Short Article, Arch Med Biotechnol Vol: 1 Issue: 2
Application of Enzymes: As an Emerging Pharmaceutical Research
Sharma M*
Department of Bioengineering and Biosciences, Lovely Professional University, Punjab, India
*Corresponding Author : Sharma M
Department of Bioengineering and Biosciences, Lovely Professional University, Punjab, India
E-mail: monika28sharma29@gmail.com
Received: July 19, 2018 Accepted: July 26, 2018 Published: August 01, 2018
Citation: Sharma M (2018) Application of Enzymes: As an Emerging Pharmaceutical Research. Arch Med Biotechnol 1:2.
Abstract
Enzymes are most prominent catalysts, which offer a competitive process for the chemical catalysts. Though enzymes have a great potential, its industrial applications have been hampered in terms of catalytic efficiency, specificity and stability. A variety of approaches are considered to overcome this situation including enzyme screening form natural resources, immobilization and random mutations. Industrial enzymes demand is continuously rising in terms of sustainable solutions. More than 600 industrial products are produced by using enzyme.
Keywords: Enzymes, Pharmaceutical, Marine
Introduction
Enzymes are most prominent catalysts, which offer a competitive process for the chemical catalysts [1]. Though enzymes have a great potential, its industrial applications have been hampered in terms of catalytic efficiency, specificity and stability. A variety of approaches are considered to overcome this situation including enzyme screening form natural resources, immobilization and random mutations [2]. Industrial enzymes demand is continuously rising in terms of sustainable solutions. More than 600 industrial products are produced by using enzyme [3].
Activase, the first recombinant enzyme was approved by Food and Drug administration (FDA) in 1987. This enzyme is used specifically for treating heart attacks (caused by coronary artery blockage) and known as “clot-buster”. After insulin, it was the second recombinant drug to be marketed. Since then many enzymes as coagulant and anticoagulant agents have been approved by FDA [4].
Trends in Engineering of Enzymes for Pharmaceutical Application
For the need to expand the industrial application of enzymes, substrate specificity and catalytic efficiency should be satisfied [5]. Thermo stability is in the current trend in engineering to produce enzymes. Thermo-stability combines computational methods (with directed evolution) with the structure based rational design [6]. For instance, DNA shuffling was performed via SCHEMA which generated cellobiohydrolases (CBH II), a thermo stable fungal. SCHEMA being a computational method helps in the estimation of enzyme structural disruption (after recombination of DNA) [7,8]. A useful source for enzymes is extremophiles because of the high stability in terms of pH, salts and heat [9].
In the same scenario, non-natural reactions are also performed to produce enzymes with latest catalytic functions (depends upon catalytic function) and computational methods (in addition with directed evolution) [10,11]. Molecular dynamics, calculating hydrogen bond energy and simulation of substrate docking are also employed in the design of rational approaches [12,13].
Enzyme Therapy
Adagen, a pegadamase bovine is used to treat SCID. This represents the first enzyme therapy application to treat an inherited disease [14]. ADA enzyme cleaves the extra amount of adenosine present in the circulatory system and gets reduced to being toxic to the patient’s immune system where adenosine level is high. As soon as ADA gets modified to PEG, success rate of enzyme is enhanced because PEG helps to enhance the half-life of an enzyme. Ceredase, is used in the replacement therapy for Gaucher’s disease. It is a lysosomal storage disease (LSD). During therapy, missing glucocerebrosidase is utilized by placental glucocerebrosidase (modified form) [15].
Marine Enzymes
Enzymes obtained from chemical catalysis require high pressure and temperature with sophisticated and analytical techniques. This finally affects both environment and health. This marked the era of marine biotechnology where marine enzymes were begin to be produced due to its application and characteristics [16]. This meant the utilization of fungi, algae, bacteria and sponges from marine source to produce commercial products. Xylanase (a hydrolytic enzyme) used in brew industry and Laccase used in pulp and textile industry are obtained from marine origin [17]. Enzyme fucoidanase is obtained from Sphingomonas paucimobilis (a marine bacterium), thermotolerant chitinase from Pseudoalteromonas sp. (present in Caspian sea), Ectoine synthase from Vibrio campbellii, ectoine synthase from Sphngopyxis alaskensis, endoglucanase from Paenibacillus sp. etc. are all marine source enzyme [18,19].
References
- Bruggink A, Roos EC, Vroom E (1998) Penicillin acylase in the industrial production of β-lactam antibiotics. Org Process Res Dev 2: 128-133.
- Elleuche S, Schroder C, Sahm K, Antranikian G (2014) Extremozymes-biocatalysts with unique properties from extremophilic microorganisms. Curr Opin Biotechnol 29: 116-123.
- Kumar A, Singh S (2013) Directed evolution: Tailoring biocatalysis for industrial application. Crit Rev Biotechnol 33: 365–378.
- Cui Y, Cui W, Liu Z, Zhou L, Kobayashi M, et al. (2014) Improvement of stability of nitrile 747 hydratase via protein fragment swapping. Biochem Biophys Res Commun.
- Huisman GW, Liang J, Krebber A(2010) Practical chiral alcohol manufacture using ketoreductases. Curr Opin Chem Biol 14: 122–129.
- Reetz MT, Carballeira JD, Vogel A (2006) Iterative saturationmutagenesis on the basis of B factors as a strategy for increasing protein thermostability. Angew Chem Int Ed 45: 7745–7751.
- Silberg JJ, Endelman JB, Arnold FH (2004) SCHEMA-guided protein recombination. In: Dan ER, Joseph PN, editors. Methods In Enzymology. Academic Press 35-42.
- Heinzelman P, Snow CD, Wu I, Nguyen C, Villalobos A, et al. (2009) A family of thermostable fungal cellulases created by structure-guided recombination. Proc Natl Acad Sci 106: 5610–5615.
- Illanes A, Cauerhff A, Wilson L, Castro GR (2012) Recent trends in biocatalysis engineering. Bioresources Technol 115: 48–57.
- Lee SC, Kim JH, Kim HS (2010) Design and evolution of biocatalysts. Curr Org Chem 14: 1894–1901.
- Sterner R, Merkl R, Raushel FM (2008) Computational design of enzymes. Chem Biol 15: 421–423.
- Krieger E, Koraimann G, Vriend G (2002) Increasing the precision of comparative models with YASARA NOVA — a self-parameterizing force field. Proteins 47: 393–402.
- Schwab T, Skegro D, Mayans O, Sterner RA (2008) rationally designed monomeric variant of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus is as active as the dimeric wild-type enzyme but less thermostable. J Mol Biol 376: 506–516.
- Aiuti A (2002) Advances in gene therapy for ADA-deficient SCID. Curr Opin Mol Ther 4: 515-522.
- Barton NW, Brady RO, Dambrosia JM, Bisceglie AM, Doppelt SH, et al. (1991) Replacement therapy for inherited enzyme deficiencymacrophage- targeted glucocerebrosidase for Gaucher’ disease. N Engl J Med 324: 1464-1470.
- Van BJB, Li Z (2002) Enzyme technology: An overview. Curr Opin Biotechnol 4: 338–344.
- Li S, Yang X, Yang S, Zhu M , Wang X (2012) Technology prospecting on enzymes: Application, marketing and engineering. Comput Struct Biotechnol J.
- Kim W, Park J, Park J, Choi, D, Park Y (2015) Purification and characterization of a fucoidanase (FNase S) from a marine bacterium Sphingomonas paucimobilis PF-1. Mar Drugs 13: 4398–4417.
- Mao X, Hong Y, Shao Z, Zhao Y, Liu Z (2010) A novel cold-active and alkalistable β-glucosidase gene isolated from the marine bacterium Martelella mediterranea. Appl Biochemistry Biotechnol 162: 2136–2148.