Degradation of N‐(1‐Deoxy‐d‐xylulos‐1‐yl)glycine and N‐(1‐Deoxy‐d‐xylulos‐1‐yl)proline using thermal treatment

The formation and degradation of N‐(1‐Deoxy‐d ‐xylulos‐1‐yl)glycine and N‐(1‐Deoxy‐d ‐xylulos‐1‐yl)proline, derived from the secondary amine Maillard reaction in xylose‐amino acid model solutions, were detailed in this study. The identification and quantitative analysis of N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)glycine and N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)proline were carried out using high‐performance anion‐exchange chromatography and high‐performance liquid chromatography. The formation of intermediate and advanced products derived from N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)glycine and N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)proline was also tested using an UV‐Vis spectrophotometer to gain a better comparing of the degradation process of the two important Maillard reaction products using thermal treatment. Results showed that the degradation of N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)glycine was more significant than N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)proline. Moreover, xylose was tested in the degradation products of both N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)glycine and N‐(1‐Deoxy‐d‐ xylulos‐1‐yl)proline, which indicated that the degradation of N‐substituted 1‐amino‐1‐deoxyketoses was a reversible reaction to form reducing sugar.     

Formation of protein adducts of 2‐amino‐1‐methyl‐6‐phenylimidazo[4,5‐b]pyridine in cooked foods

Heterocyclic amines (HCAs) are mutagenic and carcinogenic compounds found in cooked meat and fish. Although HCAs are known to form adducts with protein after metabolic activation, adduct formation during cooking has not been elucidated. In this study, we showed that 2‐amino‐1‐methyl‐6‐phenylimidazo[4,5‐b]pyridine (PhIP) is released from high molecular weight compounds by acid or enzymatic hydrolysis of cooked foods. Formation of free and protein adduct forms of PhIP was dependent on cooking temperature and time, and PhIP–protein adducts were estimated to form after formation of free PhIP. We also demonstrated that PhIP–protein adduct is formed by heating of PhIP and albumin as a model protein. A new adduct peak including [M+H]⁺ (m/z=225) of PhIP as a fragment ion was detected in the high molecular weight fraction of heat‐treated protein by LC–MS analysis. From model experiments by heating of PhIP and amino acids, the adduct was estimated to be produced by condensation of the amino group of PhIP and the carboxyl group of protein. PhIP–protein adducts were detected in several cooked meat and fish at ng/g food level as PhIP content. These results suggest that food‐borne protein adducts of HCAs may influence human HCA exposure and carcinogenic risk.     

Characterization of the Supermolecular Structure of Polydatin/6‐O‐α‐Maltosyl‐β‐cyclodextrin Inclusion Complex

Polydatin is the main bioactive ingredient in many medicinal plants, such as Hu‐zhang (Polygonum cuspidatum), with many bioactivities. However, its poor aqueous solubility restricts its application in functional food. In this work, 6‐O‐α‐Maltosyl‐β‐cyclodextrin (Malt‐β‐CD), a new kind of β‐CD derivative was used to enhance the aqueous solubility and stability of polydatin by forming the inclusion complex. The phase solubility study showed that polydatin and Malt‐β‐CD could form the complex with the stoichiometric ratio of 1:1. The supermolecular structure of the polydatin/Malt‐β‐CD complex was characterized by ultraviolet–visible spectroscopy (UV), Fourier transform infrared spectroscopy (FT‐IR), X‐ray diffractometry (XRD), thermogravimetric/differential scanning calorimetry (TG/DSC), and proton nuclear magnetic resonance (¹H‐NMR) spectroscopy. The changes of the characteristic spectral and thermal properties of polydatin suggested that polydatin could entrap inside the cavity of Malt‐β‐CD. Furthermore, to reasonably understand the complexation mode, the supermolecular structure of polydatin/Malt‐β‐CD inclusion complex was postulated by a molecular docking method based on Autodock 4.2.3. It was clearly observed that the ring B of polydatin oriented toward the narrow rim of Malt‐β‐CD with ring A and glucosyl group practically exposed to the wide rim by hydrogen bonding, which was in a good agreement with the spectral data.     

Variation in 1‐fructo‐exohydrolase (1‐FEH) and 1‐kestose‐hydrolysing (1‐KH) activities and fructo‐oligosaccharide (FOS) status in onion bulbs. Influence of temperature and storage time

Effects of storage temperature and duration on 1‐fructo‐exohydrolase (1‐FEH) and 1‐kestose‐hydrolysing (1‐KH) activities and trisaccharide (Tri) and fructo‐oligosaccharide (FOS) status in onion bulbs var Tenshin kept for 24 weeks at 10 and 20 °C were investigated. 1‐FEH activity peaked sharply after 10 weeks and seemed to be triggered by a decrease in sucrose content. 1‐KH activity increased during the first 8 weeks and remained stable during the last 8 weeks. Contents of Tri, FOS and total FOS decreased abruptly during the first 8 weeks; however, at 10 °C, contents of Tri, FOS (DP 3–12) and total FOS were lower than those at 20 °C. The consumption rate of fructo‐oligosaccharides also appeared to be higher at 20 °C than at 10 °C, despite the slight degradation in activities observed at this low temperature. 1‐FEH seems to be under the control of a triggering signal which induces its activity, and sucrose seems to be this biochemical signal which initiates dormancy release and the onset of sprouting, as found previously. Thus changes in carbohydrates seem to be a strong indicator of the end of the dormant state of the bulb and the beginning of the sprouting period. Copyright © 2004 Society of Chemical Industry     

Alterations of the Profiles of Iso‐α‐Acids During Beer Ageing,Marked Instability of Trans‐Iso‐α‐Acids and Implications for Beer Bitterness Consistency in Relation to Tetrahydroiso‐α‐Acids

Age‐induced decomposition of iso‐α‐acids, the main bittering principles of beer, determines the consistency of the beer bitter taste. In this study, the profiles of iso‐α‐acids in selected high‐quality top‐fermented and lager beers were monitored by quantitative high‐performance liquid chromatography at various time intervals during ageing. The degradation of the iso‐α‐acids as a function of time is represented by the ratio, in percentage, of the sum of the concentrations of trans‐isocohumulone and trans‐isohumulone to the sum of the concentrations of cis‐isocohumulone and cis‐isohumulone. This parameter is relevant with respect to the evaluation of bitterness deterioration in aged beers. Trans‐iso‐α‐acids having a shelf half‐life of less than one year proved to be significantly less stable than cis‐iso‐α‐acids, but it appears feasible to counteract degradation if a suitable beer matrix is available. The fate of the trans‐iso‐α‐acids in particular adversely affects beer bitterness consistency. In addition to using hop products containing low amounts of trans‐iso‐α‐acids, brewers may profit of the remarkable stability of tetrahydroiso‐α‐acids, even on prolonged storage, for the production of consistently bitter beers.     

Investigation of the interaction between (−)‐epigallocatechin‐3‐gallate with trypsin and α‐chymotrypsin

Tea polyphenol (TP) inhibits digestive enzymes and reduces food digestibility. To explore the interaction between TP with digestive enzymes, bindings of ‐epigallocatechin‐3‐gallate (EGCG) to trypsin and α‐chymotrypsin were studied in detail using fluorescence, resonance light‐scattering, circular dichroism, fourier transform infrared spectroscopy methods and protein‐ligand docking. The binding parameters were calculated according to Stern–Volmer equation, and the thermodynamic parameters were determined by the van't Hoff equation. The results indicated that EGCG was capable of binding trypsin and α‐chymotrypsin with high affinity, resulting in a change of native conformation of these enzymes. EGCG had a greater influence on the structure of α‐chymotrypsin than trypsin. This study can be used to explain the binding interaction mechanism between TP and digestive enzymes.     

α‐(1,4)‐Amylase,but not α‐ and β‐(1,3)‐glucanases,may be responsible for the impaired growth and morphogenesis of Paracoccidioides brasiliensis induced by N‐glycosylation inhibition

The cell wall of Paracoccidioides brasiliensis, which consists of a network of polysaccharides and glycoproteins, is essential for fungal pathogenesis. We have previously reported that N‐glycosylation of proteins such as N‐acetyl‐β‐d ‐glucosaminidase is required for the growth and morphogenesis of P. brasiliensis. In the present study, we investigated the influence of tunycamicin (TM)‐mediated inhibition of N‐linked glycosylation on α‐ and β‐(1,3)‐glucanases and on α‐(1,4)‐amylase in P. brasiliensis yeast and mycelium cells. The addition of 15 µg/ml TM to the fungal cultures did not interfere with either α‐ or β‐(1,3)‐glucanase production and secretion. Moreover, incubation with TM did not alter α‐ and β‐(1,3)‐glucanase activity in yeast and mycelium cell extracts. In contrast, α‐(1,4)‐amylase activity was significantly reduced in underglycosylated yeast and mycelium extracts after exposure to TM. In spite of its importance for fungal growth and morphogenesis, N‐glycosylation was not required for glucanase activities. This is surprising because these activities are directed to wall components that are crucial for fungal morphogenesis. On the other hand, N‐glycans were essential for α‐(1,4)‐amylase activity involved in the production of malto‐oligosaccharides that act as primer molecules for the biosynthesis of α‐(1,3)‐glucan. Our results suggest that reduced fungal α‐(1,4)‐amylase activity affects cell wall composition and may account for the impaired growth of underglycosylated yeast and mycelium cells. © 2013 The Authors. Yeast published by John Wiley & Sons Ltd.