The aperitif wine, known as vermouth, is primarily prepared by adding a mixture of herbs and spices or their extract to a base wine. As such, it could also be called aromatized liquor, or a fortified wine. Various plant parts, such as seeds, wood, leaves, bark, or roots in dry form can be used in flavoring. These additives may be infused, macerated, or distilled in a base white wine, or added at various stages of preparation. The final liquid is filtered, pasteurized, and fortified (by the addition of alcohol). Some vermouths are sweetened, whereas other are left unsweetened (dry vermouth). These tend to have a bitterish finish. The two versions differ in alcohol content as well.Vermouths are most commonly prepared from grape-based wines, but fruit-based wines made from mango, apple, plum, sand pear, and wild apricot may also be used. These possess distinct physicochemical and sensory qualities from standard vermouths.The review gives comprehensive information on the historical developments and technology of vermouth production, the various spices and herbs used in its production, and its quality characteristics. In addition, the chapter also discusses the commercial potential of nongrape fruits in vermouth production.

β-D-Galactosidase (β-D-galactoside galactohydrolase, E.C. 3.2.1.23), most commonly known as lactase, is one of the most important enzymes used in food processing, which catalyses the hydrolysis of lactose to its constituent monosaccharides, glucose and galactose. The enzyme has been isolated and purified from a wide range of microorganisms but most commonly used β-D-galactosidases are derived from yeasts and fungal sources. The major difference between yeast and fungal enzyme is the optimum pH for lactose hydrolysis. The application of β-D-galactosidase for lactose hydrolysis in milk and whey offers nutritional, technological and environmental applications to human life. In this review, the main emphasis has been given to elaborate the various techniques used in recent times for the production, purification, immobilization and applications of β-D-galactosidase. Copyright © 2006 Society of Chemical Industry