Studies on the Effect of Amadoriase from Aspergillus fumigatus on Peptide and Protein Glycation In Vitro
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- 作者：Edoardo Capuano ; Francalisa Fedele ; Carmela Mennella ; Marianna Visciano ; Aurora Napolitano ; Stefania Lanzuise ; Michelina Ruocco ; Matteo Lorito ; Marí ; a Dolores del Castillo ; Vincenzo Fogliano
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：2007
- 出版时间：May 16, 2007
- 年：2007
- 卷：55
- 期：10
- 页码：4189 - 4195
- 全文大小：118K
- 年卷期：v.55,no.10(May 16, 2007)
- ISSN：1520-5118
文摘
Amadoriase I is a fructosyl amine oxidase from Aspergillus fumigatus that catalyzes the oxidation ofAmadori products (APs) producing glucosone, H2O2, and the corresponding free amine. All theenzymes of this family discovered so far only deglycate small molecular weight products and areinactive toward large molecular weight substrates, such as glycated BSA or ribonuclease A. Therefore,they cannot be used to reverse protein glycation occurring in diabetes or in foods. In this paper, theeffect of Amadoriase I added during the in vitro reaction between glucose and peptides having differentpolarities or proteins with molecular weights ranging from to 5 to 66 kDa was tested. The formationof APs was monitored by ESI-MS of intact glycated protein or peptides and by measuring the N
-(1-deoxy-D-fructos-1-yl)-L-lysine and furosine concentrations. Results showed that the formation ofAPs is reduced up to 80% when peptides and glucose are incubated in the presence of Amadoriase.The effect is more evident for hydrophobic peptides. In protein-glucose systems, the effect wasdependent on the molecular weight and steric hindrance being negligible for BSA and at a maximumfor insulin, where the formation of APs was reduced up to 60%. These findings indicate new potentialapplications of Amadoriase I as an efficient tool for inhibiting protein glycation in real food systems.
-(1-deoxy-D-fructos-1-yl)-L-lysine and furosine concentrations. Results showed that the formation ofAPs is reduced up to 80% when peptides and glucose are incubated in the presence of Amadoriase.The effect is more evident for hydrophobic peptides. In protein-glucose systems, the effect wasdependent on the molecular weight and steric hindrance being negligible for BSA and at a maximumfor insulin, where the formation of APs was reduced up to 60%. These findings indicate new potentialapplications of Amadoriase I as an efficient tool for inhibiting protein glycation in real food systems.