Cross-linking of soybean protein isolate-chitosan coacervate with transglutaminase utilizing capsanthin as the model core.
J Microencapsul
; 31(7): 708-15, 2014.
Article
em En
| MEDLINE
| ID: mdl-24963959
ABSTRACT
Transglutaminase (TG) is an alternative coacervate cross-linking agent to aldehydes due to its safety. In this work, the cross-linking conditions of soybean protein isolate (SPI)-chitosan coacervates with TG-utilizing capsanthin as the model core were optimized and its cross-linking effectiveness was compared with that of glutaraldehyde. Results indicated that the optimum capsanthin microcapsule cross-linking conditions were as follows a suspension pH of 6.0, an incubation duration of 3 h, a TG concentration of 18.75 U/g SPI and a reaction temperature of 45 °C. Under these conditions, TG provided a cross-linking effectiveness comparable with that of glutaraldehyde in regards to microcapsule stability against swelling in 80 °C water and heating at 150 °C. Differential scanning calorimetry analysis revealed that TG cross-linking increased the integrity of the microcapsule walls. It was concluded that the SPI-chitosan coacervation pair has potential applications in the food industry in terms of cross-linker safety and effectiveness.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Transglutaminases
/
Proteínas de Soja
/
Reagentes de Ligações Cruzadas
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Quitosana
Idioma:
En
Revista:
J Microencapsul
Assunto da revista:
FARMACIA
Ano de publicação:
2014
Tipo de documento:
Article