The Impact of extremophilic Enzyme: Widely Application in Industrial uses

Vol. 7 Issue 1 Page No. 70-75

Review article

Lekha Singh^1,2, Gaurav Sharma^1*, Gyanendra Awasthi², Lokendra Kumar³

¹School of Applied Sciences, Suresh Gyan vihar University, Jaipur.

²Department of Biochemistry, Dolphin PG Institute of Biomedical and Natural Science, Dehradun.

³Department of Microbiology, PM College of education karsua, Aligarh

Abstract

Some areas to be restricted have not detected bacterial life. Over the past year, the bacterial communities have become increasingly aware that they are exposed to very different conditions, such as temperature, pH, pressure, and salt. These microorganisms are termed Extremophiles. These Extremophiles produce biocatalysts and their function under Extreme conditions. Several novel applications of their biocatalyst are unique properties in the different industrial processes. At present, only a small percentage of these earth’s resources are used. An extremophile is a new development in agriculture and production but the development is also related to the production and integration of genes into larger forces, increasing the number of enzyme-induced changes in chemicals, food, pharmaceuticals, and other industrial applications.

Keywords

Extremophiles

Biocatalyst

Psychrophiles

Thermophilies

Extremozymes

*Corresponding author’s e-mail adress:  gaurav.sharma@mygyanvihar.com

*Corresponding author’s e-mail website: turnkey casino

Received: 23 July 2020; Accepted: 22 Oct 2020; Published: 25 Jan 2021

Introduction

Extremophiles are the organisms which survive in extreme environmental condition. We study them on earth is to better understand the wide range of the condition under which life evolve and survive. It helps us to understand some different environmental extremes. For biotechnology and industrial application, more than 300 different enzymes have been identified and many available enzymes do not withstand industrial reaction conditions. The extreme condition can refer to temperature, radiation, and pressure but also to geochemical extremes.

Psychrophiles

A microorganism capable of living below a temperature of 4 °C. Psychrophiles can also grow and reproduce at low temperatures ranging from -20 °C to +10 °C. This is why they are found in colder regions such as the polar region and in the deep ocean. Recently, enzymes derived from Psychrophiles have been a boon to industrial use, thanks to ongoing efforts to reduce energy consumption.

The paper industry and Pulp are also interested in the degrading Enzyme Polymer that operates at low temperatures (Bentahir et al., 2000, Kim et al., 1999, Fields et al., 2001, Smal et al., 2000, Watanabe et al., 2002). The use of Multi-Food Processing will also benefit from the availability of low-temperature Enzyme. There is a growing desire to incorporate Psychrophilic enzymes into the detergent. A feature of the enzyme derived from Psychrophiles is the combination of low-temperature functions and high activity to produce a moderate temperature. This can be explained by the increased flexibility of molecules compared to the mesophilic and thermophilic Enzyme. There is a growing number of role models from environmental and protein engineering studies (D’Amico et al., 2003, Fersht 1999, Schoichet et al., 2002, Van den Burg et al., 1998).

Thermophilies

These microorganisms have the ability to survive in conditions as high as 140 °F or higher temperatures. In particular, the extremophilic Proteases, Lipases, and polymer degradation enzymes, such as cellulase, amylases, and chitinase have very much useful in founding an industrial application. Thermophilic eubacteria are suggested to have been among the earliest bacteria hence, mainly Extremophilic Proteases, lipases, and polymer-reducing enzymes, such as cellulase, chitinase, and Amylases found their way into the Industrial Application (Table- 1). The structural features of the thermophilic Extremozymes have attracted a lot of attention. Several three-dimensional arrangements have been resolved compared to those performed by a mesophilic partner, with the main purpose of teaching how thermostability works (Beadle and Schoicet 2002, Sterner and Liebl 2001, Vieille and Zeikus 2001, Van den Burg and Eijsink 2002).

Table-1: Classification of extremophiles and examples of applications of some of their enzymes

Alkaliphiles

Growing optimally around a Ph of 10 means this clear can capable of survival in alkaline environment. An organism with the rights to survive and flourish in compounds worthy of neutralizing powerful microorganism acid enzymes that can live in conditions of strong acidic or strong alkaline reaction, e.g., in detergent manufacturing.

Acidophilic

These microorganisms are growing rapidly in acidic environment, normally at very low pH (<3) Protease, amylase, lipases and other Enzyme that are tolerant to and active at high ph and high chelator concentration of modern detergent are desirable. Several useful Enzyme have already been identified and obtained (Kocabıyık and Erdem, 2002). To detect alkaline in the mixture homology-based PCR and activity screening have been applied to serum. Proteases in a collection of thermoacidophilic archaeal and bacterial strain isolated from hot Environment (Paiardini et al., 2003).

Halophilic

These microorganism need to survive high salt concentrations to grow[17,18], with most species requiring more than 2.0 M NaCl for growth and survival Halophiles coat themselves with a special protein layer that blacks Excessive salt from Entering its cells. Halophiles caot themselves with a special protein layer that blacks Excessive salt from Entering its cells. Halophiles absorb salt at concentrations which are isotonic to the atmosphere, like sodium and potassium chloride (NaCl, KCl) (Madern and Zaccai, 2000; Klibanov, 2001). As a consequence, the protein from halophiles has to deal with the intensity of very high salts. The Enzyme have adopted to this Environment Pressure by acquiring a relatively large number of negatively charged amino acid residues on their surface to prevent precipitation. Consequently, in surroundings with lower salt concentration (Demirjian et al., 2001) the solubility of halophilic Enzyme is often very poor, which could limit their Applicability.

Radioresistant Microbes

These organisms are able to withstand in high or extreme radiations Radioresistant microbes often channel the energy from radioactivity to purposes such as producing food for themselves, and some have evolved aggressive DNA repair mechanisms to reverse any genetic damage caused by radiation. Eg. Dienococcus radiodurans, is listed by the Guinnes Book of World Records as “the world’s toughest bacterium”.

Barophiles

These organisms are able of surving high pressure environmental condition such as ocean floor. As 1000 m depth in sea beneath is disguised by a high hydrostic pressure, where coldness, darkness and short age of organic matter takes place.

References

Beadle, B. M., & Shoichet, B. K. (2002). Structural bases of stability–function tradeoffs in enzymes. Journal of molecular biology, 321(2), 285-296.

Bentahir, M., Feller, G., Aittaleb, M., Lamotte-Brasseur, J., Himri, T., Chessa, J. P., & Gerday, C. (2000). Structural, Kinetic, and Calorimetric Characterization of the Cold-active Phosphoglycerate Kinase from the AntarcticPseudomonas sp. TACII18. Journal of Biological Chemistry, 275(15), 11147-11153.

Bertoldo, C., & Antranikian, G. (2002). Starch-hydrolyzing enzymes from thermophilic archaea and bacteria. Current opinion in chemical biology, 6(2), 151-160.

D’Amico, S., Marx, J. C., Gerday, C., & Feller, G. (2003). Activity-stability relationships in extremophilic enzymes. Journal of Biological Chemistry, 278(10), 7891-7896.

Danson, M. J., & Hough, D. W. (1997). The structural basis of protein halophilicity. Comparative Biochemistry and Physiology Part A: Physiology, 117(3), 307-312.

Demirjian, D. C., Morı́s-Varas, F., & Cassidy, C. S. (2001). Enzymes from extremophiles. Current opinion in chemical biology, 5(2), 144-151.

Fersht A: Three-dimensional structure of enzymes. In Structure and Mechanism in Protein Science. WH Freeman & Co, New York, 1999.

Fields, P. A. (2001). Protein function at thermal extremes: balancing stability and flexibility. Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology, 129(2-3), 417-431.

Kim, S. Y., Hwang, K. Y., Kim, S. H., Sung, H. C., Han, Y. S., & Cho, Y. (1999). Structural basis for cold adaptation: sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum. Journal of Biological Chemistry, 274(17), 11761-11767.

Klibanov, A. M. (2001). Improving enzymes by using them in organic solvents. nature, 409(6817), 241-246.

Kocabıyık, S., & Erdem, B. (2002). Intracellular alkaline proteases produced by thermoacidophiles: detection of protease heterogeneity by gelatin zymography and polymerase chain reaction (PCR). Bioresource technology, 84(1), 29-33.

Madern, D., Ebel, C., & Zaccai, G. (2000). Halophilic adaptation of enzymes. Extremophiles, 4(2), 91-98.

Paiardini, A., Gianese, G., Bossa, F., & Pascarella, S. (2003). Structural plasticity of thermophilic serine hydroxymethyltransferases. Proteins: Structure, Function, and Bioinformatics, 50(1), 122-134.

Serour, E., & Antranikian, G. (2002). Novel thermoactive glucoamylases from the thermoacidophilic Archaea Thermoplasma acidophilum, Picrophilus torridus and Picrophilus oshimae. Antonie Van Leeuwenhoek, 81(1), 73-83.

Shoichet, B. K., Baase, W. A., Kuroki, R., & Matthews, B. W. (1995). A relationship between protein stability and protein function. Proceedings of the National Academy of Sciences, 92(2), 452-456.

Smalås, A. O., Leiros, H. K., Os, V., & Willassen, N. P. (2000). Cold adapted enzymes. Biotechnology annual review, 6, 1-57.

Sterner, R. H., & Liebl, W. (2001). Thermophilic adaptation of proteins. Critical Reviews in Biochemistry and Molecular Biology, 36(1), 39-106.

van den Burg, B., & Eijsink, V. G. (2002). Selection of mutations for increased protein stability. Current opinion in biotechnology, 13(4), 333-337.

Van den Burg, B., Vriend, G., Veltman, O. R., Venema, G., & Eijsink, V. G. (1998). Engineering an enzyme to resist boiling. Proceedings of the National Academy of Sciences, 95(5), 2056-2060.

Vieille, C., & Zeikus, G. J. (2001). Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiology and molecular biology reviews, 65(1), 1-43.

Watanabe, S., Yamaoka, N., Fukunaga, N., & Takada, Y. (2002). Purification and characterization of a cold-adapted isocitrate lyase and expression analysis of the cold-inducible isocitrate lyase gene from the psychrophilic bacterium Colwellia psychrerythraea. Extremophiles, 6(5), 397-405.