The Interaction Between Surfactants and 2‐Hydroxy‐3‐(N,N‐dimethyl‐N‐dodecylammonium)‐propyloxy Starches

The phase behavior of temperature‐responsive hydrophobically modified starches and the interaction between oxidized potato amylose and hydrophobically modified potato amylopectin have been investigated by rheology, turbidity measurements and differential scanning calorimetry. When oxidized amylose was mixed with hydrophobically modified amylopectin, a viscosity peak was observed, indicative of a guest‐host interaction between the oxidized amylose and the hydrophobically modified amylopectin. A series of oxidized and hydrophobically modified potato starches were investigated in the presence of an anionic and cationic surfactant. A coil‐helix transition of the investigated starches was observed in the presence of surfactant, with the exception of a cationic surfactant combined with a hydrophobically modified zwitterionic starch of high positive net charge. The destabilizing mechanism (the phase separation) of the hydrophobically modified starches was studied as well as the difference in stabilizing capacity between the investigated cationic and anionic surfactants.     

Phase and Gelation Behavior of 2‐Hydroxy‐3‐(N,N‐dimethyl‐N‐dodecylammonium)propyloxy Starches

Some starches containing quaternary dimethylalkylammonium groups exhibit an unique phase behavior. A solid phase or gel phase is formed upon cooling, i.e. they are temperature‐responsive polymers. The aim of this study was to investigate the phase and gelation behavior of hydrophobically modified quaternary ammonium starch ethers in aqueous solutions. The mechanisms behind the phase behavior and hydrophobic character were investigated by light scattering (turbidity) and rheological measurements. A relatively large increase in the complex viscosity at higher concentrations was observed when the solutions were cooled to room temperature. The phase angle decreased drastically at a certain critical temperature. The decrease in the phase angle depended on the concentration of starch in solution, higher concentrations showing the greatest decrease and lower concentrations showing no significant change. Turbidity measurements indicated that a solid‐like highly concentrated phase was precipitated. The starch with zero net charge showed a larger increase in turbidity than the starch with a positive net charge, which indicates that particular precipitation is favored by a zero net charge and that the formation of a gel network is favored by charged starch molecules.     

Screening of β‐Glucosidase and β‐Xylosidase Activities in Four Non‐Saccharomyces Yeast Isolates

The finding of new isolates of non‐Saccharomyces yeasts, showing beneficial enzymes (such as β‐glucosidase and β‐xylosidase), can contribute to the production of quality wines. In a selection and characterization program, we have studied 114 isolates of non‐Saccharomyces yeasts. Four isolates were selected because of their both high β‐glucosidase and β‐xylosidase activities. The ribosomal D1/D2 regions were sequenced to identify them as Pichia membranifaciens Pm7, Hanseniaspora vineae Hv3, H. uvarum Hu8, and Wickerhamomyces anomalus Wa1. The induction process was optimized to be carried on YNB‐medium supplemented with 4% xylan, inoculated with 106 cfu/mL and incubated 48 h at 28 °C without agitation. Most of the strains had a pH optimum of 5.0 to 6.0 for both the β‐glucosidase and β‐xylosidase activities. The effect of sugars was different for each isolate and activity. Each isolate showed a characteristic set of inhibition, enhancement or null effect for β‐glucosidase and β‐xylosidase. The volatile compounds liberated from wine incubated with each of the 4 yeasts were also studied, showing an overall terpene increase (1.1 to 1.3‐folds) when wines were treated with non‐Saccharomyces isolates. In detail, terpineol, 4‐vinyl‐phenol and 2‐methoxy‐4‐vinylphenol increased after the addition of Hanseniaspora isolates. Wines treated with Hanseniaspora, Wickerhamomyces, or Pichia produced more 2‐phenyl ethanol than those inoculated with other yeasts.     

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.