Priyanka Nath

@mituniversity.ac.in

Assistant Professor School of Bioengineering Sciences and Research
MIT Art, Design and Technology University

Priyanka Nath


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https://researchid.co/priyanka123

EDUCATION

A PhD holder in Biosciences and Bioengineering from Indian Institute of Technology, Guwahati and a Gold medalist in Integrated MSc Biosciences and Bioinformatics

RESEARCH, TEACHING, or OTHER INTERESTS

Structural Biology, Molecular Biology, Multidisciplinary, Multidisciplinary

FUTURE PROJECTS

Microbial xylanase engineering and its clinical applications

Xylanase engineering from microbes focuses on optimizing enzyme properties for enhanced stability and activity, with clinical applications in improving digestive health and treating metabolic syndromes


Applications Invited
Collaborators

Identification and characterization of novel drug targets against multi-drug resistant bacteria

The identification and characterization of novel drug targets against multi resistant bacteria involve discovering and analyzing new molecular targets that could be critical for the bacterium's survival and virulence.


Applications Invited
collaborators
8

Scopus Publications

Scopus Publications

  • Metagenomics applications in enhancing cellulase production
    Priyanka Nath, Pooja Rana
    Biomass Valorization Technologies Insights Challenges and Prospects, 2025
    Cellulases play a vital role in the bioconversion of cellulose into valuable products, with applications ranging from biofuel production to bioremediation. Traditional methods of cellulase discovery and optimization face limitations in uncovering diverse and efficient enzymes for industrial use. Metagenomics has emerged as a prevailing tool to explore microbial diversity for the identification of novel cellulase enzymes. A sampling of environments rich in cellulose-degrading organisms and potential enzymes with unique properties suited for various industrial applications can be utilized. These enzymes can be engineered or optimized for enhanced cellulase production leading to more efficient biomass conversion processes in industries like biofuel production and waste management. The current chapter describes the advantages of metagenomics studies over conventional methods in cellulase discovery. It illustrates methodologies employed in metagenomics studies for cellulase discovery and demonstrates successful case studies where metagenomics has been applied to enhance cellulase production and address current challenges and prospects. The chapter will also describe how metagenomics offers a promising avenue for enhancing cellulase production by tapping into the genetic reservoir of diverse microbial communities. It will also give insight into how knowledge gained from metagenomic studies can contribute to the development of tailored enzyme cocktails for industrial applications for advancement in the efficiency and sustainability of cellulose-based bioprocesses.
  • Highly efficient, processive and multifunctional recombinant endoglucanase RfGH5_4 from Ruminococcus flavefaciens FD-1 v3 for recycling lignocellulosic plant biomasses
    Parmeshwar Vitthal Gavande, Priyanka Nath, Krishan Kumar, Nazneen Ahmed, Carlos M.G.A. Fontes, Arun Goyal
    International Journal of Biological Macromolecules, 2022
  • Structure and dynamics analysis of multi-domain putative β-1,4-glucosidase of family 3 glycoside hydrolase (PsGH3) from Pseudopedobacter saltans
    Priyanka Nath, Arun Goyal
    Journal of Molecular Modeling, 2021
  • Sequential pretreatment of sugarcane bagasse by alkali and organosolv for improved delignification and cellulose saccharification by chimera and cellobiohydrolase for bioethanol production
    Priyanka Nath, Premeshworii Devi Maibam, Shweta Singh, Vikky Rajulapati, Arun Goyal
    3 Biotech, 2021
    The online version contains supplementary material available at 10.1007/s13205-020-02600-y.
  • Assessment of combination of pretreatment of Sorghum durra stalk and production of chimeric enzyme (β-glucosidase and endo β-1,4 glucanase, CtGH1-L1-CtGH5-F194A) and cellobiohydrolase (CtCBH5A) for saccharification to produce bioethanol
    Mohanapriya Nedumaran, Shweta Singh, Sumitha Banu Jamaldheen, Priyanka Nath, Vijayanand Suryakant Moholkar, Arun Goyal
    Preparative Biochemistry and Biotechnology, 2020
    Optimization of pretreatment and saccharification of Sorghum durra stalk (Sds) was carried out. The chimeric enzyme (CtGH1-L1-CtGH5-F194A) having β-glucosidase (CtGH1) and endo β-1,4 glucanase activity (CtGH5-F194A) and cellobiohydrolase (CtCBH5A) from Clostridium thermocellum were used for saccharification. Chimeric enzyme will save production cost of two enzymes, individually. Stage 2 pretreatment by 1% (w/v) NaOH assisted autoclaving + 1.5% (v/v) dilute H2SO4 assisted oven heating gave lower total sugar yield (366.6 mg/g of pretreated Sds) and total glucose yield (195 mg/g of pretreated Sds) in pretreated hydrolysate with highest crystallinity index 55.6% than the other stage 2 pretreatments. Optimized parameters for saccharification of above stage 2 pretreated biomass were 3% (w/v) biomass concentration, enzyme (chimera: cellobiohydrolase) ratio, 2:3 (U/g) of biomass, total enzyme loading (350 U/g of pretreated biomass), 24 h and 30 °C. Best stage 2 pretreated Sds under optimized enzyme saccharification conditions gave maximum total reducing sugar yield 417 mg/g and glucose yield 285 mg/g pretreated biomass in hydrolysate. Best stage 2 pretreated Sds showed significantly higher cellulose, 71.3% and lower lignin, 2.0% and hemicellulose, 12.2% (w/w) content suggesting the effectiveness of method. This hydrolysate upon SHF using Saccharomyces cerevisiae under unoptimized conditions produced ethanol yield, 0.12 g/g of glucose. Abbreviation: Ct-Clostridium thermocellum, Sds-Sorghum durra stalk, TRS-Total reducing sugar, HPLC-High performance liquid chromatography, RI-Refractive index, ADL-acid insoluble lignin, GYE-Glucose yeast extract, MGYP-Malt glucose yeast extract peptone, SHF-separate hydrolysis and fermentation, OD-Optical density, PVDF-Poly vinylidene fluoride, TS-total sugar, FESEM-Field emission scanning electron microscopy, XRD-X-ray diffraction, FTIR-Fourier transform infra-red spectroscopy and CrI-Crystallinity index.
  • Role of glycine 256 residue in improving the catalytic efficiency of mutant endoglucanase of family 5 glycoside hydrolase from Bacillus amyloliquefaciens SS35
    Shweta Singh, Krishan Kumar, Priyanka Nath, Arun Goyal
    Biotechnology and Bioengineering, 2020
    Wild‐type, BaGH5‐WT and mutant, BaGH5‐UV2 (aspartate residue mutated to glycine), endoglucanases belonging to glycoside hydrolase family 5 (GH5), from wild‐type, and UV2 mutant strain of Bacillus amyloliquefaciens SS35, respectively, were earlier cloned in pHTP0 cloning vector. In this study, genes encoding BaGH5‐WT or BaGH5‐UV2 were cloned into pET28a(+) expression‐vector and expressed in Escherichia coli BL‐21(DE3)pLysS cells. BaGH5‐UV2 showed 10‐fold (43.6 U/mg) higher specific activity against carboxymethylcellulose sodium salt (CMC‐Na), higher optimal temperature by 10°C at 65°C, and 22‐fold higher catalytic efficiency against CMC‐Na, than BaGH5‐WT. BaGH5‐UV2 showed stability in wider acidic pH range (5.0–7.0) unlike BaGH5‐WT in narrow basic pH range (7.0–7.5). BaGH5‐UV2 displayed a mutation, Asp256Gly in L11 loop, connecting β6‐sheet with α6‐helix, near active site toward the domain surface of (α/β)8‐TIM barrel fold. Molecular dynamics simulation studies showed more stable structure, accessibility of substrate for a catalytic site, and increased flexibility of loop L11 of BaGH5‐UV2 than the wild type, suggesting enhanced catalysis by BaGH5‐UV2. Molecular docking analysis displayed enhanced hydrogen bond interactions of cello‐oligosaccharides with BaGH5‐UV2, unlike BaGH5‐WT. Thus, Gly256 residue of loop L11 plays an important role in enhancing catalytic efficiency, and pH stability of GH5 endoglucanase. Therefore, these results help in protein engineering of GH5 endoglucanase for improved biochemical properties.
  • Combined SAXS and computational approaches for structure determination and binding characteristics of Chimera (CtGH1-L1-CtGH5-F194A) generated by assembling β-glucosidase (CtGH1) and a mutant endoglucanase (CtGH5-F194A) from Clostridium thermocellum
    Priyanka Nath, Kedar Sharma, Krishan Kumar, Arun Goyal
    International Journal of Biological Macromolecules, 2020
  • Development of bi-functional chimeric enzyme (CtGH1-L1-CtGH5-F194A) from endoglucanase (CtGH5) mutant F194A and Β-1,4-glucosidase (CtGH1) from Clostridium thermocellum with enhanced activity and structural integrity
    Priyanka Nath, Arun Dhillon, Krishan Kumar, Kedar Sharma, Sumitha Banu Jamaldheen, Vijayanand Suryakant Moholkar, Arun Goyal
    Bioresource Technology, 2019

Publications

First Author:

1. Nath, P., Dhillon, A., Kumar, K., Sharma, K., Jamaldheen, S. B., Moholkar, V. S., & Goyal, A. (2019). Development of bi-functional chimeric enzyme (CtGH1-L1-CtGH5-F194A) from endoglucanase (CtGH5) mutant F194A and β-1, 4-glucosidase (CtGH1) from Clostridium thermocellum with enhanced activity and structural integrity. Bioresource Technology, 282, 494-501.
2. Nath, P., Sharma, K., Kumar, K.,& Goyal, A. (2020). Combined SAXS and computational approaches for structure determination and binding characteristics of Chimera (CtGH1-L1-CtGH5-F194A) generated by assembling β-glucosidase (CtGH1) and a mutant endoglucanase (CtGH5-F194A) from Clostridium thermocellum. International Journal of Biological Macromolecules. 148, 364-377
3. Nath, P., Maibam P.D., Singh, S., Rajulapati, V & Goyal, A. (2020). Sequential pretreatment of sugarcane bagasse by alkali and organosolv for improved delignification and cellulose saccharification by chimera and cellobiohydrolase for bioethanol production.3 Biotech, 11, 1-16.
4. Nath, P., & Goyal, A. (2021). Structure and dynamics analysis of multi-domain putative β-1, 4-glucosidase of family 3 glycoside hydrolase (PsGH3) from Pseudopedobacter saltans. Journal of Molecular Modeling, 27(4), 1-16.


Co-Author:
1. Kumar, K., Nath, P., and Goyal, A. (2018). Structural characterization of an