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Catalytic elevation effect of methylglyoxal on invertase and characterization of MGO modification products.
Li, Yixin; Wang, Zitong; Wu, Jiaqi; Zheng, Jie; Liu, Fu; Ou, Juanying; Huang, Caihuan; Ou, Shiyi.
Afiliación
  • Li Y; Department of Food and Engineering, Jinan University, Guangzhou 510632, China.
  • Wang Z; Department of Food and Engineering, Jinan University, Guangzhou 510632, China.
  • Wu J; Department of Food and Engineering, Jinan University, Guangzhou 510632, China.
  • Zheng J; Department of Food and Engineering, Jinan University, Guangzhou 510632, China.
  • Liu F; Department of Food and Engineering, Jinan University, Guangzhou 510632, China.
  • Ou J; Department of Food and Engineering, Jinan University, Guangzhou 510632, China.
  • Huang C; Department of Food and Engineering, Jinan University, Guangzhou 510632, China. Electronic address: thamy@jnu.edu.cn.
  • Ou S; Department of Food and Engineering, Jinan University, Guangzhou 510632, China; Guangdong-Hong Kong Joint Innovation Platform for the Safety of Bakery Products, Guangzhou 510632, China. Electronic address: tosy@jnu.edu.cn.
Food Chem ; 460(Pt 3): 140749, 2024 Dec 01.
Article en En | MEDLINE | ID: mdl-39142204
ABSTRACT
Reactive carbonyl species can modify digestive enzymes upon intake due to their electrophilic nature. This study evaluated the effects of methylglyoxal (MGO), glyoxal, acrolein, and formaldehyde on invertase, an enzyme presents in digestive tract. Unexpectedly, MGO enhanced, rather than inhibited, invertase activity. Moreover, MGO counteracted the inhibitory effects of the other three carbonyls on invertase activity. Kinetic analyses revealed that 150 mmolLexp.-1 MGO resulted in a 2-fold increase in the Km and a 3.3-fold increase in Vmax, indicating that MGO increased the turnover rate of sucrose while reducing the substrate binding affinity of invertase. Additionally, MGO induced dynamic quenching of fluorescence, reduced free amino groups, increased hydrophobicity, the content of Amadori products, fluorescent and nonfluorescent AGEs, and amyloid fibrils of invertase. The specific modifications responsible for the elevated activity of MGO on invertase require further investigation.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Piruvaldehído / Beta-Fructofuranosidasa Idioma: En Revista: Food Chem Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido
Texto completo
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Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Piruvaldehído / Beta-Fructofuranosidasa Idioma: En Revista: Food Chem Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido