Glycation between proteins and sugars via the Maillard reaction has been shown to improve the heat stability of proteins. In this study, inulin, a healthy dietary fiber, was glycated with whey protein isolate (WPI), and the effects of reaction conditions were investigated. Conjugates were prepared by freeze-drying mixed WPI and inulin solutions at 1:1 to 6:1 WPI-to-inulin weight ratios followed by dry heating at 70, 75, or 80 °C for 12 to 72 h under uncontrolled, 44%, or 80% relative humidity. Heat stability was evaluated by turbidity, particle size, and rheological measurements. Degree of glycation was assessed by quantifying the loss of amino groups and the formation of the Amadori compounds. Results showed that conjugation led to improved heat stability, as shown by decreased turbidity and particle size as well as the ability to maintain the viscosity compared to control samples. Based on the loss of amino groups, the optimum glycation conditions were achieved with WPI–inulin mixtures at 2:1, 4:1, and 6:1 weight ratios and 80 °C temperature for 12 to 72 h without controlling the relative humidity. The improved heat stability could be due to an increase in negative charge as well as increased structural stabilization of the proteins. Under a limited degree of glycation, glycated WPI–inulin conjugates have great potential to be utilized as food ingredients, especially in the beverage industry.
Improved heat stability of protein solutions and O/W emulsions upon dry heat treatment of whey protein isolate in the presence of low-methoxyl pectin
