Author(s): P. Sai Preethi, M Ramesh Pathy

Email(s): Psaipreethi1993@gmail.com , mrameshpathy@vit.ac.in

DOI: 10.5958/0974-360X.2018.00586.3   

Address: P. Sai Preethi, M Ramesh Pathy*
School of Bio Sciences and Technology, Vellore Institute of Technology (VIT), Vellore, India
*Corresponding Author

Published In:   Volume - 11,      Issue - 7,     Year - 2018


ABSTRACT:
Peroxidases, one of the key commercial enzymes, belong to the oxidoreductase family that catalyze the oxidation of various aromatic and non-aromatic compounds, concomitant with the decomposition of H2O2.With their prominent occurrence in bacteria, fungi, actinobacteria, higher plants and insects, peroxidases have been majorly exploited due to their pivotal role in immunological, bioremediation and industrial uses. Low productivity and expensiveness limits the use of native peroxidases. Supplementary to these shortcomings, native sources yield mixture of isozymes, which is not desirable for commercial scopes. Thus, in conjunction with this, recombinant peroxidases have gained importance for sustainable processing due to their improved catalytic property, thermal stabilities, solvent and anionic tolerance. Hence, this review mainly accentuates on the recombinant peroxidases, diverse cell factories for their expression, peroxidase engineering and their proficient biotechnological applications. The attractive traits of the recombinant forms of peroxidases emphasize the requirement to study them more for their unexplored, hidden environmental and industrial applications.


Cite this article:
P. Sai Preethi, M Ramesh Pathy. Recombinant Peroxidase: Production and its Prospective Applications- A Review. Research J. Pharm. and Tech 2018; 11(7): 3186-3196. doi: 10.5958/0974-360X.2018.00586.3

Cite(Electronic):
P. Sai Preethi, M Ramesh Pathy. Recombinant Peroxidase: Production and its Prospective Applications- A Review. Research J. Pharm. and Tech 2018; 11(7): 3186-3196. doi: 10.5958/0974-360X.2018.00586.3   Available on: https://rjptonline.org/AbstractView.aspx?PID=2018-11-7-85


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RNI: CHHENG00387/33/1/2008-TC                     
DOI: 10.5958/0974-360X 

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