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1.
Bioorg Chem ; 143: 107068, 2024 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-38181659

RESUMO

α-Amylase is a secretory enzyme commonly found in nature. The α-Amylase enzyme catalyzes the hydrolysis of α-D-(1,4)-glucosidic bonds in starch, glycogen, and polysaccharides. The chemical characterization of the composite carrier and the immobilized enzyme was performed, and the accuracy of the immobilization was confirmed by FTIR, SEM, and EDS analyses. The X-ray diffraction (XRD) analysis indicates that the magnetic nanoparticle retained its magnetic properties following the modification process. Based on the Thermogravimetric Analysis (TGA) outcomes, it was evident that the structural integrity of the FPT nanocomposite remained unchanged at 200°C. The optimal pH was determined to be 5.5, and no alteration was observed following the immobilization process. Purified α-amylases usually lose their activity rapidly above 50°C. In this study, Bacillus licheniformis α-Amylase enzyme was covalently immobilized on the newly synthesized magnetic composite carrier having more azole functional group. For novelty-designed immobilized enzymes, while there is no change in the pH and optimum operating temperature of the enzyme with immobilization, two essential advantages are provided to reduce enzyme costs: the storage stability and reusability are increased. Furthermore, our immobilization technique enhanced enzyme stability when comparing our immobilized enzyme with the reference enzyme in industrial applications. The activity of the immobilized enzyme was higher in presence of 1-3% H2O2.


Assuntos
Bacillus licheniformis , Compostos de Epóxi , Nanopartículas de Magnetita , Metacrilatos , Triazóis , Enzimas Imobilizadas/química , Bacillus licheniformis/metabolismo , Peróxido de Hidrogênio , Nanopartículas de Magnetita/química , Concentração de Íons de Hidrogênio , Estabilidade Enzimática , alfa-Amilases/metabolismo , Temperatura
2.
Protein J ; 41(6): 671-680, 2022 12.
Artigo em Inglês | MEDLINE | ID: mdl-36266499

RESUMO

Enzymes are a powerful tool employed in industrial applications due to their high specificity and efficiency. Amylase enzymes play an important role in detergent, textile, analytical chemistry, and paper industries. Here we present the design, synthesis, and characterization of azole functionalized nanoparticles for the immobilization of α-amylase from Bacillus licheniformis (BlA). A modest binding efficiency (47%) was determined by the BCA assay. Enzymatic activity was measured using DNS method and illustrated the immobilization of amylase with the designed nanoparticles enhanced the thermal stability and long-term storage of amylases at a wide range of temperatures and pHs. With the required scale-up study, these implications amplify novel ways to implement this Fe3O4-PGMA-5A immobilized BlA enzyme in particular industrial applications.


Assuntos
Bacillus licheniformis , Nanopartículas , Enzimas Imobilizadas/química , Azóis , Concentração de Íons de Hidrogênio , Cinética , alfa-Amilases/química , Temperatura , Estabilidade Enzimática
3.
J Dent ; 123: 104180, 2022 08.
Artigo em Inglês | MEDLINE | ID: mdl-35691455

RESUMO

OBJECTIVES: Imidazole and benzimidazole derivatives have recently attracted attention as remarkable materials due to their advantages in chemistry, pharmacology, and biomaterials. This article focuses on dental composites with azole functional groups incorporated to affect their physicochemical and mechanical properties and antibacterial activity. METHODS: Dental composites were fabricated by embedding the functionalized imidazole and benzimidazole nanoparticles into a Bis-GMA/TEGDMA matrix to form the imidazole and benzimidazole dental composites series (I and B). The material was produced through hand blending of the monomer (50:50, wt%), filler (0-30, wt%), and initiator combination (CQ/EDMAB:0.8:1.6, wt%), and LED light-curing unit for 60 s. RESULTS: Using various characterization techniques, I and B series were validated. The dental composites' approximate solubility and sorption significances were evaluated by conducting experiments on specific dental composite formulations. Fenton reaction test was performed to determine the chemical stability of the dental composites. The mechanical properties of the dental composites were investigated. Finally, by testing cell growth in the presence of composites, their antibacterial activities were determined. CONCLUSIONS: In this study, it was observed that the mechanical, physiochemical, and antibacterial properties of the functional azole-containing nanoparticles were positively improved by adding them to the structure of dental composites. These experimental results paved the way for the synthesized materials to be used in industrial applications. CLINICAL SIGNIFICANCE: Since the chemical, mechanical, and antimicrobial properties of dental composites containing 10% imidazole and benzimidazole functional nanoparticles are far superior, they constitute an excellent alternative for preventing dental caries and long-term use of dental composites.


Assuntos
Anti-Infecciosos , Cárie Dentária , Nanopartículas , Antibacterianos/farmacologia , Anti-Infecciosos/farmacologia , Azóis , Benzimidazóis , Bis-Fenol A-Glicidil Metacrilato/química , Bis-Fenol A-Glicidil Metacrilato/farmacologia , Resinas Compostas/química , Resinas Compostas/farmacologia , Humanos , Imidazóis , Teste de Materiais , Metacrilatos/química , Nanopartículas/química , Polietilenoglicóis/química , Ácidos Polimetacrílicos/química
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