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|Title: ||Heat-induced Maillard reaction of the tripeptide IPP and ribose: Structural characterization and implication on bioactivity|
|Authors: ||Jiang, Zhanmei|
Rai, Dilip K
O'Connor, Paula M.
|Keywords: ||Maillard reaction|
Angiotensin-I-converting enzyme inhibitory activity
|Issue Date: ||28-Sep-2012|
|Citation: ||Zhanmei Jiang, Dilip K. Rai, Paula M. O'Connor, André Brodkorb. Heat-induced Maillard reaction of the tripeptide IPP and ribose: Structural characterization and implication on bioactivity. Food Research International, 2013, 50(1), 266-274.DOI: 10.1016/j.foodres.2012.09.028|
|Series/Report no.: ||Food Research International;vol 50|
|Abstract: ||Maillard reaction products (MRPs) were prepared from aqueous model mixtures containing 60 g L− 1 ribose and 30 g L− 1 of the bioactive tripeptide IPP (Ile-Pro-Pro), heated at 98 °C. MRP and associated reactions with changes in IPP were observed within one hour of heat-treatment. The pH of MRPs decreased significantly during the heat treatment of IPP–ribose mixtures from 9.0 to 7.6 after one hour. The amino group content, IPP and ribose concentration decreased significantly during heat treatment. The fluorescence intensity of the IPP–ribose MRPs reached the maximum within 2 h. Modification of the UV/vis spectra for IPP–ribose MRPs was mainly due to a condensation reaction of IPP with ribose. Compounds with molecular weight between 300 and 650 Da were dominant while compounds smaller than 250 Da were also produced during the reactions, as characterized by size exclusion chromatography. Mass spectrometry revealed that IPP was conjugated to ribose at the N-terminal (m/z of 458.3) upon heat-treatment. The presence of ribose also promoted peptide degradation to dehydrated IP (m/z of 211.1). IPP–ribose MRPs lost the known angiotensin-I-converting enzyme (ACE) inhibitory activity of IPP; however, strong antioxidant properties were detected.|
|Appears in Collections:||Food Biosciences|
Food Chemistry & Technology
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