Escherichia coli (E. coli) can produce the enzyme β-galactosidase which breaks lactose into galactose and glucose. However, the gene for β-galactosidase is normally switched off, except in the presence of lactose. In this procedure, a sample of E. coli is treated with lactose, and then the β-galactosidase activity of this sample and an untreated sample are compared. ONPG (ortho-nitrophenyl-β-D-galactoside) is used as a substrate for the enzyme action which produces galactose and a compound that is yellow in alkaline conditions. The intensity (or optical density) of the yellow color produced is a qualitative indicator or quantitative measure (with a colorimeter) of the β-galactosidase activity.
β-Galactosidase is an important enzyme since lactose cannot be utilized as either carbon or an energy source until it has been broken down into its monosaccharide components. Beta-galactosidase is a huge bacterial enzyme that performs several tiny tasks. Its first task is to perform an initial step in energy production: it breaks lactose, a common sugar in milk, into two pieces, glucose, and galactose, so that they can be used in glycolysis. It also performs a similar side reaction: it can break lactose and then reconnect the pieces in a slightly different way to form allolactose. This cleavage reaction is important for the life of the bacterium, but it has also played a central role in many scientific discoveries.
♦ Complements the endogenous proteases & maximizes dietary protein digestibility.
♦ Breaks complex protein molecules into smaller peptides & amino acids for easy absorption.
♦ Expands the use of alternative protein sources.
♦ Optimizes the economics of meat & egg production, and boosts profitability.
Usage & Recommendation:
Poultry: 350 gm/ton of feed Or as per the recommendation of nutritionist or consultant.