Explanation of Water as a Solvent for Life

Explanation of Water as a Solvent for Life
Water is one of the most important ingredients in life. The hydrogen bonds will bind water molecules together until they fuse. When water is liquid, hydrogen bonds are so fragile that they are formed, separated and re-formed very quickly.

Water as a Solvent for Life
With the existence of hydrogen bonds can arrange water molecules so that it will have beneficial water properties. Some chemicals cannot form a solution, but are only dispersed in water.

Solution
the solution in this case is a mixture of two or more substances. Material that has dissolving properties is called a solvent. On the other hand, dissolved substances are called solutes. For example, one tablespoon of sugar is put into a glass filled with water, then the sugar will be dissolved in water. Sugar and water will become a uniform mixture of "homogeneous", sugar as a solute, while water as a solvent.
Another example is a solution of kitchen crystals that can also dissolve in water. Kitchen salt is an ionic sodium chloride "NaCI" compound, oxygen from negatively charged water molecules. The oxygen will bind to the sodium cation. Likewise, the chloride anion will attract positively charged hydrogen from water molecules. Water will penetrate the salt crystal and will eventually dissolve all the ions. The nature of water will separate sodium from chloride so that the two "sodium and chloride" solutes will be dissolved homogeneously in water.

Colloid
In this case, colloids are two or more substances whose mix is between homogeneous and heterogeneous. This is due to differences in particle size between the solute and the solvent. Colloidal particles cannot be seen on a regular microscope, but with an ultra microscope, examples of colloids are tomato mayonnaise sauce and milk clumping.

Suspension
Suspension is two substances which are mixed but heterogeneous, phase separation occurs between the solvent and the solute. This is also due to the large particle size of the solute compared to the platen, so the solute settles, for example starch in cold water.
From ancient times, chemists tried to find universal solvents that could dissolve all kinds of substances, but no one found a better solvent than water. Through the polarity of water molecules, water can be a versatile solvent for a particular substance based on particle size and relative surface area.

Mineral is a solid composed of chemical compounds that are formed naturally by inorganic events, which have regular atomic placement and have certain physical and physical properties.
The word mineral has many meanings, depending on what aspect we review it. Mineral in the sense of geology is a chemical substance or object which is composed of original or natural processes, has certain chemical and physical properties, and is usually solid. The original chemical compound is that minerals must be formed naturally by nature, because many substances that are the same nature as minerals can be made in the laboratory. Minerals are composed of atoms and molecules of different elements but have a regular pattern. Because of this regularity makes minerals have regular properties.
Mineralogy is a branch of geology that studies minerals, both in the form of individuals and in the form of unity, including learning about physical properties, chemical properties, how they are present, how they occur and how they are used. Minerology consists of the words mineral and logos, where the meaning of minerals has a different meaning and is even confused among the laity. Often interpreted as non-organic (inorganic) material. So a clear understanding of the mineral boundaries by some geologists needs to be known even though in reality there is not a single general agreement for the definition (Danisworo, 1994).

Thus the discussion about the Explanation of Water as a Solvent for Life, hopefully with this review can add insight and knowledge of you all, thank you very much for visiting

Types of Protein Based on Components

Types of Protein Based on Components
The types of proteins based on their constituent components are divided into 3, among others.
Simple Protein (Simple Protein)
simple protein is a tabf protein from hydrolysis, the total protein is a mixture of various amino acids.
Complex Protein
complex protein is a protein which is the result of total hydrolysis of that type of protein which consists of various kinds of amino acids besides that there are also other components such as metal elements, phosphate groups. etc
Protein Derivatives (Protein derivatives)
protein derivates are proteins that are a bond between (intermediate products) contained in the results of partial hydrolysis derived from native proteins.
Types of Protein Based on Protein Sources
The protein is divided into vegetable protein and animal protein:

Protein is less than perfect
imperfect proteins are proteins whose amino acids are complete but the amounts of some of these amino acids are small. The imperfect protein is unable to fulfill growth, but the imperfect protein can maintain pre-existing tissue.

Imperfect Protein
imperfect proteins are proteins that lack or also do not have essential amino acids. The imperfect protein is not able to fulfill growth and also maintain what has existed before.

Vegetable protein
Vegetable protein is a protein derived from plants or plants.
Animal protein
Vegetable protein is a protein found in animals.
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Protein Function
The function of these proteins in general, protein functions as a body building agent and also the body's protector, metabolic booster and organ supporter in various activities, and there are many functions of protein are as follows:
Can help and also encourage growth and can maintain the composition of the body structure of cells, tissues to the organs of the body.
Protein is a source of carbohydrates.
Can help the body in the fight, destroy and can also neutralize substances from outside or foreign substances that enter the body.
Protein also functions as a supply of energy for the body.
The protein functions as dietary intake as well as being low in sugar.
Can maintain and also maintain the balance of acid base and body fluids because the protein also functions as a buffer.
Can regulate and also carry out the body's metabolism because protein is an enzyme which means proteins that activate and also enter chemical reactions.
The protein also functions as a biocatalyst
Protein is an ingredient in the synthesis of substances that are very important as well as a hormone, enzymes, antibodies and also chromosomes.

Sources of Protein
Cassava is cassava that has been dried in the sun to reduce the antinutrient content. Cassava can be used as an energy source in the ration, but its protein content is low. Use in rations should be less than 20%


Sorghum, palm oil and soybean meal
Soybean meal is a source of protein feed ingredients commonly used in poultry feed formulations. Soybean meal contains high protein and is rich in lysine, but methionine is low. Soybean meal is a by-product of soybean grinding after being extracted oil mechanically (expeller) or chemically (solvent). Soybean meal produced mechanically contains more oil and crude fiber, and less protein content compared to soybean meal produced using hexan solution. This soybean meal supplies nearly 25% of protein in poultry.
The availability of soybean meal in Indonesia does not exist, but is generally imported from several countries such as America and India. The nutritional content of soybean meal varies, depending on the type of processing such as solvent and expeller.
Soybean meal quality is listed, which consists of two qualities, namely quality 1 whose protein is higher than quality 2. The limiting factor of concern is the aflatoxin content which must not exceed 50 ppb.

Fish flour
Fish meal is a source of animal protein which is often used for chicken because it has good quality protein and amino acid sources. Some flour is imported and some is local.
Fish flour imported from America has the names herring meal, white fish meal, and menhaden meal which are distinguished based on the type of fish used. The quality of imported fish meal was measured at density of 674 kg / m cubic.
The use of fish meal in rations> 2% causes fishy odors in eggs and meat. In addition, excessive use causes symptoms of erosin in gizzard, especially young chickens.
Local fish meal has a very varied nutrient content because it comes from nonstandard fish species or from fish processing waste. Before use, it is better to analyze fish meal with crude protein and calcium content. Fish meal derived from fish processing waste (consisting of heads and bones) generally contains higher ash content than whole fish.
The quality of fish flour is controlled by. According to SNI the fish meal used in the free-range chicken ration is free of Salmonella.

Coconut cake
Coconut industry waste that can be used as animal feed is coconut cake. The quality of coconut cake varies depending on the way it is processed and the quality of raw materials. Based on its chemical composition, coconut cake includes a source of protein for livestock, the protein contained therein is 21%. In its use, especially for monogastric, it is necessary to consider the balance of amino acids, because coconut cake lacks the amino acids lysine and histidine. Coconut cake can be used for poultry should not be more than 20%.
Coconut cake is a by-product obtained from the extraction of fresh or dried coconut flesh and can be used as a source of protein. The limitations on the use of coconut cake in rations are caused by low protein digestibility, imbalance of lysine and methionine, and easy rancidity if stored for too long due to high oil content. The quality of coconut flour has been standardized with SNI 01-2904-1992.

Peanut meal
Peanut meal is a by-product of grinding peanut seeds after oil extraction mechanically (expeller) or chemically (solvent). Peanut meal is a source of protein for chicken. Its use in rations is limited because it contains high crude fiber.

Meat and bone flour
Meat and bone flour is a food source of animal protein. The quality varies depending on the amount of bone used. If the bone used to make high MBM, it can be seen from the high ash and mineral content of Ca and P. MBM as a feed source for protein sources has 50% protein content and can contribute quite high Ca in the feed.

Combined Protein which is a Protein Composed and Non-Protein Groups

Combined Protein which is a Protein Composed and Non-Protein Groups
Combined protein which is a protein composed of proteins and non-protein groups. This group is called a prosthetic group and consists of carbohydrates, lipids or nucleic acids:
Posferoprotein:
contains folic acid groups which are bound to the hydraulics of serine and theroin. Lots found in milk and egg yolks.
Lipoprotein:
contains fatty acid lipids, listin. So that it has the capacity as a good emulsifying agent, found in eggs, milk and blood.
Nucleoprotein:
a combination of nucleic acids and proteins. For example: mucin in saliva, ovomucin in eggs, nucleoid in serum.
Chromoprotein:
combination of proteins with pigmented groups which usually contain metal elements. Example: hemoglobin, myglobulin, chlorophyll and flavoprotein.
Metalloprotein:
is a major complex between proteins and metals as well as chromator protein. Example: ferritrin (containing Fe), coalbumin (containing CO and Zn).
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Globulin
Soluble in neutral salt solution, but not soluble in water. Coagulated by heat and will settle to a high concentration of salting solution (salting out) in the body there are many antibodies and fibrinogen. In milk there is in the form of lactoglobulin, in eggs ovoglobulin, in the meat of myosin and acitin and in soybeans called glycillin or generally in legumes called legumin.

Glutelin
Soluble in dilute acids and bases, but not soluble in neutral solvents. Example: gluten in wheat and oryzenin in rice.

Prolanin
Soluble in ethanol 50-90% and insoluble in water. This protein contains a lot of proline and glutamic acid, and there are many in the serelia. For example: zein in corn, gliadin in wheat, and cordurine in barley.

Scleroprotein
Insoluble in water and neutral solvent and resistant to enzymatic hydrolysis. This protein functions as a protective structure in humans and animals. Examples of collagen, elastin, and keratin.

Histones
Is a basic protein, because it contains lysine and arginine. Is soluble in water and will be clotted by ammonia.

Globulin
Almost the same as histones. Globulin is rich in arginine, tryptophan, histidine but does not contain isoleucines found in the blood (hemoglobin).

Protein
A very simple protein, BM is relatively low (4000-8000), rich in arginine, soluble in water and coagulated by heat and is basic.
Simple proteins according to their molecular shape are divided into 2 groups, namely:
Fiber protein (= skleroprotein = albumoid = skrelin)
Fibers are long and are bound together as fibrils by hydrogen bonds. Insoluble in water, so this lack of solution results in strong intermolecular forces. For example, keratin (hair, nails, feathers, horns), in kalogen (connective tissue), fibroin (silk) and myosin (muscle).
These fibrous proteins are fibrous; insoluble in dilute solvents, either salt, base or alcohol solutions. The molecule consists of a long chain of molecules, parallel to the main chain, does not form crystals and when pulled extends back to its original shape. The function of this protein is to form the structure of materials and tissues, for example keratin in the hair. This protein molecule consists of several polypeptide chains that extend and are connected to each other by several cross bonds to form a stable fiber or fiber. Its large molecular weight cannot be determined with starch and is difficult to be purified.

Globural protein
Globural protein shaped like a ball, found in many animal ingredients (milk, meat, eggs). This protein dissolves easily in salts and dilute acids and is easily changed due to the influence of temperature, concentration of salt, acids and bases and is easily denatured. Globular proteins are generally round or elliptical and consist of the polypeptide chains involved.

Types of Protein
In these proteins there are types or kinds of proteins that are divided into 3 parts, including the following:
Types of Protein Based on Function
Protein based on its function consists of 3 types, including the following:

Perfect Protein
Perfect protein is a protein which contains a complete amino acid. That perfect protein is generally found in animal protein.

Antiparallel Conformation and Tertiary Structure of Protein

Antiparallel Conformation and Tertiary Structure of Protein
The tertiary structure of a protein is the overall fold of the polypeptide chain so that it forms a certain 3-dimensional structure. For example, the tertiary structure of an enzyme is often dense, globular in shape. A tertiary structure is a combination of a variety of secondary structures. Tertiary structures are usually lumps. Some protein molecules can interact physically without covalent bonds to form stable oligomers (for example dimers, trimers, or quarters) and form quaternary structures.
These folds are controlled by hydrophobic interactions, but the structure can be stable only if the parts of the protein are locked into place by specific tertiary interactions, such as salt bridges, hydrogen bonds, and tight side chain packaging and disulfide bonds.
The tertiary structure of a protein is an overlapping layer over a secondary structural pattern consisting of irregular twists of bonds between side chains (R groups) of various amino acids (Figure 9). This structure is a three-dimensional conformation that refers to the spatial relationship between secondary structures. This structure is stabilized by four types of bonds, namely hydrogen bonds, ionic bonds, covalent bonds, and hydrophobic bonds. In this structure, hydrophobic bonds are very important for proteins. Amino acids that have hydrophobic properties will bind to the inside of globular proteins that don't bind to water, while amino acids that are hodrophilic in general will be on the outer surface of the surface that binds to the surrounding water (Murray et al, 2009; Lehninger et al., 2004).

Secondary structure
The secondary structure of proteins is regular, the pattern of repeated folds of the protein skeleton. The two most patterns are alpha helix and beta sheet. The secondary structure of proteins is the local three-dimensional structure of various amino acid sequences in proteins that are stabilized by hydrogen bonds. Various forms of secondary structures, for example, are as follows:
alpha helix (α-helix, "torsion-alpha"), in the form of a twisted chain of amino acids shaped like a spiral;
beta-sheet (β-sheet, "beta-plate"), in the form of wide sheets composed of a number of amino acid chains bound together through hydrogen bonds or thiol (S-H) bonds;
beta-turn, (β-turn, "beta-indentation"); and gamma-turn, (γ-turn, "gamma-indentation").
The secondary structure is a combination of the primary structure which is linearly stabilized by hydrogen bonds between the CO = and NH groups along the polypeptide spine. One example of a secondary structure is α-helical and β-pleated (Figures 4 and 5). This structure has segments in the polypeptide that are twisted or folded repeatedly. (Campbell et al., 2009; Conn, 2008).

Secondary structure
The α-helical structure is formed between each of the carbonyl oxygen atoms in a peptide bond with hydrogen attached to the amide group in a peptide bond of four amino acid residues along the polypeptide chain (Murray et al, 2009).
In the secondary structure β-pleated is formed through hydrogen bonds between linear regions of the polypeptide chain. β-pleated two forms are found, namely antiparrel and parallel (Figures 6 and 7). Both are different in terms of the hydrogen bonding pattern. In the form of antiparrel conformation has a bond conformation of 7 Å, while conformation in the parallel form is shorter which is 6.5 Å (Lehninger et al, 2004). If this hydrogen bond can be formed between two separate polypeptide chains or between two regions in a single chain that folds itself which involves four amino acid structures, then it is known as β turn shown in Figure 8 (Murray et al, 2009).

Tertiary structure and quaternary structure
Some proteins are composed of more than one polypeptide chain. Quartener structures describe different subunits that are used together to form protein structures.
The quaternary structure is a picture of the arrangement of sub-units or protein promoters in space. This structure has two or more of the protein sub-units with tertiary structures that will form functional protein complexes. the bonds that play a role in this structure are noncovalent bonds, namely electrostatic, hydrogen and hydrophobic interactions. Proteins with quaternary structures are often referred to as multimeric proteins. If a protein composed of two subunits is called a dimeric protein and if it is made up of four subunits it is called a tetrameric protein (Figure 10) (Lodish et al., 2003; Murray et al, 2009).

Protein Primary Structure

Protein Primary Structure
A kind of amino acid
There are 20 kinds of amino acids, each of which is determined by the type of R group or side chain of amino acids. If the R group is different then the type of amino acid is different. For example, the amino acids serine, aspartic acid and leucine have differences only in the type of R group
The R groups of amino acids vary in size, shape, charge, hydrogen binding capacity and chemical reactivity. The twenty types of amino acids have never changed. The simplest amino acid is glycine with H atoms as side chains. Next is alanine with a methyl group (-CH3) as a side chain.

Peptide Bonds
The twenty kinds of amino acids bind together, in a variety of order to form proteins. The process of forming proteins from amino acids is called protein synthesis. The bond between one amino acid and another is called a peptide bond. This peptide bond can also be called an amide bond.
Try to review the basic structure of amino acids. In proteins or amino acid chains, the carboxyl group (-COOH) binds to the amino group (-NH2). Each peptide bond is formed, issued 1 water molecule (H2O).

Protein Structure
Proteins made up of amino acid chains will have a variety of structures that are unique to each protein. Because proteins are composed of amino acids that are chemically different, a protein will be strung through peptide bonds and sometimes even connected by sulfide bonds. Furthermore, proteins can be folded to form various structures.

There are 4 levels of protein structure namely primary structure, secondary structure, tertiary structure and quaternary structure.
Primary structure
The primary structure is a simple structure with sequences of amino acids arranged in a linear fashion similar to the order of letters in a word and no chain branching occurs.

Primary structure
The primary structure is formed by the bond between the α-amino group and the α-carboxyl group (Figure 3). These bonds are called peptide bonds or amide bonds. This structure can determine the order of an amino acid from a polypeptide.

Peptide formation reaction
Frederick Sanger was a scientist who contributed to the discovery of methods for determining amino acid sequences in proteins, with the use of several protease enzymes that slice the bonds between certain amino acids into shorter peptide fragments to be further separated with the help of chromatographic paper. The amino acid sequence determines the function of proteins, in 1957, Vernon Ingram found that amino acid translocation would change the function of proteins, and further trigger genetic mutations.
The primary structure of a protein refers to the linear amino acid sequence of the polypeptide chain. The primary structure is caused by covalent bonds or peptides, which are made during the process of protein biosynthesis or called the translation process. The two ends of the polypeptide chain are called carboxyl (C-terminal) and amino (N-terminal) ends based on the nature of the free group. Residue calculations always begin at the end of the N-terminal (amino group, -NH2), which is the end where the amino group is not involved in the peptide bond. The primary structure of proteins is determined by genes associated with proteins. A certain sequence of nucleotides in DNA is transcribed into mRNA, which is read by ribosomes in a process called translation. Protein sequences can be determined by methods such as Edman's degradation.

Quartener structure
Judging from its structure, proteins can be divided into 2 groups, namely:
A simple protein which is a protein consisting only of amino acid molecules. Included in the group for example:
Protamin
This protein is alkaline and does not experience coagulation on heating.

Albumin
Protein is soluble in water and aqueous salt solution, the BM is relatively low. Albumin is found in egg white (egg albumin), milk (lactalbumin), blood (blood albumin) and vegetables.

Complete Definition of Protein Type and Function

Complete Definition of Protein Type and Function
Protein: Definition, Function, Source, Benefits, Elements and Structure are complex organic compounds with high molecular weight, which are polymers of amino acid monomers

Definition of Protein
Proteins are high molecular weight complex organic compounds which are polymers of amino acid monomers that are connected to each other by peptide bonds. Protein molecules contain carbon, hydrogen, oxygen, nitrogen and sometimes sulfur and phosphorus. Protein plays an important role in the structure and function of all living cells and viruses. Most of the protein is an enzyme or enzyme subunit. Other types of proteins play a role in structural or mechanical functions, such as proteins that make up the cytoskeleton in the rods and joints.
Protein is involved in the immune system (immune) as an antibody, a control system in the form of hormones, as a storage component (in seeds) and also in nutrient transportation. As one source of nutrition, protein acts as a source of amino acids for organisms that are unable to form these amino acids (heterotrophs). Protein is one of the giant biomolecules, in addition to polysaccharides, lipids and polynucleotides, which are the main constituents of living things. In addition, protein is one of the most studied molecules in biochemistry.
Protein was discovered by Jöns Jakob Berzelius in 1838. Biosynthesis of natural proteins equals genetic expression. The genetic code carried by DNA is transcribed into RNA, which acts as a template for the translation by the ribosome. Until this stage, the protein is still "raw", only composed of proteinogenic amino acids. Through the post-translational mechanism, proteins are formed which have full biological functions. Sources of protein come from Meat, Fish, Eggs, Milk, and similar products of Quarks, Plant seeds, Tribes of legumes and Potatoes.
Protein (protos which means "foremost") is a complex organic compound that has a high molecular weight which is a polymer of amino acid monomers that are connected to each other by peptide bonds. Peptides and proteins are amino acid condensation polymers by removing water elements from amino groups and carboxyl groups.

If the molecular weight of a compound is less than 6,000, it is usually classified as a polypeptide. Proetin is contained in many foods that are often consumed by humans. As in tempeh, tofu, fish and so on. In general, the source of protein is from vegetable and animal sources. Protein is very important for the life of organisms in general, because it functions to repair damaged body cells and supply the nutrients the body needs. So, it is important for us to know about protein and related matters. Protein is one of the giant biomolecules in addition to polysaccharides, lipids and polynucleotides which are the main constituents of living things.
Proteins are high molecular weight complex organic compounds which are polymers of amino acid monomers that are connected to each other by peptide bonds. The protein molecule itself contains carbon, hydrogen, oxygen, nitroge and sometimes sulfur and phosphorus. The protein was formulated by Jons Jakob Berzelius in 1938.

Components of Protein Components
The basic unit of protein structure is amino acids. Amino acids are organic compounds that contain amino groups (NH2), a carboxylic acid group (COOH), and one of the other groups, especially from a group of 20 compounds that have the basic formula NH2CHRCOOH, and are linked together by peptide bonds. In other words, proteins are composed of amino acids that bind to one another.

Amino acid structure An amino-α acid consists of:
Atom C α. Called α because it is next to a carboxyl (acid) group.
The H atom is bound to the C α atom.
Carboxyl groups are bound to the C α atom.
The amino group is bound to the C α atom.
The R group which is also bound to the C α atom.

Carbohydrate Testing Methods in Food

Carbohydrate Testing Methods in Food
The three reactions above have almost the same principle, namely using an aldehyde group in sugar to reduce the Cu2SO4 compound to Cu2O (brick red enpadan) after being heated in an alkaline atmosphere (Benedict and Fehling) or acid (Barfoed) with the addition of a binding agent (chelating agent) like Na-citrate and K-Na-tatrat.

Iodine reaction
KH (poilisaccharide) + Iod (I2) à specific color (black blue)

Seliwanoff's reaction
KH (ketose) + H2SO4 à furfural à + resorcinol à red color.
KH (aldosa) + H2SO4 à furfural à + resorcinol à negative

Osazon reaction
This reaction can be used both for aldose and ketose solutions, by adding a phenylhydrazine solution, then heated to form a yellow crystal called hydrazone (osazon).

Quantitative Test
For the determination of carbohydrate levels can be done by physical, chemical, enzymatic, and chromatographic methods (not discussed).

Physical Method
There are two (2) types, namely:
Based on the refractive index
This method uses a device called a refractometer, which is by the formula:
X = [(A + B) C - BD)]

Where :
X =% of sucrose or sugar obtained
A = weight of sample solution (g)
B = weight of diluent solution (g)
C =% sucrose in camp A and B in the table
D =% sucrose in thinner B

Based on optical rotation
This method is used based on the optical properties of sugars that have an asymmetrical structure (can rotate the plane of polarization) so that it can be measured using a device called a polarimeter or digital polarimeter (the result can be known directly) called a sacarimeter.
According to Biot law; "The optical rotation size of each individual sugar is proportional to the concentration of the solution and the thickness of the liquid" so that it can be calculated using the formula:
[a] D20 = 100 A
L x C

Where :
[a] D20 = rotation type at 20 oC using
D = yellow light at a wavelength of 589 nm from the Na lamp
A = observed angle of rotation
C = content (in g / 100 ml)
L = tube length (dm)
so C = 100 A
L x [a] D20

Chemical Method
This method is based on the reducing properties of sugars, such as glucose, galactose, and fructose (except sucrose because it has no aldehyde group). Even though fructose does not have an aldehyde group, it has an alpha hydroxy ketone group, so that it can still react.

In this chemical method there are two (2) kinds of ways, namely:
Titration
For the first way, it can see the standardized method by BSN, namely the SNI for food and beverage testing SNI number 01-2892-1992.

Spectrophotometry
The second method uses the principle of CuSO4 reduction reaction by carbonyl groups on reducing sugars which after heating is formed of oxide oxide deposits (Cu2O) and then added Na-citrate and Na-tatrate and phosphomolibdic acid to form a blue compound compound that can be measured by spectrophotometer at a wavelength of 630 nm.

Enzymatic Method
For this enzymatic method, it is very appropriate to be used for determining the sugar casing individually, due to the work of a very specific enzyme. Examples of enzymes that can be used are glucose oxidase and hexokinase. Both are used to measure glucose levels.

Glucose oxidase
D-Glucose + O2 by glucose oxidase à Gluconate Acid and H2O2
H2O2 + O-disianidin by the peroxidase enzyme à 2H2O + brown-oxidized O-disianidin (can be measured at 1540 nm)

Hexokinase
D-Glucose + ATP by hexokinase à Glucose-6-Phosphate + ADP
Glucose-6-Phosphate + NADP + by glucose-6-phosphate dehydrogenase à Gluconate-6-Phosphate + NADPH + H + The presence of fluorescent NADPH (having chromophore groups) can be measured at 334 nm where the amount of NADPH formed is equal to the amount of glucose.