tryptophanase
The indole test is based on the ability of certain bacteria to produce the enzyme tryptophanase, which converts tryptophan into indole. This indole is then detected by adding a reagent such as Kovac's reagent, which reacts with indole to produce a red color. A positive test indicates the presence of tryptophanase enzyme in the bacteria.
A negative indole test typically shows no color change, indicating the absence of indole production. The medium remains yellow or unchanged, suggesting that the tested organism does not possess the enzyme tryptophanase, which is responsible for converting tryptophan to indole.
L-Tryptophane is an amino acid that is made from plant or animal resources
The indole test is a biochemical test performed on bacterial species to determine the ability of the organism to split indole from the amino acid tryptophan. This division is performed by a chain of a number of different intracellular enzymes, a system generally referred to as "tryptophanase."
The component in SIM deep tubes that makes the medium suitable to detect the production of indole by bacteria is tryptophan. Bacteria that possess the enzyme tryptophanase can break down tryptophan to produce indole, which can be detected by the addition of Kovac's reagent that reacts with indole to form a red color.
The enzyme responsible for converting glucose to fructose is glucose isomerase. It catalyzes the reversible isomerization of glucose to fructose. This enzyme is commonly used in the production of high-fructose corn syrup.
its called an enzyme
class of alkaloids containing a structural moiety of indole.
An enzyme is called a denatured enzyme once it changes its shape.
Sulfur Indole Motility test
Indole test,Proteus vulgaris is be indole positive and Citrobacter freundii will be indole negative
Changes in pH or temperature can disrupt the interactions that maintain the enzyme's specific shape, leading to denaturation and loss of enzyme activity. This is because enzymes are sensitive to changes in their environment, and alterations in pH or temperature can affect the enzyme's active site conformation, preventing it from binding to the substrate effectively.