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1.
Carbohydr Res ; 498: 108191, 2020 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-33157460

RESUMO

Chitin and chitosan can undergo nonspecific enzymatic hydrolysis by several different hydrolases. This susceptibility to nonspecific enzymes opens up many opportunities for producing chitooligosaccharides and low molecular weight chitopolysaccharides, since specific chitinases and chitosanases are rare and not commercially available. In this study, chitosan and chitin were hydrolyzed using several commercially available hydrolases. Among them, cellulases with the highest specific activity demonstrated the best activity, as indicated by the rapid decrease in viscosity of a chitosan solution. The hydrolysis of chitosan by nonspecific enzymes generated a sugar release that corresponded to the decrease in the degree of polymerization. This decrease reached a maximum of 3.3-fold upon hydrolysis of 10% of the sample. Cellulases were better than lysozyme or amylases at hydrolyzing chitosan and chitin. Analysis of 13C CP-MAS NMR and FTIR spectra of chitin after cellulase treatment revealed changes in the chitin crystal structure related to rearrangement of inter- and intramolecular H-bonds. The structural changes and decreases in crystallinity allowed dissolution of chitin molecules of high molecular weight and enhanced the solubility of chitin in alkali by 10-12% compared to untreated chitin.


Assuntos
Quitina/química , Quitosana/química , Ligação de Hidrogênio , Hidrolases/metabolismo , Hidrólise , Viscosidade
2.
J Biophotonics ; 11(7): e201700322, 2018 07.
Artigo em Inglês | MEDLINE | ID: mdl-29488694

RESUMO

Interaction between nanoparticles and biomolecules leads to the formation of biocompatible or bioadverse complexes. Despite the rapid development of nanotechnologies for biology and medicine, relatively little is known about the structure of such complexes. Here, we report on the changes in conformation of a blood protein (bovine serum albumin) adsorbed on the surface of single all-dielectric nanoparticles (silicon and germanium) following light-induced heating to 640 K. This protein is considerably more resistant to heat when adsorbed on the nanoparticle than when in solution or in the solid state. Intriguingly, with germanium nanoparticles this heat resistance is more pronounced than with silicon. These observations will facilitate biocompatible usage of all-dielectric nanoparticles.


Assuntos
Temperatura Alta , Luz , Nanopartículas/química , Soroalbumina Bovina/química , Adsorção , Animais , Bovinos , Impedância Elétrica , Germânio/química , Conformação Proteica , Silício/química , Propriedades de Superfície
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