Dr. Muthu Prasad, M.Sc., Ph.D., - Bharathidasan University - SERB-National Post-Doctorate

Dr. Muthu Prasad

M.Sc., Ph.D.,

Bharathidasan University

SERB-National Post-Doctorate

Tiruchirappalli, Tamil Nadu | India

Main Specialties: Biology, Biotechnology, Infectious Disease, Medical Microbiology, Molecular Genetic Pathology, Public Health

Additional Specialties: Molecular Microbiology

ORCID logohttps://orcid.org/0000-0003-0017-963X


Top Author

Dr. Muthu Prasad, M.Sc., Ph.D., - Bharathidasan University - SERB-National Post-Doctorate

Dr. Muthu Prasad

M.Sc., Ph.D.,

Introduction

I graduated in Life Sciences from The American College, Madurai Kamaraj University, Tamil Nadu, India. I acquired immense knowledge on molecular microbiology, protein-structure, function relationship and analytical biochemical techniques. I received a meritorious research fellowship from University Grants Commission (UGC), India for my doctoral research work. I have been awarded SERB National Postdoctoral Fellowship and also have research experience from Indian Institute of Technology, Kanpur.

Primary Affiliation: Bharathidasan University - Tiruchirappalli, Tamil Nadu , India

Specialties:

Additional Specialties:

Research Interests:


View Dr. Muthu Prasad’s Resume / CV

Education

Jul 2016 - Jul 2018
Bharathidasan University School of Life Sciences
SERB N-PDF
Microbiology
Mar 2015 - Nov 2015
Indian Institute of Technology Kanpur
Project Scientist
Mechanical Engineering
Jul 2010 - Oct 2015
Madurai Kamaraj University School of Biotechnology
Ph.D.,
Molecular Microbiology
Aug 2014 - Feb 2015
Indian Institute of Technology Kanpur
Research Associate
Biological Sciences and Bioengineering & Mechanical Engineering
May 2008
The American College, Madurai
M.Sc.,
Botany (Spl. Microbiology)
May 2006
The American College, Madurai
B.Sc.,
Botany (Spl. Industrial Microbiology)

Experience

Jul 2016
SERB N-PDF
Postdoctorate
Microbiology
Mar 2015
Project Scientist
Research
Biotechnology
Sep 2014
Senior Project Associate
Research
Biotechnology

Publications

7Publications

234Reads

1Profile Views

2PubMed Central Citations

Silver enhanced nano-gold dot blot immunoassay for leptospirosis.

J Microbiol Methods 2019 01 28;156:20-22. Epub 2018 Nov 28.

Medical Microbiology Laboratory, Department of Microbiology, Center for Excellence in Life Sciences, Bharathidasan University, Tiruchirappalli 620 024, Tamil Nadu, India. Electronic address:

View Article

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.mimet.2018.11.021DOI Listing
January 2019
193 Reads
2.026 Impact Factor

A novel method for the immobilization of a thermostable fungal chitinase and the properties of the immobilized enzyme.

Biotechnol Appl Biochem 2014 Jul-Aug;61(4):441-5. Epub 2014 Mar 1.

Department of Molecular Microbiology, School of Biotechnology, Madurai Kamaraj University, Madurai, India.

View Article

Download full-text PDF

Source
http://dx.doi.org/10.1002/bab.1179DOI Listing
April 2017
15 Reads
2 Citations
1.362 Impact Factor

Immobilization of a thermostable, fungal recombinant chitinase on biocompatible chitosan beads and the properties of the immobilized enzyme.

Biotechnol Appl Biochem 2015 Jul-Aug;62(4):523-9. Epub 2015 Jul 26.

Department of Molecular Microbiology, School of Biotechnology, Madurai Kamaraj University, Madurai, India.

View Article

Download full-text PDF

Source
http://dx.doi.org/10.1002/bab.1283DOI Listing
May 2016
26 Reads
1.362 Impact Factor

IMMOBILIZATION OF A THERMOSTABLE, FUNGAL RECOMBINANT CHITINASE ON BIOCOMPATIBLE CHITOSAN BEADS AND THE PROPERTIES OF THE IMMOBILIZED ENZYME

2015 Jul-Aug;62(4):523-9. Epub 2015 Jul 26

Biotechnol. Appl. Biochem.

A recombinant, thermostable fungal chitinase from the thermophilic fungus, Thermomyces lanuginosus, was immobilized on glutaraldehyde cross-linked chitosan beads, and the properties of the immobilized chitinase were studied. The enzyme was found to be almost completely immobilized in 6 H under shaking condition at 30 °C. The immobilized enzyme exhibited much wider pH optimum and was more stable at alkaline pH values as compared with the soluble enzyme. Both the forms of the enzyme were optimally active at 60 °C and stable at 50 °C for 3 H, and after 3 H, the activity of the soluble enzyme declined sharply, whereas the immobilized chitinase was stable up to 6 H without any significant loss in the activity. KM and Vmax values of the immobilized enzyme were 1.18 mM and 445.7 μmol/Min/mg of protein, respectively. The immobilized enzyme was stable at least for 1 month at 4 °C without any significant loss in the activity.

View Article
July 2015
19 Reads

Purification and characterization of a fungal recombinant chitinase, overexpressed in Saccharomyces cerevisiae -suitable for bioconversion of chitin wastes

Ind J Appl Res. 4(11): 55-63

Indian Journal of Applied Research

A chitinase gene of the thermophilic fungus, T. lanuginosus, was cloned and overexpressed in Saccharomyces cerevisiae. The overexpressed recombinant chitinase was purified by ammonium sulphate precipitation, ion exchange and hydrophobic interaction column chromatographic techniques. The enzyme was purified 20-fold with a specific activity of 69817. The recombinant chitinase was homogeneous as judged by SDS-PAGE and the molecular mass of the protein was ~ 39 kDa. The purified chitinase was optimally active at pH 6.0 and at 60 ˚C. KM and Vmax of the purified recombinant were found to be 0.66 mM and 81.6 moles/min/mg protein, respectively. The enzyme was found to be highly thermostable and retained about 80% of the activity even after 3 h at 50 ˚C. The enzyme was found to be glycosylated. MALDI-MS analysis confirmed that the purified enzyme belongs to an extracellular, family 18 chitinase type. Atomic force microscopic data clearly indicate the degradation of the native chitin polymer by the recombinant purified chitinase to much smaller units. Efficient hydrolysis of native chitins by the recombinant chitinase suggests potential industrial applications for this enzyme requiring chitin processing at elevated temperatures. CD spectra of the native and denatured recombinant chitinase suggest that the beta structures play an important role on the stability of the enzyme at high temperatures.

View Article
November 2014
20 Reads

Bioinformatics analyses of a Thermophilic Fungal Recombinant Chitinase

International Journal of ChemTech Research CODEN (USA): IJCRGG ISSN : 0974-4290 Vol.6, No.8, pp 4042

International Journal of ChemTech Research

A thermophilic fungal chitinase was cloned, sequenced and overexpressed in Saccharomyces cerevisiae. Multiple sequence alignment of the recombinant chitinase revealed that the catalytic domain is 100% conserved with other family GH18 chitinases. Phylogenetic analysis revealed that the recombinant chitinase exhibited a very close proximity to the chitinases of other thermophilic fungi and higher fungi. Glycosylation of the recombinant chitinase was analyzed by in silico methods and confirmed by experimental data. Homology modeling of the chitinase showed the typical (α/β)8 TIM barrel structure. Molecular docking of the enzyme revealed the involvement of a glutamic acid of the catalytic domain in the catalytic process.

View Article
September 2014
20 Reads

Overexpression of a Chitinase Gene from the Thermophilic Fungus, Thermomyces lanuginosus in Saccharomyces cerevisiae and Characterization of the Recombinant Chitinase

J Microb Biochem Technol 4: 086-091. doi: 10.4172/1948-5948.1000076

Journal of Microbial & Biochemical Technology

A chitinase gene from the thermophilic fungus, Thermomyces lanuginosus ATCC 44008 has been cloned and overexpressed in Saccharomyces cerevisiae SEY 2101. The recombinant chitinase was produced as soluble secreted protein. The enzyme activity was found to be maximum on fourth day at 30°C in the induction medium. The overexpressed chitinase displayed optimum activity at pH 6.5 and at 60°C. The recombinant chitinase attributed remarkable thermostability by holding more than 60% of the enzyme activity after 6 h at 50°C. The molecular mass of the overexpressed chitinase was 42 kDa as measured by SDS-PAGE. The kinetic parameters such as KM and Vmax of the enzyme were found to be 0.403 mM and 8.74 mmoles/min/mg protein, respectively. Synthesis of the recombinant chitinase was strongly repressed by glucose. The eukaryotic translational inhibitor, cycloheximide in the induction medium showed 10% of higher activity whereas 30% of the activity was inhibited by transcriptional inhibitors, viz. 8-azaguanine and 8-hydroxyquinoline. The overexpressed recombinant chitinase may find potential application in pharmaceutical industry to prepare chitooligosaccharides.

View Article
December 2012
19 Reads