Question

The purity of an enzyme at various stages of purification is best measured by

Answer 1

Specific activity of the enzyme

Answer 2

Answer:

Utilising inhibitor-based tests, substrate-based research, and/or comparative studies, one can determine the purity of an enzyme. The most popular and effective method for confirming enzymatic purity is through inhibitor-based tests. Combinations of these techniques can also be employed to boost assay confidence.

Explanation:

The maximum specific activity, measured in micro moles/mg protein/hour, is often found in pure enzymes, which are typically single, homogeneous proteins. Therefore, the specific activity of an unclean (heterogeneous) enzyme combined with unneeded proteins will be lower.

Table for purification. A purification table is used to keep track of the enzyme purification's progress. Utilising the protein content and enzyme activity that have been established experimentally for each fraction, the yield and relative purity of the enzyme are computed.

A solution of urea can be used to extract the enzymes from bacteria and fungus. The liquid cultured cells are collected by centrifugation or filtration, cleaned with water, and employed in the subsequent operations. Naturally, the innovation can use either fresh cells or dried cells.

The ratio of the enzyme's specific activity in the re suspended precipitate and the crude enzyme (U/mg), respectively, was called the purification factor (PF).

General Enzyme Purification Procedures

• Prepare an extract of cells. Cell extract preparation, often known as cell  lysis, is a stage of the capture phase.
• Clarification of enzymes. This procedure is regarded as the middle stage of purification.
• Clarified extract enrichment.
• Final cleansing.