These enzymes are generally added to the dough of bread in order to degrade the starch into smaller dextrins, which are further fermented by the yeast. Amylases are utilized for desizing process in textile industry. Sizing agents like starch are added to yarn before fabric production for fast and secure weaving process.
Starch is a very attractive size, because it is cheap, easily available all over, and it can be easily removed. Desizing is the process where removal of starch from the fabric takes place and acts as the strengthening agent to prevent breaking of the warp thread during the weaving process. For a long time amylase from Bacillus strain was employed in textile industry. The coating treatment makes the surface of paper smooth and strong to improve the writing quality of the paper. Starch is considered to be the good sizing agent for the finishing of paper, improving the quality and reusability, besides being a good coating for the paper.
A higher than normal concentration of amylases may predict one of several medical conditions, including acute inflammation of the pancreas, perforated peptic ulcer, strangulation ileus, torsion of an ovarian cyst, macroamylasemia, and mumps. In other body fluids also amylase can be measured, including urine and peritoneal fluid.
It is an enzyme that catalyzes the breakdown or hydrolysis of fats [ 45 ]. Lipases are a subclass of the esterases. Lipases perform essential roles in the digestion, transport, and processing of dietary lipids e.
Genes encoding lipases are even present in certain viruses [ 46 ]. Most lipases act at a specific position on the glycerol backbone of lipid substrate especially in small intestine. For example, human pancreatic lipase as shown in Figure 4 , which is the main enzyme that breaks down dietary fats in the human digestive system, converts triglyceride substrates found in ingested oils to monoglycerides and two fatty acids.
Some lipases are expressed secreted by pathogenic organisms during the infection. In particular, Candida albicans has a large number of different lipases, possibly reflecting broad lipolytic activity, which may contribute to the persistence and virulence of C.
Lipases are considered as major group of biotechnologically valuable enzymes, mainly due to the versatility of their applied properties and easy mass production. Microbial lipases are largely diversified in their enzymatic properties and substrate specificity, which make them potential source for industrial applications.
The interest in this enzyme is primarily due to investigations of their role in pathogenesis and their wide application in biotechnology. Bacterial lipases are more stable than animal or plant lipases.
The energy expenditure required to conduct reactions at elevated temperatures and pressures is eliminated as lipases are active under ambient temperature, and it also reduces the denaturation of labile reactants and products.
Computer simulated 3D image of pancreatic lipase [ 48 ]. There are no such distinguished types of lipase, but mainly it is categorized according to its use, namely, human digestive system in human pancreatic lipase HPL and pancreatic lipase. Others include hepatic lipase HL , endothelial lipase, and lipoprotein lipase. Lipases are involved in diverse biological processes ranging from routine metabolism of dietary triglycerides to cell signaling and inflammation [ 53 , 54 ].
Thus, some lipase activities are confined to specific compartments within cells, while others work in extracellular spaces. In the example of lysosomal lipase, the enzyme is confined within an organelle called the lysosome.
Other lipase enzymes, such as pancreatic lipases, are secreted into extracellular spaces where they serve to process dietary lipids into more simple forms that can be more easily absorbed and transported throughout the body. Fungi and bacteria may secrete lipases to facilitate nutrient absorption from the external medium or in examples of pathogenic microbes to promote invasion of a new host.
As biological membranes are integral to living cells and are largely composed of phospholipids, lipases play important roles in cell biology. Malassezia globosa , a fungus that is thought to be the cause of human dandruff, uses lipase to break down sebum into oleic acid and increase skin cell production, causing dandruff. Lipases serve important roles in human practices as ancient as yogurt and cheese fermentation. However, lipases are also being exploited as cheap and versatile catalysts to degrade lipids in more modern applications.
For instance, a biotechnology company has brought recombinant lipase enzymes to market for use in applications such as baking, laundry detergents, and even as biocatalysts [ 55 ] in alternative energy strategies to convert vegetable oil into fuel [ 56 ].
High enzyme activity lipase can replace traditional catalyst in processing biodiesel; this enzyme is more environmental and safe. Some of the lipase-producing bacterial genera include Bacillus , Pseudomonas, and Burkholderia. The commercially important bacterial lipases are usually extracellular, and also their bulk production is much easier. There are a number of lipase-producing bacteria, but only a few are commercially exploited as wild or recombinant strains [ 57 ].
Of these, the important ones are Achromobacter , Alcaligenes , Arthrobacter , Bacillus , Burkholderia , Chromobacterium , Enterococcus , Corynebacterium, and Pseudomonas. In a variety of biotechnological applications lipases from Pseudomonas are widely used [ 58 , 59 ].
Various products based on bacterial lipases have been launched in the market in the past few years, such as Lumafast and Lipomax from Pseudomonas with their major application in detergent enzymes, while Chiro CLEC-PC, Chirazyme L-1, and Amano P, P and PS have numerous applications in organic synthesis.
Fungi capable of synthesizing lipases are found in several habitats, including soils contaminated with wastes of vegetable oils, dairy byproduct, seeds, and deteriorated food [ 60 , 61 ]. Candida rugosa lipases have been known for their diverse biotechnological potential [ 62 ]. The presence of C. Rhizopus oryzae lipase, Rhizopus delemar lipase and Rhizopus javanicus lipase have a substitution in the His and the Leu was referred by Minning et al.
The LIP2 lipase from the Yarrowia lipolytica YLLIP2 have a high potential for enzyme replacement therapy due to its unique biochemical properties: It shows highest activity at low pH values and is not repressed by bile salts.
It was also reported that Thermomyces lanuginosus lipase has variety of applications in the field of detergents and biotechnological processes and it was also reported that YLLIP2 belongs to same family [ 65 ]. The extracellular thermostable lipase is produced by thermophilic Mucor pusillus , Rhizopus homothallicus , and Aspergillus terreu s. Mucor sp. There are few reports that have been made so far with molds with alkaliphilic and thermostable lipase [ 67 , 68 ].
In the textile industry lipases are used for the removal of size lubricants, which increases fabrics absorbance ability for improved levelness in dyeing. In the denim abrasion systems, it is used to lessen the frequency of cracks and streaks. Commercial preparations used for the desizing of denim and other cotton fabrics contain both alpha amylases, and lipase enzymes are used for the desizing of cotton fabrics and denim during its commercial preparation [ 69 ].
The hydrolytic lipases are commercially very important, and their addition to detergents is mainly used in laundries and household dishwashers.
Enzymes reduce the environmental load of detergent products, as they save energy by enabling a lower wash temperature to be used, and use of chemicals in detergents is reduced, mostly biodegradable, leaving no harmful residues has no negative impact on sewage treatment processes; and does not possess any kind of risk to aquatic life [ 70 ].
To modify the food flavour by synthesis of esters of short-chain fatty acids and alcohols flavour and fragrance lipases have been frequently used. Lipases play a major role in the fermentative steps during manufacturing of sausage and also to measure changes in long-chain fatty acid liberated during ripening.
Previously, lipases of different microbial sources were used for refining rice flavour, modifying soybean milk, and for enhancing the aroma and speed up the fermentation of apple wine [ 71 ]. By adding lipases the fat is removed while processing meat and fish, and this process is called biolipolysis. Lipases are considered as important drug targets or marker enzymes in the medical field.
The presence or high levels of lipases can indicate certain infection or disease and can be used as diagnostic tool. They are used in the determination of serum triglycerides to liberate glycerol which is determined by enzyme-linked colorimetric reactions.
Acute pancreatitis and pancreatic injury can be determined by the level of lipases in blood [ 72 ]. Few new developments have been made by using lipases for the diagnosis of pancreatitis.
The development of a test for measurement of canine pancreatic lipase has been developed using pancreatic lipases as they are fixed markers for the pancreas. A serum feline pancreatic lipase immunoreactivity fPLI test was currently developed, and findings suggest that this test is more accurate than other diagnostic tools used for the diagnosis of feline pancreatitis [ 73 ].
The nontypable strains clearly show the most frequent group with elevated level of lipase, proteinase, elastase, hydrophobicity, and motility [ 74 ]. This preliminary research may be considered as part of global unselected screening of biological and other samples for detecting new promising sources of drugs [ 75 ]. Lipases can be used as digestive aids. Lipases can be used in the treatment of malignant tumors as they are the activators of tumor necrosis factor. Human gastric lipase HGL is the most stable acid lipase and considered to be a good tool for enzyme substitution therapy.
Earlier lipases have been used in the treatment of gastrointestinal disturbances, dyspepsias, cutaneous manifestations of digestive allergies, and so forth. Lipase from Candida rugosa synthesizes lovastatin, a drug that lowers serum cholesterol level. The asymmetric hydrolysis of 3-phenylglycidic acid ester which is a key intermediate in the synthesis of diltiazem hydrochloride is a widely used coronary vasodilator and is synthesized using S.
Retinoids vitamin A and derivatives are commercially very important in cosmetics and pharmaceuticals such as skin care products. Immobilized lipases are used for the preparation of water-soluble retinol derivatives. Lipases are used in hair waving preparation and have also been used as an ingredients of topical antiobese creams or as oral administration [ 77 ].
The enzyme-catalysed dissolution of biodegradable polymer films based on biosensor has been developed. The polymer enzyme system. Within the last few years, different processes have been designed using enzyme-labelled probes in order to avoid unstable and harmful isotopes.
While screening various hydrolytic enzymes to fulfil the special demands, fungal lipases turned out to be the most relevant one. Margesin et al. In the coastal environment fungal strains are used to degrade oil spills, which in turn increase ecorestoration and enzymatic oil processing in industries. Lipase produced by Bacillus subtilis, Bacillus licheniformis, Bacillus amyloliquefaciens, Serratia marcescens, Pseudomonas aeruginosa, and Staphylococcus aureus was reported to degrade palm oil mill, diary, slaughter house, soap industry, and domestic waste water [ 80 ].
Pseudomonas aeruginosa lipases were recommended for castor oil degradation [ 81 ]. Therapeutic enzymes have a wide variety of specific uses such as oncolytics, thrombolytics, or anticoagulants and as replacements for metabolic deficiencies. Proteolytic enzymes serve as good anti-inflammatory agents. The list of enzymes which have the potential to become important therapeutic agents and its microbial sources are shown in Table 3 and Table 4 respectively.
A number of factors severely decrease the potential utility of microbial enzymes once we enter the medical field due to large molecular size of biological catalyst which prevents their distribution within somatic cells, and another reason is the response of immune system of the host cell after injecting the foreign enzyme protein.
As compared to the industrial use of enzymes, therapeutically useful enzymes are required in relatively less amounts, but the degree of purity and specificity should be generally high.
The sources of such enzymes should be selected with great care to prevent any possibility of undesirable contamination by incompatible material and also to enable ready purification. Therapeutic enzymes are usually marketed as lyophilised pure preparations with biocompatible buffering salts and mannitol diluent. The cost of these enzymes is high but comparable to those of therapeutic agents or treatments.
As an example, urokinase is derived from human urine and used to dissolve blood clots. One of the major applications of therapeutic enzymes is in the treatment of cancer and various other diseases as shown in the Figure 5.
For the treatment of acute lymphocytic leukaemia asparaginase enzyme has proved to be promising. Its activity depends upon the fact that tumour cells lack aspartate-ammonia ligase activity, which stops the synthesise of nonessential amino acid L-asparagine. Hence, they are extracted from body fluids. The asparaginase does not affect the normal cells which are capable of synthesizing enough for their own requirements, but they decrease the free exogenous concentration, so it causes a state of fatal starvation in the susceptible tumour cells.
The enzyme can be administered intravenously and is only effective in reducing asparagine levels within the bloodstream, showing a half-life of about a day in a dog. This half-life can be increased by fold with use of polyethylene glycol-modified asparaginase.
Application of therapeutic enzymes in different disorders and diseases [ 49 — 52 ]. A large number of proteolytic enzymes of plant and bacterial origin have been studied for the removal of dead skin of burns. Various enzymes of higher quality and purity are now in clinical trials. Debrase gel dressing, containing a mixture of several enzymes extracted from pineapple, received clearance in from the US FDA for a Phase II clinical trial for the treatment of partial-thickness and full-thickness burns.
A proteolytic enzyme VibrilaseTM obtained from Vibrio proteolyticus is found to be effective against denatured proteins such as those found in burned skin. The regeneration of injured spinal cord have been demonstrated using chondroitinases, where this enzyme acts by removing the glial scar and thereby accumulating chondroitin sulfate that stops axon growth [ 99 ].
Hyaluronidase has also been found to be a similar hydrolytic activity on chondroitin sulphate and may help in the regeneration of damaged nerve tissue [ ]. Lysozyme is a naturally occurring antibacterial agent and used in many foods and consumer products, as it is able to breakdown carbohydrate chains in bacterial cell wall. Chitinases is another naturally occurring antimicrobial agent. The cell wall of various pathogenic organisms, including fungi, protozoa, and helminths is made up of chitin and is a good target for antimicrobials [ ].
The lytic enzyme derived from bacteriophage is used to target the cell walls of Streptococcus pneumonia , Bacillus anthracis, and Clostridium perfringens [ ]. The application of lytic bacteriophages can be used for the treatment of several infections and could be useful against new drug-resistant bacterial strains. The cancer research has some good instances of the use of enzyme therapeutics.
Recent studies have proved that arginine-degrading enzyme PEGylated arginine deaminase can inhibit human melanoma and hepatocellular carcinomas [ ]. Currently, another PEGylated enzyme, Oncaspar1 pegaspargase , has shown good results for the treatment of children newly diagnosed with acute lymphoblastic leukemia and are already in use in the clinic.
The normal cells are able to synthesize asparagine but the cancerous cells cannot and thus, die in the presence of asparagine degrading enzyme.
Asparaginase and PEG-asparaginase are effective adjuncts for standard chemotherapy. Another important feature of oncogenesis is proliferation. It has been proved that the removal of chondroitin sulfate proteoglycans by chondroitinase AC and, to a lesser extent, by chondroitinase B, stops tumor growth, metastasis, and neovascularization [ ].
The further application of enzymes as therapeutic agents in cancer is described by antibody-directed enzyme prodrug therapy ADEPT. A monoclonal antibody carries an enzyme specific to cancer cells where the enzyme activates a prodrug and destroys cancer cells but not normal cells.
This approach is being utilized for the discovery and development of cancer therapeutics based on tumor-targeted enzymes that activate prodrugs. The targeted enzyme prodrug therapy TEPT platform, involving enzymes with antibody-like targeting domains, will also be used in this effort [ ].
Enzymes are one of the most important biomolecules which has a wide range of applications in industrial as well as biomedical field as describe in Table 5. Today it is one of the most important molecules which are widely used since the ancient human civilization.
With the growing population and raising need enzymes seem to be one of the most vital molecules that have a great impact in every sector that may be dairy, industrial, agriculture, or medicine.
Previously in the 19th up till midth century, the world has seen great industrial expansions which we all know as industrial revolution which has created a steep raise in population and its demand for survival thus creating a great impact in the agricultural, industrial, dairy, and medicinal fields. To meet the raising demand, many scientists had put their great effort to develop many chemical processes to meet the demand, but in later years, the harmful effects of using chemical catalysts to fast up the process have come in front of the mankind.
Many chemical transformation processes used in various industries have inherent drawbacks from a commercial and environmental point of view. Nonspecific reactions may result in poor product yields. Harsh and hazardous processes involving high temperatures, pressures, acidity, or alkalinity need high capital investment and specially designed equipment and control systems.
Unwanted by-products may prove difficult or very costly to produce. High chemicals and energy consumption as well as harmful by-products have a negative impact on the environment. In a number of cases, some or all of these drawbacks can be virtually eliminated by using enzymes.
Interestingly enzyme reactions may often be carried out under mild conditions; they are highly specific and involve high reaction rates. Industrial enzymes originate from biological systems which can effectively contribute to sustainable development through being isolated from microorganisms which are fermented using primarily renewable resources. In addition, as only small amounts of enzymes are needed in order to carry out chemical reactions even on an industrial scale, both solid and liquid enzyme preparations take up very little storage space.
Mild operating conditions enable uncomplicated and widely available equipment to be used, and enzyme reactions are generally easily controlled. Enzymes also reduce the impact of manufacturing on the environment by reducing the consumption of chemicals, water, and energy and the subsequent generation of waste.
Developments in genetic and protein engineering have led to improvements in the stability, economy, specificity, and overall application potential of industrial enzymes. When all the benefits of using enzymes are taken into consideration, it is not surprising that the number of commercial applications of enzymes is increasing every year.
Biotechnology offers an increasing potential for the production of goods to meet various human needs. Enzyme technology are a subfield of biotechnology where new processes had been developed and are still developing to manufacture both bulk and high added value products utilizing enzymes as biocatalysts, in order to meet needs such as food e.
Enzymes are also used to provide services, as in washing and environmental processes especially clean-up processes or for analytical and diagnostic purposes. The driving force in the development of enzyme technology, both in academic research and industry, has been and will continue to the development of new and better products, processes, and services to meet these needs along with the improvement of the processes to produce existing products from new raw materials as biomass.
The goal of these approaches is to design innovative products and processes that are not only competitive but also meet criteria of sustainability and economic viability. The concept of sustainability was introduced in the World Commission on Environment and Development WCED, with the aim to promote the necessary development that meets the needs of the present and future demand without compromising the ability of future generations to meet their own needs.
To determine the sustainability of a process, criteria that evaluate its economic, environmental and social impact must be used [ — ]. A positive effect in all these three fields is required for a sustainable process. Criteria for the quantitative evaluation of the economic and environmental impact are in contrast with the criteria for the social impact, easy to formulate. In order to be economically and environmentally more sustainable than the existing processes, a new process must be designed to reduce not only the consumption of resources e.
Because enzymes are highly specific in the reactions they catalyse, an abundant supply of enzymes must be present in cells to carry out all the different chemical transformations required. Most enzymes help break down large molecules into smaller ones and release energy from their substrates. To date, scientists have identified over 10, different enzymes. Because there are so many, a logical method of nomenclature has been developed to ensure that each one can be clearly defined and identified.
Thus, from this table we can get a clear idea that the use of enzymes and bioengineering of them is nowadays very much practised in almost every industry. These biomolecules which are also known as biocatalyst too are now playing a very major role in the modern industrial development that is mainly aimed in economical, high efficiency, and ecofriendly production of different products and by-products.
Enzymes are now an important area of studies of different human diseases. Like other proteins, enzymes are produced inside cells by ribosomes, which link up amino acids into chains. Although the majority of industrial enzymes are produced by microorganisms, the enzymes are formed in exactly the same way as in human cells.
The structure and properties of the enzymes produced by a particular cell are determined by the genetic instructions encoded in the deoxyribonucleic acid DNA found in chromosomes of the cell. DNA enables the production of specific enzymes through a code consisting of four bases: adenine A , guanine G , cytosine C , and thymine T.
DNA's characteristic double helix consists of two complementary strands of these bases held together by hydrogen bonds. A always pairs with T, while C always pairs with G. The order in which these bases are assembled in the DNA double helix determines the sequence of amino acids in the enzyme protein molecule. Each fully functional segment of DNA—or gene—determines the structure of a particular protein, with each of the 20 different amino acids being specified by a particular set of three bases.
These products will be useful as chemicals, pharmaceuticals, fuel, food, or agricultural additives. Since the tight control of enzyme activity is essential for homeostasis, any malfunction mutation, overproduction, underproduction, or deletion of a single critical enzyme can lead to a genetic disease. The importance of enzymes is shown by the fact that a lethal illness can be caused by the malfunction of just one type of enzyme out of the thousands of types present in our bodies.
For example, the most common type of enzyme deficiency disorder is phenylketonuria, and a mutation of a single amino acid in the enzyme phenylalanine hydroxylase which catalyzes the amino acid phenylalanine results in buildup of phenylalanine and related products.
This can lead to mental retardation if the disease is untreated in early childhood [ ]. Another example of enzyme deficiency is germline mutations in genes coding for DNA repair enzymes which cause hereditary cancer syndromes such as xeroderma pigmentosum [ ]. Defects in these enzymes cause cancer since the body is less able to repair mutations in the genome. This causes a slow accumulation of mutations and results in the development of many types of cancer in the sufferer. Some enzymes are produced in increasing amounts for therapeutic purposes; this applies especially to recombinant enzymes such as factor VIII, tPA, and urokinase that cannot be produced in sufficient amounts from natural sources blood serum or urine.
Another advantage of the recombinant production of these enzymes is that possible contamination with pathogenic human viruses HIV, herpes can be avoided. Enzymes are now orally administrated to treat several diseases e. Since enzymes are proteins themselves, they are potentially subject to inactivation and digestion in the gastrointestinal environment. Therefore a noninvasive imaging assay had been developed to monitor gastrointestinal activity of exogenous enzymes like prolyl endopeptidase as potential adjuvant therapy for celiac disease [ ].
Proteins are abundant in nature. Many proteins can cause allergies like pollen, house dust mites, animal dander, and baking flour. Like many other proteins foreign to the human body, enzymes are potential inhalation allergens. The inhalation of even small amounts of foreign protein in the form of dust or aerosols can stimulate the body's immune system to produce specific antibodies.
In some individuals, the presence of these specific antibodies can trigger the release of histamine when reexposed to the allergen. This compound can cause symptoms well known to hay fever sufferers such as watery eyes, a runny nose, and a sore throat.
When exposure ceases, these symptoms also cease. Enzymes must be inhaled for there to be a risk of causing sensitization that may lead to an allergic reaction. It may be necessary to monitor the working environment in facilities where enzymes are used, especially if large quantities are handled on a daily basis. Monitoring is used to confirm that threshold limit values TLVs for airborne enzymes are not being exceeded. In many countries, the TLVs for enzymes are based on the proteolytic enzyme subtilisin and are stated as 0.
But one industry that has come a long way in the safe handling of enzymes is the detergent industry. The use of encapsulated enzymes, combined with improved industrial hygiene and operating practices, has brought levels of airborne enzyme dust down dramatically in developed countries since the occupational problem of enzyme allergies first came to light in the late s. The trade association AISE has generated a guide to safe handling of enzymes in the detergent industry [ ].
It should be emphasized that allergy to enzymes is solely an occupational hazard, and no effects on end consumers using products containing enzymes have ever been reported during more than 35 years of use. In one of the most important reports on the subjects, the National Research Council NRC , USA, concluded that consumers of enzymatic laundry products did not develop respiratory allergies [ ]. Further studies of enzyme allergy over the years have confirmed that enzymatic laundry and dishwashing detergents are safe for consumers to use.
The HERA Risk Assessment document gives a comprehensive overview of consumer safety in regards to enzyme application within the household cleaning sector. The safe use of enzymes in food processing has been documented in a recent study by Novozymes and the University Hospital of Odense, Denmark [ ].
The application of enzymes in food processing is governed by food laws. Within the EU, large parts of the food laws of individual member states have been harmonized by directives and regulations. AMFEP members ensure that the enzymes used in food processing are obtained from nonpathogenic and nontoxigenic microorganisms, that is, microorganisms that have clean safety records without reported cases of pathogenicity or toxicosis attributed to the species in question.
When the production strain contains recombinant DNA, the characteristics and safety record of each of the donor organisms contributing genetic information to the production strain are assessed. The majority of food enzymes are used as processing aids and have no function in the final food. In this case, they do not need to be declared on the label because they are not present in the final food in any significant quantity. A few enzymes are used both as processing aids and as food additives.
When used as additives, they must be declared on the food label. Good Manufacturing Practice is used for industrial enzymes for the food industry. The key issues in GMP are microbial control of the microorganism selected for enzyme production, the control and monitoring systems ensuring pure cultures and optimum conditions for enzyme yield during fermentation, and the maintenance of hygienic conditions throughout the recovery and finishing stages.
Commercial enzyme products are usually formulated in aqueous solutions and sold as liquids or processed into nondusting, dry products known as granulates or microgranulates. Both liquid and dry preparations must be formulated with the final application in mind. It is important for both the producer and customer to take into account storage stability requirements such as stability of enzyme activity, microbial stability, physical stability, and the formulation of the enzyme product itself.
Enzyme molecules are far too complex to synthesize by purely chemical means, with a very instability of its pure form, and so the only way of making them is to use living organisms. The problem is that the useful enzymes produced by microorganisms in the wild are often expressed in tiny amounts and mixed up with many other enzymes. These microorganisms can also be very difficult to cultivate under industrial conditions, and they may create undesirable by-products.
Even there is a possibility of cross-contamination and production of toxins which may be lethal if used. Genetic engineering is a far more efficient option because the changes are completely controlled. This process basically involves taking the relevant gene from the microorganism that naturally produces a particular enzyme donor and inserting it into another microorganism that will produce the enzyme more efficiently host. The first step is to cleave the DNA of the donor cell into fragments using restriction enzymes.
The DNA fragments with the code for the desired enzyme are then placed, with the help of ligases, in a natural vector called a plasmid that can be transferred to the host bacterium or fungus.
The DNA added to the host in this way will then divide as the cell divides, leading to a growing colony of cloned cells each containing exact replicas of the gene coding for the enzyme in question. Since the catalytic properties of any enzyme are determined by its three-dimensional structure, which in turn is determined by the linear combination of the constituent amino acids, we can also alter an enzyme's properties by replacing individual amino acids.
For example, detergent enzymes can be made more bleach-stable using this type of protein engineering. Bleach-stable protein engineered enzymes have been on the market for a number of years, for example, Novozymes' Everlase. Furthermore, enzymes can be given other useful properties using this technique, for example, improved heat stability, higher activity at low temperatures, and reduced dependency on cofactors such as calcium.
New and exciting enzyme applications are likely to bring benefits in other areas like less harm to the environment, greater efficiency, lower cost, lower energy consumption, and the enhancement of a product properties.
New enzyme molecules capable of achieving this will no doubt be developed through protein engineering and recombinant DNA techniques. Industrial biotechnology has an important role to play in the way modern foods are processed.
New ingredients and alternative solutions to current chemical processes will be the challenge for the enzyme industry. When compared with chemical reactions, the more specific and cleaner technologies made possible by enzyme-catalyzed processes will promote the continued trend towards natural processes in the production of food.
Enzymes are being known to mankind since the ancient human civilization. The use of enzymes had been done intensively in different fields especially, in ancient brewing and other uses. But since the 18th century it has been technically known to us as enzymes. Many scientists had tried to study the use of enzymes, and from their pioneer work, we have come to know about its power and utility in our daily life. Today different types of enzymes are being manufactured by many big companies and being sold for their important role in different industries like food, dairy, detergent, and chemical as well as for their important lifesaving therapeutically application.
Due to advancement of modern biotechnology and protein engineering a new area of enzyme engineering, has evolved which mainly deals with the purification and stability of these important enzymes. Different microbes as well as other model systems are extensively used for the production of these important biomolecules. Since then many microorganisms and their enzymes with unique function have also been discovered by means of extensive screening, and now they are commonly used in different industrial and medical fields.
Development of these medically important enzymes has been at least as extensive as those for industrial applications thus reflecting the magnitude of the potential rewards of this sector in the near. Enzymes industry is one among the major industries of the world, and there exists a great market for further improvement in this field. Amylase and lipase are few of these mentionable enzymes that have a wide spectrum role in this sector.
Its use is almost done in every industry whether it may be detergent, dairy, food, or medicineThis review especially emphasizes the important wide spectrum role of amylase and lipase in various sectors of industries and also discussed the role of other enzymes in therapeutic field.
There is an indeed need of future research in these biomolecules which will later be beneficial for the mankind in their relevance. National Center for Biotechnology Information , U. Journal List Biomed Res Int v. Biomed Res Int. Published online Sep Author information Article notes Copyright and License information Disclaimer. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
This article has been cited by other articles in PMC. Abstract Enzymes are the large biomolecules that are required for the numerous chemical interconversions that sustain life.
Introduction Enzymes are the biological substance or biological macromolecules that are produced by a living organism which acts as a catalyst to bring about a specific biochemical reaction. Enzymes, Classification, and Their Use Enzymes are large biological molecules responsible for all those important chemical interconversions that are required to sustain life [ 10 ].
Table 1 Enzyme classes and types of reactions [ 14 ]. Enzyme commission number Class of enzyme Reaction profile EC 1 Oxidoreductases Oxidation reactions involve the transfer of electrons from one molecule to another.
In biological systems we usually see the removal of hydrogen from the substrate. Typical enzymes in this class are called dehydrogenases. If A is oxygen, the relevant enzymes are called oxidases or laccases; if A is hydrogen peroxide, the relevant enzymes are called peroxidases.
EC 2 Transferases This class of enzymes catalyzes the transfer of groups of atoms from one molecule to another. Aminotransferases or transaminases promote the transfer of an amino group from an amino acid to an alpha-oxoacid. EC 3 Hydrolases Hydrolases catalyze hydrolysis, the cleavage of substrates by water.
The reactions include the cleavage of peptide bonds in proteins, glycosidic bonds in carbohydrates, and ester bonds in lipids. In general, larger molecules are broken down to smaller fragments by hydrolases. EC 4 Lyases Lyases catalyze the addition of groups to double bonds or the formation of double bonds through the removal of groups.
Thus bonds are cleaved using a principle different from hydrolysis. Pectate lyases, for example, split the glycosidic linkages by beta-elimination. EC 5 Isomerases Isomerases catalyze the transfer of groups from one position to another in the same molecule. In other words, these enzymes change the structure of a substrate by rearranging its atoms. EC 6 Ligases Ligases join molecules together with covalent bonds. These enzymes participate in biosynthetic reactions where new groups of bonds are formed.
Such reactions require the input of energy in the form of cofactors such as ATP. Open in a separate window. Table 2 A selection of enzymes used in industrial processes. Sl no. Application of Enzyme 3. Amylase Amylase is an enzyme that catalyses the breakdown of starch into sugars. Figure 1. Figure 2. Figure 3.
Use They are used in food, pharmaceutical, drug delivery, and chemical industries, as well as agriculture and environmental engineering. Application of Amylase Amylases have a wide range of application in various industries such as in the food, bread making, paper industries, textiles, sweeteners, glucose and fructose syrups, fruit juices, detergents, fuel ethanol from starches, alcoholic beverages, digestive aid, and spot remover in dry cleaning.
Use in Starch Industry The starch industry has the most widespread applications of amylases, which are used during starch hydrolysis in the starch liquefaction process that converts starch into fructose and glucose syrups [ 40 ].
Use in Detergent Industry Both in terms of volume and value detergent industry are the primary consumers of enzymes. Use in Food Industry There is an extensive use of amylase in processed food industry such as baking, brewing, production of cakes, preparation of digestive aids, fruit juices, and starch syrups.
Use in Textile Industry Amylases are utilized for desizing process in textile industry. Use in Medicine A higher than normal concentration of amylases may predict one of several medical conditions, including acute inflammation of the pancreas, perforated peptic ulcer, strangulation ileus, torsion of an ovarian cyst, macroamylasemia, and mumps. Lipase It is an enzyme that catalyzes the breakdown or hydrolysis of fats [ 45 ].
Figure 4. Types There are no such distinguished types of lipase, but mainly it is categorized according to its use, namely, human digestive system in human pancreatic lipase HPL and pancreatic lipase. Application of Lipase Lipases are involved in diverse biological processes ranging from routine metabolism of dietary triglycerides to cell signaling and inflammation [ 53 , 54 ]. Bacterial Lipase Some of the lipase-producing bacterial genera include Bacillus , Pseudomonas, and Burkholderia. Fungal Lipase Fungi capable of synthesizing lipases are found in several habitats, including soils contaminated with wastes of vegetable oils, dairy byproduct, seeds, and deteriorated food [ 60 , 61 ].
Use in Textile Industry In the textile industry lipases are used for the removal of size lubricants, which increases fabrics absorbance ability for improved levelness in dyeing. Use in Detergent Industry The hydrolytic lipases are commercially very important, and their addition to detergents is mainly used in laundries and household dishwashers.
Use in Food Industry To modify the food flavour by synthesis of esters of short-chain fatty acids and alcohols flavour and fragrance lipases have been frequently used. Use in Diagnosis Lipases are considered as important drug targets or marker enzymes in the medical field.
Use in Cosmetics Retinoids vitamin A and derivatives are commercially very important in cosmetics and pharmaceuticals such as skin care products. Use as Biosensor The enzyme-catalysed dissolution of biodegradable polymer films based on biosensor has been developed. Use in Biodegradation Margesin et al. General Therapeutic Application of Other Enzymes Therapeutic enzymes have a wide variety of specific uses such as oncolytics, thrombolytics, or anticoagulants and as replacements for metabolic deficiencies.
Table 3 Some important enzymes and their therapeutic importance. Table 4 List of some common enzymes found from different species. Figure 5. Treatment of Damaged Tissue A large number of proteolytic enzymes of plant and bacterial origin have been studied for the removal of dead skin of burns. Treatment of Infectious Diseases Lysozyme is a naturally occurring antibacterial agent and used in many foods and consumer products, as it is able to breakdown carbohydrate chains in bacterial cell wall.
Treatment of Cancer The cancer research has some good instances of the use of enzyme therapeutics. Modern Application of Enzyme: A Biotechnology View Enzymes are one of the most important biomolecules which has a wide range of applications in industrial as well as biomedical field as describe in Table 5.
Table 5 A broad spectrum idea about using the application of enzymes in different areas. Also for degrading complex proteins into sugars thus to increase the fermentation efficiency. Conclusion Enzymes are being known to mankind since the ancient human civilization. Development of these medically important enzymes has been at least as extensive as those for industrial applications thus reflecting the magnitude of the potential rewards of this sector in the near future.
References 1. Ungeformter Fermente. Verhandlungen des Heidelb. Vereins, Neue Folge. Vallery R, Devonshire RL. Life of Pasteur. Asimov I. Asimov's Biographical Encyclopedia of Science and Technology. Payen A, Persoz JF. Memoir on diastase, the principal products of its reactions, and their applications to the industrial arts. Annales de Chimie et de Physique. Ullmann A.
Pasteur-Koch: distinctive ways of thinking about infectious diseases. Wang JL, Liu P. Comparison of citric acid production by Aspergillus niger immobilized in gels and cryogels of polyacrylamide.
Journal of Industrial Microbiology. Bennett TP, Frieden E. Modern Topics in Biochemistry. Macmillan; Production of microbial enzymes and their applgications. Applied Microbiology. Smith AL. Oxford Dictionary of Biochemistry and Molecular Biology. Oxford University Press; Bairoch A. Nucleic Acids Research. Fischer E. Einfluss der configuration auf die wirkung der enzyme. Berichte der Deutschen Chemischen Gesellschaft. Webb EC. Sumner of Cornell University. Sumner was able to isolate and crystallize the enzyme urease from the jack bean.
His work was to earn him the Nobel Prize. John H. Northrop and Wendell M. They discovered a complex procedure for isolating pepsin. This precipitation technique devised by Northrop and Stanley has been used to crystallize several enzymes. PDF version of Introduction to Enzymes. Introduction to Enzymes Video. Place Order.
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