Priyanka Nath

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

Scopus Publications

Metagenomics applications in enhancing cellulase production
Priyanka Nath, Pooja Rana
Biomass Valorization Technologies Insights Challenges and Prospects, 2025
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, et al.
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
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, et al.
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, et al.
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

Priyanka Nath

EDUCATION

RESEARCH, TEACHING, or OTHER INTERESTS

FUTURE PROJECTS

Microbial xylanase engineering and its clinical applications

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

Scopus Publications

Publications