Dr MUNI KUMAR DOKKA
@mallareddyuniversity.ac.in
ASSOCIATE PROFESSOR IN BIOCHEMISTRY
MALLA REDDY UNIVERSITY
Completed Ph.D. in Biochemistry from Andhra University, Visakhapatnam in the year 2014. Worked as Research Scientist in DST-PURSE Program, Advanced Analytical Laboratory, Andhra University, Visakhapatnam for one year. Completed Post-Doctoral Studies in the Department of Biochemistry, Andhra University from Dec 2015 to Dec 2020. Broad area of specialization includes Clinical Biochemistry, Plant Biochemistry, Protein Chemistry, Enzymology, Microbial Biotechnology and Cancer Biology. Qualified in CSIR - UGC NET (JRF) in 2005 and GATE in 2006. Recipient of the UGC- Rajiv Gandhi National Fellowship (RGNF) during 2008 - 2013. Published 29 papers in peer reviewed and indexed National and International journals. Presented work at several Indian and International Conferences. Received Young Scientist Award from the Andhra Pradesh Akademi of Sciences for his outstanding research in the field of Life Sciences for the year 2016.
EDUCATION
M.Sc in Biochemistry
Ph.D in Biochemistry
Post Doctoral Scientist in Biochemistry
RESEARCH, TEACHING, or OTHER INTERESTS
Biochemistry, Clinical Biochemistry, Cancer Research, Biotechnology
Scopus Publications
Scholar Citations
Scholar h-index
Scholar i10-index
Scopus Publications
Teja Mandragutti, Muni Kumar Dokka, Bindiya Panchagnula, and Sudhakar Godi
Springer Science and Business Media LLC
Abstract Background Microbial community is one of the diversified communities of the marine environment. Studies have shown that microorganisms isolated from the marine environment are metabolically active and have adapted to life in the ocean. The marine microorganisms use various survival strategies to combat heavy metal stress and decolorization of various textile dyes, thus playing an important role in the bioremediation of cadmium and degradation of textile dyes. The present study deals with the isolation and 16S rRNA molecular characterization of M3 and M8 bacterial strains isolated from marine water samples collected from Visakhapatnam harbor. M3 and M8 isolates were also checked for their efficacy in the removal of cadmium and decolorization of various textile dyes from the environment. Results The water sample was subjected to tube dilution method to isolate bacterial strains, and ten different isolates were screened. The biochemical tests were performed for the isolates to prove their validity and 16S rRNA molecular sequencing and phylogenetic analysis for species identification. Out of interest, two bacterial strains, namely, M3 and M8 were subjected to 16S rRNA molecular sequencing and phylogenetic analysis and were identified as Bacillus subtilis and Pseudomonas resinovorans. The two bacterial strains showed promising dye degradation property when checked with nine different textile dyes of wavelength ranging from 400 to 600 nm and removal of cadmium from the growth medium. Conclusion The present study demonstrates the isolates M3 and M8 to be potential strains having dye decolorization and bioremediation of cadmium applications.
Muni Kumar Dokka, Hemalatha K. P. J, and Siva Prasad Davuluri
Innovare Academic Sciences Pvt Ltd
Objective: The objective of the present study was to characterize the monoheaded trypsin inhibitors, Abelmoschus moschatus trypsin inhibitor-I (AMTI-I) and AMTI-II from the seeds of A. moschatus with respect to their specificity, mode of action, and active site residues.Methods: Standard methods were followed in determining inhibitory activities of monoheaded inhibitors. IC50 values and inhibitory constants (Ki) of AMTI-I and AMTI-II were determined. Studies on complex formation and chemical modification of inhibitors were performed.Results: AMTI-I and AMTI-II were found to be serpins, strongly active against trypsin, moderately active against porcine elastase, Staphylococcus aureus protease, and Aspergillus oryzae protease. AMTI-I and AMTI-II have shown non-competitive type of inhibition toward bovine trypsin with Ki values of inhibitors for trypsin found to be 0.25±0.02 nM and 0.22±0.06 nM, respectively. Complex studies revealed the formation of stable 1:1 complex of trypsin with both AMTI-I and AMTI-II. Chemical modification of the functional groups of the inhibitors by selective reagents indicated that arginine residues are essential for their trypsin inhibitory activities.Conclusion: Investigations on the specificity of protease inhibitors are important for understanding their physiological role, control mechanisms involved in the regulation of proteolysis in biological systems and mode of action.
Muni Kumar Dokka, Lavanya Seva, and Siva Prasad Davuluri
Springer Science and Business Media LLC