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1.
Int J Biol Macromol ; 185: 572-581, 2021 Aug 31.
Artigo em Inglês | MEDLINE | ID: mdl-34216659

RESUMO

Chitosan microspheres (CMS) by the emulsion-chemical cross-linking method with and without lysozyme immobilization were synthesized and characterized. The technique conditions were adjusted, and spherical particles with approximate diameters of 3.74 ± 1.08 µm and 0. 29 ± 0.029 µm to CMS and chitosan-lysozyme microspheres (C-LMS), respectively, were obtained. The microspheres were characterized by scanning electron microscopy (FESEM), Spectroscopy Fourier Transform Spectroscopy (ATR-FTIR), X-ray diffraction (XRD), and zeta potential. Particle size was identified by laser light scattering (DLS) and the thermal properties by Differential Scanning Calorimetry (DSC) and Thermogravimetry (TGA) were determined. By the lysis of Micrococcus lysodeikticus, the activity of the microspheres was determined, and the results correlated with the amount of lysozyme used in the immobilization process and the enzyme loading efficiency was 67%. Finally, release tests pointed out the amount of enzyme immobilized on the microsphere surface. These results showed that chitosan microspheres could be used as material for lysozyme immobilization by cross-linking technique. The antimicrobial activity was tested by inhibition percent determination, and it evidenced both chitosan microspheres (CMS) and chitosan-lysozyme microspheres (C-LMS) positive antimicrobial activity to Staphylococcus aureus, Enterococcus faecalis and Pseudomonas aeruginosa.


Assuntos
Antibacterianos/farmacologia , Quitosana/farmacologia , Enterococcus faecalis/efeitos dos fármacos , Muramidase/química , Pseudomonas aeruginosa/efeitos dos fármacos , Staphylococcus aureus/efeitos dos fármacos , Antibacterianos/química , Varredura Diferencial de Calorimetria , Quitosana/química , Emulsões , Enzimas Imobilizadas/química , Microscopia Eletrônica de Varredura , Microesferas , Estrutura Molecular , Tamanho da Partícula , Propriedades de Superfície , Termogravimetria , Difração de Raios X
2.
Enzyme Microb Technol ; 132: 109384, 2020 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-31731948

RESUMO

Cellulose triacetate (CTAB) synthesized by cellulose extracted from sugarcane bagasse, and commercial cellulose acetate (CA) were used to produce nanofiber membranes contained bromelain by electrospinning technique. About 1.3 g of cellulose acetate per gram of bagasse were obtained, and both CTAB and CA was characterized by analysis of Fourier Transform Infrared Spectroscopy (FTIR) and Differential Scanning Calorimetry (DSC). The nanofiber membranes were produced by electrospinning process testing the following conditions: voltage 25 kV, flow rate 4 mL/h and distance 10 cm, using acetone/ dimethylformamide (DMF) (85:15 m/ m) to 15% cellulose triacetate (70% CA + 30% CTAB) or CA solutions. Scanning Electron Microscopy (SEM) was used to nanofiber membranes characterization. Bromelain was immobilized on the nanofiber membranes by crosslinking with glutaraldehyde and directly in the electrospinning step, the highest activity recovery was about 675% and in vitro controlled release tests were performed to semi-quantitatively evaluate the release of the enzyme bromelain thus demonstrating complete release process in 3 days.


Assuntos
Bromelaínas/química , Celulose/análogos & derivados , Eletroquímica/métodos , Nanofibras/química , Saccharum/química , Varredura Diferencial de Calorimetria , Celulose/química , Enzimas Imobilizadas/química , Microscopia Eletrônica de Varredura , Espectroscopia de Infravermelho com Transformada de Fourier
3.
J Biotechnol ; 93(1): 87-94, 2002 Jan 31.
Artigo em Inglês | MEDLINE | ID: mdl-11690697

RESUMO

Glucose oxidase was covalently immobilized on commercially available alumina and glass supports, with a high level of protein recovery. The operational stability of the alumina carrier was an advantage over the glass support, though the rate of generation of hydrogen peroxide in the case of the latter was higher. The immobilization technique provided repeated application of the enzyme even in low concentration, and the hydrogen peroxide generated in the enzymatic reaction was successively used for textile bleaching.


Assuntos
Glucose Oxidase , Peróxido de Hidrogênio/metabolismo , Têxteis , Óxido de Alumínio , Aspergillus niger/enzimologia , Biotecnologia , Celulose , Corantes/isolamento & purificação , Enzimas Imobilizadas/metabolismo , Vidro , Glucose Oxidase/metabolismo , Gossypium
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