Enzymes in Industry

We will see that many different enzymes are produced in our digestive systems to help with the breakdown of food. Enzymes are also used by humans during many different industrial processes, for example, in the pharmaceutical, food and clothing industries.

Your task is to firstly read pages 34-35 of the textbook for some background information. Then you must describe the use of one enzyme in industry. You must not choose the same enzyme as anyone else in your class so please check all other responses before you begin.

Please write a summary of at leat 150 words on this enzyme. You must include information about;

- What the enzyme does
- Where the enzyme comes from
- The advantages of using this enzyme

You must provide a reference for your main source of information. This must not be Wikipedia!!!

Good Luck and remember that this material may be tested.

DUE DATE: Your second class during week 29 (11/10/10)[u]

Catalase

The enzyme Catalase has found use in one particular area of cheese production. Hydrogen peroxide is a Powerfull oxidizer and toxic to cells. It is used instead of pasteurization, when making numerous cheeses like Swiss, for preserve natural milk enzymes that are a benefit to the end product and flavour development of the cheese. These enzymes would be destroyed by the high heat of pasteurization. The residues of hydrogen peroxide in the milk will inibit the bacterial cultures that are required for the actual cheese production, so all traces of it must be removed. Catalse enzymes are typically obtained from bovine livers or microbial sources, and are added to convert the hydrogen peroxide to water and molecular oxygen.

The enzyme in yeast

The enzyme in yeast is used for many different purposes, the most known use is the use in making bread and beer.
In bread, yeast converts the fermentable sugars present in the dough into carbon dioxide and ethanol so it's volume increases.
in beer, the enzymes break down sugar (glucose) into alcohol (ethanol) and carbon dioxide (gas):
glucose(with yeast) ethanol + carbon dioxide
C6H12O6(aq)(with yeast) 2 C2H5OH(aq) + 2 CO2(g)

Fermentation works best if the yeast and glucose solution are kept warm. That's why home brewers leave their fermenting mixtures in the airing cupboard. (Remember that enzymes work best at their optimum temperature, but become ineffective if the temperature gets too high.)

People use the fermentation reaction to make all alcoholic drinks. However, stronger drinks, such as whisky or vodka, have to be distilled after fermentation to increase the concentration of the ethanol(alcohol) in the fermented mixture. This is because the ethanol poisons the yeast and stops it working when its concentration builds up to about 18 % by volume.

benjamin salata wrote:

Catalase

The enzyme Catalase has found use in one particular area of cheese production. Hydrogen peroxide is a Powerfull oxidizer and toxic to cells. It is used instead of pasteurization, when making numerous cheeses like Swiss, for preserve natural milk enzymes that are a benefit to the end product and flavour development of the cheese. These enzymes would be destroyed by the high heat of pasteurization. The residues of hydrogen peroxide in the milk will inibit the bacterial cultures that are required for the actual cheese production, so all traces of it must be removed. Catalse enzymes are typically obtained from bovine livers or microbial sources, and are added to convert the hydrogen peroxide to water and molecular oxygen.

http://biotech.about.com/od/casestudies/tp/dairyenzymes.htm

Pepsin is a digestive enzyme found in gastric juice that catalyzes the breakdown of protein to peptides. Pepsin is one of three principal protein-degrading, or proteolytic, enzymes in the digestive system. Pepsin degrades food proteins in the stomach. Pepsin acts as a potent proteolytic enzyme cleaving proteins into peptides in the gastric lumen at a low pH.
These enzyme is one of the more useful ones in the body, it is also a very common enzyme every human has it, if someone doesn’t have this they wouldn’t be able to digest the food and they would die.
These enzyme is stored between -20 to -80 degrease to prevent autolysis (self-cleavage). Autolysis may also be prevented by storage of pepsins at pH 11 or by using modified pepsins When the pH is adjusted back to 4.0 activity returns.
Finaly I woud like to add these extra information. Pepsin is one of three principal protein-degrading, or proteolytic, enzymes in the digestive system, the other two being chymotrypsin and trypsin.

Lipase
The enzyme Lipase is a water soluble enzyme that catalyzes the hydrolysis of ester chemical bonds in water insoluble lipid substrates. This enzyme does that the body break down fats in food so they can be absorbed in the intestines. Most lipases act at a specific position on the glycerol backbone of lipid substrate Lipase is primarily produced in the pancreas but is also produced in the mouth and stomach.
Along with lipase, the pancreas secretes insulin and glucagon, hormones that the body needs to break down sugar in the bloodstream. Lipases perform essential roles in the digestion, transport and processing of dietary lipids.By this we can say that hhe advantages of using the Lipase enzyme is that you can prevents lots of Diseases for example; celiac disease, indigestion cystic fibrosis, orlistat, and others.
Antonia Garbarino

Maltase

Maltase is an enzyme that catalyzes the hydrolysis of the disaccharide maltose to the simple sugar glucose. This enzyme is found in plants, bacteria, and yeast. Then there is what is called Acid maltase deficiency. It is categorized into three separate types based on the age of onset of symptoms in the affected individual.

Type a, or infantile, acid maltase deficiency usually begins to produce observable symptoms in affected individuals between the ages of two and five months.

Type b, or childhood, acid maltase deficiency usually begins to produce observable symptoms in affected individuals in early childhood. This type generally progresses much more slowly than infantile acid maltase deficiency.

Type c, or adult, acid maltase deficiency generally begins to produce observable symptoms in affected individuals in the third or fourth decades of life. This type progresses even more slowly than childhood acid maltase deficiency.

In humans and other vertebrates it is thought to be synthesized by cells of the mucous membrane lining the intestinal wall. During digestion, starch is partially transformed into maltose by the pancreatic or salivary enzymes called amylases; maltase secreted by the intestine then converts maltose into glucose. The glucose so produced is either utilized by the body or stored in the liver as glycogen (animal starch).

Ligases:
A ligase is an enzyme that acts as a catalyst for the joining of two molecules. It performs this ligation by enabling them to form a new chemical bond, and often involves simultaneous hydrolysis of ATP or a similar molecule. When working with DNA, ligases catalyze phosphodiester bonds between the 5' phosphate of a strand of DNA to the 3' hydroxyl of the other. This links two strands of DNA together. DNA ligases may also bind a DNA fragment into a plasmid vector, a primary technique when creating recombinant DNA.

The most popular DNA ligase comes from the T4 bacteriophage; it uses ATP as its cofactor. It is also possible to use a DNA ligase from E. coli using NAD as a cofactor, but it isn't often used.
This article describes a method for the global profiling of the substrate specificities of DNA ligases and illustrates examples using the Taq and T4 DNA ligases.

The method combines oligonucleotide arrays, which offer the benefits of high throughput and multiplexed assays, with mass spectrometry to permit label-free assays of ligase activity. Arrays were prepared by immobilizing ternary biotin-tagged DNA substrates to a self-assembled monolayer presenting a layer of streptavidin protein. The array represented complexes having all possible matched and mismatched base pairs at the 3′ side of the nick site and also included a number of deletions and insertions at this site. The arrays were treated with ligases and adenosine triphosphate or analogs of the nucleotide triphosphate and then analyzed by matrix-assisted laser desorption-ionization mass spectrometry to determine the yields for both adenylation of the 5′-probe strand and joining of the two probe strands. The resulting activity profiles reveal the basis for specificity of the ligases and also point to strategies that use ATP analogs to improve specificity. This work introduces a method that can be applied to profile a broad range of enzymes that operate on nucleic acid substrates.

Protease refers to a group of enzymes whose catalytic function is to hydrolyze (breakdown) peptide bonds of proteins. They are also called proteolytic enzymes or proteinases. Proteases differ in their ability to hydrolyze various peptide bonds. Each type of protease has a specific kind of peptide bonds it breaks. Examples of proteases include: fungal protease, pepsin, trypsin, chymotrypsin, papain, bromelain, and subtilisin.

Proteolytic enzymes are very important in digestion as they breakdown the protein foods to liberate the amino acids needed by the body. Additionally, proteolytic enzymes have been used for a long time in various forms of therapy. Their use in medicine is gaining more and more attention as several clinical studies are indicating their benefits in oncology, inflammatory conditions, blood rheology control, and immune regulation.

Contrary to old beliefs several studies have shown that orally ingested enzymes can bypass the conditions of the GI tract and be absorbed into the blood stream while still maintaining their enzymatic activity. Commercially, proteases are produced in highly controlled aseptic conditions for food supplementation and systemic enzyme therapy. The organisms most often used are Aspergillus niger and oryzae.

Amylase
is an enzyme that breaks down starch, converting it into sugar.There are two major types of amylase, alpha and beta. Alpha-amylase is found in human saliva, where it begins a chemical process in digestion with the hydrolysis of starch. It is also found in the pancreas. Beta-amylase is found in the seeds of some plants, as well as bacteria, yeast, and molds. Amylase is also found in other animals that use it to aid the digestive process.
The advantages are:
better specificity of reaction and therefore fewer reaction products;
• greater control over amylolysis;
• milder reaction conditions (lower temperature and pH conditions) so producing less
unwanted side reactions and by-products responsible for unwanted off-flavours and
odours;
• milder reaction conditions being responsible for more economic production, with lower
energy requirements; and
• less neutralisation of acids is required.[/font][/center]

Papain
Function: The mechanism by which it breaks peptide bonds involves deprotonation of Cys-25 by His-159. Asparagine-175 helps to orient the imidazole ring of His-159 to allow this deprotonation to take place. Cys-25 then performs a nucleophilic attack on the carbonyl carbon of a peptide backbone. This frees the amino terminal of the peptide, and forms a covalent acyl-enzyme intermediate. The enzyme is then deacylated by a water molecule, and releases the carboxy terminal portion of the peptide. In immunology, papain is known to cleave the Fc (crystallisable) portion of immunoglobulins from the Fab (antigen-binding) portion.
Uses:
-Its utility is in breaking down tough meat fibers.
-Papain, in the form of a meat tenderizer such as Adolph's, made into a paste with water, is also a home remedy treatment for jellyfish, bee, yellow jacket, stings, mosquito bites, and possibly stingray wounds, breaking down the protein toxins in the venom.
-It is also used as an ingredient in various enzymatic debriding preparations, notably Accuzyme. These are used in the care of some chronic wounds to clean up dead tissue.
-Papain can be found as an ingredient in some toothpastes or mints as teeth-whitener. Its whitening effect in toothpastes and mints is however minimal, because the papain is present in low concentrations, and will be quickly diluted by saliva.
-It is the main ingredient of Papacarie, a gel used for chemomechanical dental caries removal. Besides the advantage of avoiding the use of rotary cutting tools.
-Papain has been known to destroy THC (active chemical in marijuana) from urine. It is found in some drug detox products.
Production: Papain is usually produced as a crude, dried material by collecting the latex from the fruit of the papaya tree. The latex is collected after scoring the neck of the fruit where it may either dry on the fruit or drip into a container. This latex is then further dried. A purification step is necessary to remove contaminating substances. This purification consists of the solubilization and extraction of the active papain enzyme system through a government-registered process. This purified papain may be supplied as powder or as liquid.

Carbon film electrodes have been modified with films of cobalt hexacyanoferrate by potential cycling from solutions containing cobalt and hexacyanoferrate ions. The voltammetric characteristics of the films have been investigated in different electrolyte solutions and the properties related to insertion reactions within the crystal structure. The application of these modified electrodes as redox mediators in enzyme biosensors has been investigated using the mediated detection of hydrogen peroxide, demonstrated by the determination of glucose using glucose oxidase. Excellent detection limits in the micromolar region have been attained and the principle of measurement in real samples demonstrated by that of glucose in sweet wine.

This enzyme is found in the papaya. It is very valuable because of its diverse uses for medicinal care. It reduces inflammation and have the Tumor Necrosis Factor (TNF), which destroys tumors. Also it is used to treat, by ditroying the bacteria, stomaches dissorders like gastritis and ulcers.
The use of the papain enzyme has several benefits, such as reducing swelling and fever after surgery, treating cold sores and food allergies,helps to clean away dead tissues from the body, dissolving fats, increase inmune system functions and help those who uffer of lower pack pain, strains and sprains.
Also, papain is used in many beauty products, it helps to keep skin healthy, purguring and softening it.
Eventhought it has many uses and benefits, it also has side effects and as yet, there is no scientific evidene to prove this.