Lysozyme, a muramidase enzyme from egg whites (EC 3.2.1.17), is widely used in soluble form to control lactic acid bacteria in different foods. Moreover, hen egg white lysozyme is a hydrolytic enzyme that can be used to the control malolactic fermentation (MLF) during winemaking. MLF is only desirable in red and in some white wine, this suggest that MLF is at fault and needs to be controlled in all other types of wine. Lysozyme exhibits selective antimicrobial activity based on the hydrolysis of peptidoglycan cell wall constituents in lactic acid bacteria. In the last decade, several studies identified allergic reactions due to the presence of lysozyme in food. Given this relatively high incidence of lysozyme sensitization, and in accordance with the recently changed EC food legislation (1266/2010/CE), the use of lysozyme as an additive has to be declared on the ingredient label. To overcome this problem, the immobilization of the enzyme on insoluble supports, which allows the enzyme to be removed, has been the preferred strategy. In this context, this article offers a review of reports on lysozyme enological use over the last decade. It surveys the immobilization techniques and support materials used for lysozyme food preservation. This study attempts to provide useful guidance from the wealth of available immobilization data in the literature and, more importantly, to develop an integrated perspective on how to customize lysozyme for future enological uses.

Cynara cardunculus, Carica papaya and Ficus carica extracts are proposed as milk coagulants herein. Their coagulation efficiency was measured in bovine, buffalo, goat and sheep milk incubated at different temperatures. The milk-clotting and proteolytic activities as well as the lactodynamographic parameters were determined considering animal rennet as a reference coagulant. The vegetable coagulant, extracted from C. cardunculus pistils, proved to be the most suitable milk-clotting enzyme for cheesemaking, since it possesses similar milk clotting properties to conventional calf rennet. F. carica latex, but seemed to be a promising alternative coagulant at higher temperatures. The strong proteolytic activity of papain caused poor milk coagulation in all milk samples. To conclude, this result also supports the original hypothesis of this study that the excessive proteolytic nature of plant coagulants can negatively affect the cheesemaking process. The optimization of using a plant rennet in a dairy application can be done by selecting the appropriate plant rennet with a consistent clotting efficiency. These innovative manufacturing processes may also lead to the optimization and production of new cheese varieties.

The performance of 10 natural yellow colourants at different concentrations (0.001–0.3% w/v) was investigated in a model beverage system at various pH levels (3.5, 5.5 and 7.5) containing 10% w/v of sucrose, with or without ethanol (15% v/v) to simulate both alcoholic and non-alcoholic lemon-like beverages. Thus, the incidence of pH, ethanol and colourant concentration on spectral properties as well as turbidity were evaluated. The λ_max was found to be independent from concentration in the tested range (0.001– 0.3% w/v), whereas the specific absorbance at λ_max increased linearly. Moreover, the absorption spectrum and λ_max of yellow pigments were found to be independent of pH and ethanol. Gardenia, safflower, and curcumin had the highest colour intensity and the lowest turbidity level. Heat and light stability were studied for these as well. Safflower was found to be the most stable colourant against heat (25, 40, 60, 80°C) and light (550 W/m², 30°C).