl)methyl cellulose (HPMC) and chitosan (CS).…”

Section: Introductionmentioning

confidence: 99%

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(Hydroxypropyl)methyl Cellulose-Chitosan Film as a Matrix for Lipase Immobilization—Part ΙΙ: Structural Studies

Vassiliadi

Tsirigotis-Maniecka

Symons

et al. 2022

Gels

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The present work reports on the structural study of a film made of a hybrid blend of biopolymers used as an enzyme carrier. A cellulose derivative (HPMC) and chitosan (CS) were combined in order to formulate a film on which Mucor miehei lipase was immobilized. The film was successfully used as a biocatalyst; however, little is known about the structure of the system. Therefore, small-angle X-ray scattering, Fourier transform infrared spectroscopy (FTIR), optical microscopy, and scanning electron microscopy (SEM), as well as microindentation measurements, were used to shed light on the structure of the promising biocatalyst. Among the results, intermolecular hydrogen bonds were observed between the amide groups of the two polymers and the lipase. The presence of the enzyme does not seem to affect the mechanical properties of the matrix. The used film after 35 cycles of reaction seemed to be fatigued and had lost part of its humidity, explaining the reduction of the enzyme activity.

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Section: Resultssupporting

confidence: 88%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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(Hydroxypropyl)methyl Cellulose-Chitosan Film as a Matrix for Lipase Immobilization—Part ΙΙ: Structural Studies

Vassiliadi

Tsirigotis-Maniecka

Symons

et al. 2022

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Immobilization of Thermoplasma acidophilum Glucose Dehydrogenase and Isocitrate Dehydrogenase Through Enzyme-Inorganic Hybrid Nanocrystal Formation

Oshima,

Oku,

T.sriwong

et al. 2024

Curr Microbiol

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The development of green catalysts, specifically biocatalysts, is crucial for building a sustainable society. To enhance the versatility of biocatalysts, the immobilization of enzymes plays a vital role as it improves their recyclability and robustness. As target enzymes to immobilize, glucose dehydrogenases and carboxylases are particularly important among various kinds of enzymes due to their involvement in two significant reactions: regeneration of the reduced form of coenzyme required for various reactions, and carboxylation reactions utilizing CO2 as a substrate, respectively. In this study, we immobilized Thermoplasma acidophilum glucose dehydrogenase (TaGDH) and T. acidophilum isocitrate dehydrogenase (TaIDH) using a previously reported method involving the formation of enzyme-inorganic hybrid nanocrystals, in the course of our continuing study focusing on carboxylation catalyzed by the free form of TaGDH and TaIDH. Subsequently, we investigated the properties of the resulting immobilized enzymes. Our results indicate the successful immobilization of TaGDH and TaIDH through the formation of hybrid nanocrystals utilizing Mn2+. The immobilization process enhanced TaIDH activity, up to 211%, while TaGDH retained 71% of its original activity. Notably, the immobilized TaGDH exhibited higher activity at temperatures exceeding 87 °C than the free TaGDH. Moreover, these immobilized enzymes could be recycled. Finally, we successfully utilized the immobilized enzymes for the carboxylation of 2-ketoglutaric acid under 1 MPa CO2. In conclusion, this study represents the first immobilization of TaGDH and TaIDH using the hybrid nanocrystal forming method. Furthermore, we achieved significant activity enhancement of TaIDH through immobilization and demonstrated the recyclability of the immobilized enzymes.

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Poly(vinyl alcohol)-tragacanth gum/Titania bio-nanocomposite film for photodecomposition of malachite green

Mallakpour,

Ramezanzade

2024

Molecular Catalysis

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(Hydroxypropyl)methyl cellulose-chitosan film as a matrix for lipase immobilization: Operational and morphological study

Cited by 4 publications

References 55 publications

(Hydroxypropyl)methyl Cellulose-Chitosan Film as a Matrix for Lipase Immobilization—Part ΙΙ: Structural Studies

(Hydroxypropyl)methyl Cellulose-Chitosan Film as a Matrix for Lipase Immobilization—Part ΙΙ: Structural Studies

Immobilization of Thermoplasma acidophilum Glucose Dehydrogenase and Isocitrate Dehydrogenase Through Enzyme-Inorganic Hybrid Nanocrystal Formation

Poly(vinyl alcohol)-tragacanth gum/Titania bio-nanocomposite film for photodecomposition of malachite green

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