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Transglycosylation catalysed by Caco-2 membrane disaccharidases: A new approach to understand carbohydrates digestibility.
Cristina Julio-Gonzalez, Lesbia; Garcia-Cañas, Virginia; Rico, Fabian; Hernandez-Hernandez, Oswaldo.
Afiliação
  • Cristina Julio-Gonzalez L; Institute of Food Science Research, CIAL (CSIC-UAM), Madrid-28049, Spain; Faculty of Engineering, Universidad de Cartagena, Cartagena de Indias, Colombia.
  • Garcia-Cañas V; Institute of Food Science Research, CIAL (CSIC-UAM), Madrid-28049, Spain.
  • Rico F; Faculty of Engineering, Universidad de Cartagena, Cartagena de Indias, Colombia.
  • Hernandez-Hernandez O; Institute of Food Science Research, CIAL (CSIC-UAM), Madrid-28049, Spain. Electronic address: o.hernandez@csic.es.
Food Res Int ; 172: 113067, 2023 10.
Article em En | MEDLINE | ID: mdl-37689856
Under appropriate experimental conditions, some glycoside hydrolases can catalyze transglycosylation reactions; a hypothesis associated with this is that the glycosidic linkages formed will be preferentially hydrolyzed under optimal conditions. Therefore, the hydrolytic and transglycosylation activities of isolated membranes from differentiated Caco-2 cells on sucrose, maltose and isomaltulose were evaluated. After the enzymatic reactions, the di- and trisaccharides obtained were identified by gas chromatography coupled to a mass spectrometer. Differentiated Caco-2 cell membranes exerted hydrolytic and transglycosylation activities towards the studied disaccharides. The obtained di- and trisaccharides were detected for the first time using human cell models. Due to the absence of maltase-glucoamylase complex (MGAM) in Caco-2 cells, and the known hydrolytic activity of sucrase-isomaltase (SI) towards sucrose, maltose and isomaltulose, it is plausible that the glycosidic linkages obtained after the transglycosylation reaction, mainly α-glucosyl-fructoses and α-glucosyl-glucoses, were carried out by SI complex. This approach can be used as a model to explain carbohydrate digestibility in the small intestine and as a tool to design new oligosaccharides with low intestinal digestibility.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Dissacaridases / Maltose Limite: Humans Idioma: En Revista: Food Res Int Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Colômbia País de publicação: Canadá

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Dissacaridases / Maltose Limite: Humans Idioma: En Revista: Food Res Int Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Colômbia País de publicação: Canadá