American Journal of Chemical Engineering
Volume 5, Issue 6, November 2017, Pages: 135-139
Received: Sep. 13, 2017;
Accepted: Sep. 26, 2017;
Published: Nov. 13, 2017
Views 1833 Downloads 94
Abubakar Muhammad Nazif, Department of Biotechnology, Modibbo Adama University of Technology, Yola, Nigeria
Ayuba Yohanna Musa, Department of Chemistry, Abubakar Tafawa Balewa University, Bauchi, Nigeria
Muhammad Muawiya Alkali, Department of Biochemistry, Modibbo Adama University of Technology, Yola, Nigeria
Ilesanmi Esther, Department of Chemistry, University of Benin, Benin, Nigeria
Indigenous enzymes found in nature have found wide application in industries ascribable to their ability to catalyze complex chemical processes under moderate experimental and environmental conditions. However, the use of indigenous enzymes is yet to achieve the needed industrial goal for, indigenous enzymes are readily unstable when subjected to harsh environmental conditions. Since the emergence of recombinant DNA technology and recent developments in protein engineering in recent years, there have been continuous reports regarding enzyme stability – most especially by the introduction of site-directed mutagenesis. With these new developments, scientists have been able to engineer enzymes using a variety of strategies in rational design such as the introduction of disulfide bridges and engineering hydrophobic residues. This review aims to highlight rational design methods and enzyme immobilization from various studies, which may be used to increase stability in industrial enzymes.
Abubakar Muhammad Nazif,
Ayuba Yohanna Musa,
Muhammad Muawiya Alkali,
Maximizing Stability in Industrial Enzymes: Rational Design Approach – A Review, American Journal of Chemical Engineering.
Vol. 5, No. 6,
2017, pp. 135-139.
Copyright © 2017 Authors retain the copyright of this article.
This article is an open access article distributed under the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/
) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
J. A Littlechild. Improving the ‘tool box’ for Robust Industrial Enzymes. J. Ind. Microbial. Biotechnol. 2017; 44(4):711-720.
Rao LV, Chandel AK, Chandrasekhar G, Rodhe AV, Stridevi j. Environmental and Industrial Biotechnology, biotechnology of thermophiles. 2. New York: springer publishers; 2013. Cellulases of thermophilic microbes in thermophilic microbes; pp. 730-771.
Sharma R, Thakur V, Sharma M, Birkland Nils-Kare. Thermophilic microbes in environmental and industrial biotechnology, biotechnology of thermophiles. 2. New York: Springer publishers; 2013. Biocatalysis through thermostable lipases: adding flavor to chemistry; pp. 905-928.
M. K Tiwari, R. Singh, R. K Singh, I. Kim. (2012). Computational approaches for rational design of proteins with novel functionalities. Computational and Structural Biotechnology Journal. (2) 3:, http://dx.doi.org/10.5936/csbj.201209002.
Ulmer, K. M. (1983). Protein engineering. Science, 2: (19)666-671.
U. T Bornsheuer, M. Pohl (2001). Improved biocatalysts by directed evolution and rational protein design. Curr Opin Chem Biol. 5:137-143.
Jurgens C, Strom A, Wegener D, Hettwer S, Wilmanns M. (2000) Directed evolution ofa(beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways. Proc Natl Acad Sci. USA 97:9925-9930.
D. N. Rubingh, R. A. Grayling (2000). “Proein Engineering” encyclopedia of life support systems (online article). http://www.eolss.net/sample-chapter/c17/E6-58-03-06.pdf
Arnold FH, Volkov AA. (1999). Directed evolution of biocatalysts. Curr Opin Chem Biol. 3:54-59.
Iyer, P. V. and Ananthanarayan, L., (2008). Enzyme stability and stabilization-Aqueous and non-aqueous environment. Process Biochemistry, 43: 1019-1032.
Eijsink, V. G. H., Vriend, G., Van der Burg, B., van derZee, J. (1992). Introduction of a stabilizing 10 residue hairpm in Badussubti Iisneutral protease. Protein Eng. 5:157-163.
D. P Clark and N. J Pazdernik (2009). Biotechnology: applying the genetic revolution. Library of Congress. pp 329-348. ISBN 978-0-12-175552-2.
Perry LJ, & Wetzel R (1984). Disulphide bond engineered into T4 lysozyme: stabilization of the protein toward thermal inactivation. Science. 2:226(4674):555-7.
Matsumura M, & Mathews BW (1989). Control of enzyme activity by an engineered disulfide bond. Science. 10:243(4892):792-4.
Murby M, Samuelsson E, Nguyen TN, Mignard L, et al. (1995). Hydrophobicity engineering to increase solubility and stability of a recombinant protein from respiratory syncytial virus. Eur J Biochem. 15:230(1):38-44.
Wright HT (1991). Sequence and structure determinants of the non-enzymatic deamination of asparagines and glutamine residues in proteins. Protein Eng. 4(3):283-94.
Alber, T. 1989. Prediction of Protein Structure and the Principles of Protein Conformation. Plenum Press, New York, USA, pp. 161-192.
Stefan Janecek (1993). Strategies for obtaining stable enzymes. Process Biochemistry. 28:435-445.
Sahoo, B., Sahu, S. K., Bhattacharya, D., Dhara, D., Pramanik, P. (2012). A novel approach for efficient immobilization and stabilization of papain on magnetic gold nano composites. Colloids Surf. B, 101:280–289.