Entropy

Entropy is a measure of the number of specific ways in which a system may be arranged, often
taken to be a measure of disorder, or a measure of progressing towards thermodynamic
equilibrium. The entropy of an isolated system never decreases, because isolated systems
spontaneously evolve towards thermodynamic equilibrium, which is the state of maximum
entropy.

As an example, for a glass of ice water in air at room temperature, the difference in temperature
between a warm room (the surroundings) and cold glass of ice and water (the system and not part
of the room), begins to be equalized as portions of the thermal energy from the warm
surroundings spread to the cooler system of ice and water. Over time the temperature of the glass
and its contents and the temperature of the room become equal. The entropy of the room has
decreased as some of its energy has been dispersed to the ice and water. However, as calculated
in the example, the entropy of the system of ice and water has increased more than the entropy of
the surrounding room has decreased. In an isolated system such as the room and ice water taken
together, the dispersal of energy from warmer to cooler always results in a net increase in
entropy. Thus, when the "universe" of the room and ice water system has reached a temperature
equilibrium, the entropy change from the initial state is at a maximum. The entropy of the
thermodynamic system is a measure of how far the equalization has progressed

Source of glucose isomerase

A process for the production of glucose isomerase, comprising cultivating under aerobic conditions an
atypical Bacillus coagulans productive of a glucose isomerase, said Bacillus coagulans being capable of
growth on only inorganic nitrogen sources as the nitrogen source and at a temperature of 65 source, a
carbon source, optionally including xylose, small amounts of inorganic salts, at a pH value between 5 and
9 and a temperature between 40 is recovered.
Enzymes capable of isomerizing glucose to fructose may be obtained from a large number of different
microorganism species, and the properties of the enzymes vary from species to species. Enzyme
properties, which are particularly important for the use in the isomerization process are, stability at high
temperatures and activity at low pH values.
In an enzymatic isomerization of glucose to fructose, the following conditions are of importance:

PH: A pH value as low as possible is desired in order to avoid the alkali-catalyzed by-product formation,
i.e. below pH 7, pH 5-7 is a suitable range.
Temperature: The enzyme should be stable at a temperature of about 55

A urine test strip or dipstick is a basic diagnostic tool used to determine

pathological changes in a patients urine in standard urinalysis.
Active Site of An Enzyme
In biology, the active site is the small portion of an enzyme where substrate molecules bind and
undergo a chemical reaction. This chemical reaction occurs when a substrate collides with and slots into
the active site of an enzyme. The active site is usually found in a 3-D groove or pocket of the enzyme,
lined with amino acid residues (or nucleotides in RNA enzymes). These residues are involved in
recognition of the substrate. Residues that directly participate in the catalytic reaction mechanism are
called active site residues. After an active site has been involved in a reaction, it can be used again.

An active site is the part of an enzyme that directly binds to a substrate and carries a reaction. It
contains catalytic groups which are amino acids that promote formation and degradation of
bonds. By forming and breaking these bonds, enzyme and substrate interaction promotes the
formation of the transition state structure. Enzymes help a reaction by stabilizing the transition
state intermediate. This is accomplished by lowering the energy barrier or activation energythe energy that is required to promote the formation of transition state intermediate. The three
dimensional cleft is formed by the groups that come from different part of the amino acid
sequences. The active site is only a small part of the total enzyme volume. It enhances the
enzyme to bind to substrate and catalysis by many different weak interactions because of its
nonpolar microenvironment. The weak interactions includes the Van der Waals, hydrogen
bonding, and electrostatic interactions. The arrangement of atoms in the active site is crucial for
binding spectificity. The overall result is the acceleration of the reaction process and increasing
the rate of reaction. Furthermore, not only do enzymes contain catalytic abilities, but the active
site also carries the recognition of substrate.
The enzyme active site is the binding site for catalytic and inhibition reactions of enzyme and
substrate; structure of active site and its chemical characteristic are of specific for the binding of
a particular substrate. The binding of the substrate to the enzyme causes changes in the chemical
bonds of the substrate and causes the reactions that lead to the formation of products. The
products are released from the enzyme surface to regenerate the enzyme for another reaction
cycle
The active site is in the shape of a three-dimensional cleft that is composed of amino acids
from different residues of the primary amino acid sequence. The amino acids that play a
significant role in the binding specificity of the active site are usually not adjacent to each other
in the primary structure, but form the active site as a result of folding in creating the tertiary
structure. This active site region is relatively small compared to the rest of the enzyme. Similar to

a ligand-binding site, the majority of an enzyme (non-binding amino acid residues) exist
primarily to serve as a framework to support the structure of the active site by providing correct
orientation. The unique amino acids contained in an active site promote specific interactions
that are necessary for proper binding and resulting catalysis. Enzyme specificity depends on
the arrangement of atoms in the active site. Complementary shapes between enzyme and
substrate(s) allow a greater amount of weak non-covalent interactions including electrostatic
forces, Van der Waals forces, hydrogen bonding, and hydrophobic interactions. Specific amino
acids also allow the formation of hydrogen bonds. That shows the uniqueness of the
microenvironment for the active site.
To locate the active site, the enzyme of interest is crystallized in the presence of an analog. The
analogs resemblance of the original substrate would be considered a potent competitive inhibitor
that blocks the original substrates from binding to the active sites. One can then locate the active
sites on an enzyme by following where the analog binds.