Commercial Uses of enzymes; Pectinases and Proteases

Hi, I need notes on the following:

"The commercial uses of enzymes as illustrated by pectinases in food modification and proteases in biological detergents."

I will send +ve rep in the direction of the first person who can provide me with appropriate notes. Thanks in advance.

Reply 1

Dimez

The industrial use of enzymes (not using the whole microbe)
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Leather:

The earliest example of enzymes in industry is a colourful one! To make leather soft, it has to be bated, which means that some of the protein fibres are removed. Otherwise, the leather will be hard - perfect for the soles of shoes but of little use for anything else.

The Roman writer Pliny reported the use of pigeon droppings for this process over 2000 years ago. Later, leather was bated by smearing it with dog excrement! People used to go around the streets collecting dog turds and then rubbed them into the skins by hand, paddle or by trampling it in by foot.

By the early 1900’s it was known that the excrement was rich in bacteria which produced proteases, which degraded part of the leather. It was a highly skilled job to prevent the enzymes damaging the leather, which is largely made up of protein. But thanks to the The German scientist Ršhm, developed a standardized bate in 1908, based on an extract from the pancreases of slaughtered animals. This contained trypsin - one of a mixture of enzymes found in the digestive system. Since then, all bates have been based on enzyme preparations, though now bacterial and fungal enzymes are used instead.

Washing powders:

Ršhm was quite a genius - he was the first to examine the chemical composition of dirt on laundry and he came up with the idea of using the pancreatic extract to wash clothes. His wife tested trypsin at home on their dirty underwear - and found it was excellent! When soaked overnight, their clothes became clean and the water became dirty. So, he patented his idea and in 1914, developed the first enzymatic washing agent. It was so effective that only a small quantity was required: it was sold as a spot remover. Unfortunately German housewives were used to bulky washing powders that produced lots of lather so they regarded it with suspicion. In 1915, some people even thought it was a hoax. The product was investigated by scientists who found that it really did work – indeed, it was about 50 years ahead of its time: it wasn’t until the 1960s that enzymatic detergents gained widespread acceptance.

The mass-production of an alkaline protease suitable for wash conditions began in 1962. Unlike trypsin, this wasn’t an animal extract but a product of microbial fermentation. This new enzyme was initially shunned by detergent manufacturers but there were exceptions. In 1963, it was incorporated into Bio-tex, which took the market by storm. Industry began to take notice of enzymes and by 1967 their widespread use in domestic detergents was commonplace.

Enzymes used:

These are produced from Bacillus licheniformis. They are usable at high pH and temperatures up to 60o C and are all relatively non-specific proteases. They attack the C-terminal of carboxyl amino acids producing small peptides which can be readily dissolved by the detergent. There is currently considerable interest in developing better proteases for washing powders through protein engineering, particularly in engineering oxidation-resistance into the proteases.

Enzymes used:

These are produced from Bacillus licheniformis. They are usable at high pH and temperatures up to 60o C and are all relatively non-specific proteases. They attack the C-terminal of carboxyl amino acids producing small peptides which can be readily dissolved by the detergent. There is currently considerable interest in developing better proteases for washing powders through protein engineering, particularly in engineering oxidation-resistance into the proteases.

Engineered Subtilisin for improved wash performance

Not just proteases

Since the 1990’s, amylases have also been added to detergents to remove stains from spaghetti, sauces, oatmeal and baby foods. In 1988 the first detergent lipase was released - the first commercial enzyme to be produced from a genetically-modified organism (GMO). Today more than 90% of detergent enzymes are made from GMOs.

The detergent industry has been the largest market for industrial enzymes for over 25 years, accounting for 37% of world sales of enzymes. Apart from laundry detergents, many automatic dishwashing detergents now also contain enzymes.

To maximise the effectiveness and to be as economical as possible in the production process the enzyme molecules must be brought into maximum contact with the substrate molecules. This can be achieved by mixing the solutions of enzyme and substrate in suitable concentrations. However this means that the enzyme is ‘lost’ with each batch of product made and that the end-product will be contaminated too – as in cheese manufacture:

Cheese making: Warm milk is mixed (about 2000:1) with the enzyme rennin (rennet) (formerly extracted from (dead) calves’ stomachs, but now produced from bacteria) and allowed to react for several hours. The caesinogen in the milk is uncoiled and clots to casein. This turns the milk solid. The curds (solid) are then cut with a knife and the whey (liquid) drained away and fed to animals (remember Miss Tuffet?). The chopped up curd is then salted and placed in a mould before squeezing to remove any trapped air (a process known as ‘cheddaring’ – hence Cheddar cheese). Sometimes the cheese is then dipped in brine or a solution of fungal spores to inoculate it and produce a surface ‘rind’.

The cheese is then left at a constant, low, temperature (in the old days, in a cave, hence many cheeses are associated with cave-rich districts) to mature. this may take up to a year or more, so cheese-making was an important way of preserving a valuable food through the winter in the days before refrigeration.

The ‘blue’ in cheeses such as Stilton, is added by pushing spore-covered wires (Penicillium notatum- the same fungus that gave us penicillin) into the partially ripened cheese. This fungus needs oxygen to make the blue pigment, so holes have to be made in the cheese – the more holes, the faster the blue veins develop.

The role of the rennin in young mammals is to clot the mother’s milk in baby’s stomach. This then ‘tricks’ the stomach into keeping the contents there for several hours, thus allowing protein digestion and the mother to get some (much-needed) rest! In most mammals the rennin is only made until the animal is weaned, but in Caucasian people, milk was (historically) drunk throughout life and so the enzyme continues to be made, even in adults. Also made is the enzyme lactase, which breaks down the milk sugar and stops the bacteria from fermenting it in the colon, with subsequent large volumes of gas produced and embarrassing side–effects!
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Pectinases

Reply 2

Stranded

Hello,

Well I have got some info pertaining to proteases right here:
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Protease is responsible for digesting proteins in your food, which is probably one of the most difficult substances to metabolize. Because of this, protease is considered to be one of the most important enzymes that we have. If the digestive process is incomplete, undigested protein can wind up in your circulatory system, as well as in other parts of your body.

When you take protease in higher quantities, it can help to clean up your body by removing the unwanted protein from your circulatory system. This will help to clean up your blood stream, and restore your energy and balance.

One of the tricks of an invading organism is to wrap itself in a large protein shell that the body would view as being "normal". Large amounts of protease can help to remove this protein shell, and allow the body's defense mechanisms can go into action. With the protective barrier down, your immune system can step in and destroy the invading organism.

Additional amounts of protease are also helpful in fighting such things as colds, flu's, and cancerous tumor growths. Protease helps in the healing and recovery from cancer by dissolving the fibrin coating on cancer cells, and thereby giving your immune system a chance to do its job. It can effectively shrink these tumors by helping to remove the dead and abnormal tissues, and by stimulating healthy tissue growth.

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.
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I have this booklet on acrobat for pectinases...if you want it, PM me ur email add & I'll send it to you...If you wish to do so that is :smile: