The Nomenclature, Uses, and Discovery of Enzymes - Literature review Example

Name : xxxxxxxxxxx Institution : xxxxxxxxxxx Title : xxxxxxxxxxx Tutor : xxxxxxxxxxx Course : xxxxxxxxxxx @2012 Introduction Enzymes are very essential in industrial processes. They normally work as catalyst for particular chemical reactions. A set of reactants such as substrates are usually converted into specific product by enzyme (Klauss, 2005). Enzymes are highly employed in several latest applications within the food, paper, agriculture and texture industries, thus causing the cost to go down. Similarly, enhanced technological developments are of late encouraging the pharmacy and chemistry industries to consider enzyme technology, a trend powered by concerns relating to health, raw materials, energy and the environment. Enzymes productions do always occur in huge quantities, measured in thousands of kilograms. The market value for industrial enzyme products is still increasing very fast (Gary, 2002). According to Chaplin (1990), strong catalysts from biology sources were discovered in nineteenth century. However, it is essential to note that, in around 400 B.C, biocatalysts were also employed in ancient manufacturing and preservation of food and alcoholic drinks. Several essential advantages can be associated with production of industrial enzyme (Klauss, 2005). The most pronounced advantage is that, enzymes do always catalyze reactions of narrow variations of reactants that may include some groups of closely related compounds, a group of compounds or a compound. It is believed that enzyme technology has made greater impact on society and is the main theme around which many biotechnological sciences revolve. This paper therefore seeks to evaluate the nomenclature, uses and discovery of enzymes. The paper will then explain technology engineering, industry and markets for enzymes. Finally,it will elaborate the evolution of enzyme technologies from initial discovery to date. Nomenclature, uses and discovery of enzymes Enzymes refer to biological catalysts that enhance the rate of reaction or that enable the reaction to take place. As catalysts, enzymes enhance invisible reactions, without experiencing any change in their structure. Enzymes mediate the synthetic and degradative reactions that take place within the body of living organisms. They are more efficient than conventional chemical catalysts, thus making it possible to be highly employed in today’s modern technological world, as an essential part of biotechnological advancement. Chaplin (1990) argues that all enzymes have protein backbone. Some enzymes do have protein as the only component in their structure. However, additional non-protein moieties do always prevail that may or may not involve in enzyme’s catalytic activity. Covalently linked carbohydrates groups are structural features that are normally encountered, which, in most cases, lack direct bearing on catalytic activity, though they have the ability of affecting stability and solubility of enzymes. Other factors that are always found in enzyme include metal ions or cofactors and coenzymes or organic molecule of low molecular weight. These factors, in some cases, can be tightly or loosely bound by covalent forces or non-covalent forces. They are believed to be essential constituents that contribute to enzymes’ activity and stability. By considering the type of reaction they catalyze, enzymes can be categorized into six groups. The three commonly known groups include oxidoreductaes, transferases, hydrolases. Oxidoreductases entail redox reactions within which oxygen or hydrogen electrons or atoms are transferred among molecules (Illanes, 2008). This group of enzyme entails dehydrogenases, oxygenases, oxidases and peroxidases. Transferases are group of enzymes that catalyze transfer of either an atom, or group of atoms, among two molecules. Hydrolases on the other hand entail hydrolytic reactions and their reversal. Of late, it is the most common group of enzymes in enzyme technology and incorporates asterases, lipases, proteases and glycosidases (Chaplin, 1990). Enzymes are highly employed in industries. They are produced in huge amounts and used for diagnostic or therapeutic reasons. Therapeutic, diagnosticand other compositions that are similar normally incorporate materials that are logically labile. Labile materials can include any huge variety of substances such as biological materials or pharmaceuticals. The stated biological materials include fats, sugars, hormones, oils, enzymes, cell components, blood and blood fractions. Therefore, as one of the biological materials enzymes are extremely labile and enjoy a broad variety of therapeutic and analytic uses (Bonderman, 1992). For example, enzymes are helpful in several diagnostic tests, such as in vitro determination of creatine, glucose and blood urea nitrogen (Herranz & Burke, 1993). In order to avoid problems that is associated with lability, preparation of enzymes are normally lyophilized or entrained within a solid matrix so as to display stability. For many years, there have been efforts to organize stabilized enzyme composition that is in liquid form so as toapply in diagnostic processes. Propanediol, an organic solvent, can be used to stabilize preparation of liquid enzyme. The composition normally consists of aqueous medium that contain lyophilized, dry enzyme and propanediol, an organic solvent. Bonderman (1992) argue that the organic solvent normally protects active group sites within the enzyme molecule. Enzymes discovery is not easy to determine historically. Its discovery is normally associated with Payen and persoz, who in the year 1833 treated aqueous extract of malt with ethanol and precipitated heat-labile substance that promotes starch’s hydrolysis. Payen and Persoz named their fraction diastase, which is a Greek word implying separation. Most of the ancient enzymology concentrated on fermentation, an essential aspect in today’s studies(Barglow, 2008). Majority of researchers have for along time concentrated on speeding up and maximizing their fermentation procedure so as to allow for huge ferments’ variety and faster product delivery. Throughout there study, there prevail a scientific controversy pertaining fermentation’s nature in microorganisms placed in juices so as to induce production of alcohol. Pasteur, who participated in various scientific controversies, viewed fermentation as an important part of microorganism’s lifecycle. The entire process of fermentation, such as transformation of sugar to alcohol, was hard to separate from living organism(Aehle, 2008). The renowned chemists, such as Liebig and Stahl, supported the chemical theory of fermentation. In 1860, a researcher, known as Berthelow, found an alcohol-precipitable fraction in yeast that converts sucrose into two monosaccharide components. Kuhne, in 1878, named the substance that undertakes the reaction as enzyme. Enzyme practically implied ‘’in years’’. Five years later, the suffix ‘’ase’’ was suggested to be used in naming enzymes. The controversy among chemical and lifecycle debates arise in 1897 when Edouard Buchner and Hans placed a side a cell-free juice that undertook complete sugar fermentation. Technology engineering, industry and markets for enzymes Enzymes are important aspects in life. These proteins do always function as catalysts for almost all the chemical reactions that explain cellular metabolism (Gary, 2002). Their huge level of accelerations and exacting selectivities make them more important outside the cell. Enzymes are highly employed in research, medicine and industry. Their properties are normally determined by their accurate three-dimensional structures (Hilvert, 2001). Biomacromolecules’ study, like current interesting scientific crisis, requires multidisciplinary observation. Enzyme engineering has a lot to attain from combination of immunology, genetics, chemistry and molecular biology. Several enzymes have been engineered by protein engineering approaches. The most common examples include the application of error-prone PCR, DNA shuffling, saturation mutagenesis, mutants of toluene 4-monooxygenase, toluene-4-monooxygenase and toluene-o-xylene monooxygenase (Dalby, 2007). B12-depedent dehydrates plus enhanced reaction kinetics has been discovered through the use of error-prone PCR and oligonucleotide-directed mutagenesis to aim DhaB1 gene that encodes α-subunit of glycerol dehydratase. These kinds of enzymes are essential in glycerol and 1, 3-propanediol generation. Nitrilases can be employed in biocatalytic procedures to transform nitriles into carboxylic acids. Of late, error-prone PCR has been employed to produce mutants of acidovorax facilis nitrilase. Several enzymes that were set aside were able to enhance activities in transforming 3-hydroxynitrile to 3-hydroxycarboxylic acid (Greenberg eat al, 2002). According to Liese & Seelbach (2006), industry and markets for enzymes are highly developing. It is believed that the market value of industrial enzyme commodity is intended to grow in future. The international market for industrial enzymes has been immune to current turmoil within the global economy. In 2008 and 2009, the global market for industrial enzymes grew moderately causing the demand for enzymes in developed economies to stabilize. The growth in industrial enzymes market is currently being steered by enhanced demand for several specialty polymerases, enzymes and nucleases. Enhanced acquisition of medical care facilities plus services in several developing nations and the need to attain general health care in few developed nations boost the demand for research and biotechnology enzymes(Nerker, 2004). However, the demand for enzymes that are normally employed in ethanol production can easily reduce in the future as many nations around the globe are increasingly re-evaluating the utilization of food-derived raw materials in ethanol manufacturing. Evolution of enzyme technologies from initial discovery to date Development of enzyme technology started in 1874, when Christian Hansen, a Danish chemist, generated a first ever specimen of rennet by removing dried calves’ stomachs with saline solution.Pandey (2006) argue that this was the first enzyme preparation of moderately high purity employed for industrial reasons. This essential activity was directed by lengthy evolution. Enzymes have for a long time been employed by human beings throughout the ages. They have been employed either in vegetables formrich in enzymes or in form of microorganisms employed for several reasons, for example in brewing procedures, in alcohol production and in baking. Since ancient times, enzymes were generally employed in cheese production. In 1950 and 1970, an integration of technical and scientific know how and the enhanced demand for enzymes for use in starch processing and washing procedure stimulated the development of enzyme technology. This therefore made several enzymes to be discovered, purified and characterized. In the 1960s, enzyme development gained pace in only modest proportions, as displayed by growing proteases and bacterial amylases sales. During this period, enzyme procedure, employed in producing dextrose, was highly utilized in starch formation. The establishment of gene technology in 1970s offered a steady drive for both developed and inexpensive biocatalysts. It also broadened the application’s scope. Similar to enzyme stability, productivity through recombinant microorganisms was seriously enhanced, thus resulting to great price reduction and development of enzyme applications economics. Of late, majority of enzymes are employed as biocatalysts within the enzyme processes (Bornscheuer eat al, 2005). Li and Beilen (2002) suggest that enzyme technology has joined a stage in which current technologies, an enhanced understanding of essential biology and bioinformatics are starting to build the discovery, purification, development and use of biocatalysts to greater margins. Conclusion From the discussion, it is clear that enzymes refer to biological catalysts that enhance the rate of reaction or that enable the reaction to take place. Enzymes do have protein backbone. Other factors that are always found in enzyme include metal ions or cofactors and coenzymes or organic molecule of low molecular weight. These factors, in some cases, can be tightly or loosely bound by covalent forces or non-covalent forces. They are believed to be essential constituents that contribute to enzymes’ activity and stability. Enzymes are highly employed in industries. They are produced in huge amounts and used for diagnostic or therapeutic reasons. Enzymes discovery is not easy to determine historically. Its discovery is normally associated with Payen and Persoz. Enzymes are important aspects in life. These proteins do always function as catalysts for almost all the chemical reactions that explain cellular metabolism. Their huge level of accelerations and exacting selectivities make them more important outside the cell. Enzymes are highly employed in research, medicine and industry. Enzyme engineering has a lot to attain from combination of immunology, genetics, chemistry and molecular biology. Industry and markets for enzymes are highly developing. It is believed that the market value of industrial enzyme commodity is intended to grow in future. The international market for industrial enzymes has been immune to current turmoil within the global economy. Development of enzyme technology started in 1874. Of late, majority of enzymes are employed as biocatalysts within the enzyme processes. References Aehle, W. 2008. Enzymes in Industry: Production and Applications. John Wiley & Sons Barglow, K, 2008, Enzyme Discovery and Characterization by Proteome Reactivity Profiling, New York: ProQuest. Bonderman, P. R, 1994, Diagnostic and therapeutic compositions, New York: Noblesville, Ind. Bornscheuer, T. U. eat al. 2005, Biocatalyst and enzyme technology. Introduction to enzyme technology.wiley-vchverlaggmbh& co. kgaa, weinheimisbn: 3-527-30497-5 Chaplin M. F,1990, Enzyme technology, Cambridge University press Gary W,2002, Proteins Biochemistry and biotechnology England: John Wiley & Son LTD. Greenberg, eat al. 2002, Biocatalysis:  Development of Nitrilases for Enantioselective Production of Carboxylic Acid Derivatives, An Enzyme Library Approach , Journal of American chemical society, 124 (31), pp 9024–9025. Herranz, A & Burke, J.M, 1993, In vitro selection and evolution of RNA: applications for catalytic RNA, molecular recognition and drug discovery. The FASEB Journal. Hilvert, D, 2001, Enzyme Engineering. Chimia, Biochemistry , 55 (10); 867–869 Illanes, A, 2008, Principles and Applications, Enzyme Biocatalysis, New York: Springer Klauss eat al,2005,Biocatalysts and enzymes technology , Wiley. Li, Z & Beilin, J, 2002, Current Opinion in Biotechnology: an overview, Enzyme technology. 13:338-344. Liese, A. & Seelbach, K, 2006, Industrial Biotransformations. New York: John Wiley & Sons. Pandey, A, 2006, Enzyme Technology, New York: Springer Nerker, A, 2004, Technology and product-market experience and the success of new product introductions in the pharmaceutical industry, Strategic management journal, 22(19). Read More