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Rani Gupta

Professor & Head of Department
Bachhawat Block, First Floor
University of Delhi South Campus

Ph: 011-24157165
Email: ranigupta.udsc57@gmail.com
CV (Download pdf file)
BSc (1976), University of Delhi, Delhi
MSc (1978), University of Delhi, Delhi
MPhil (1979), University of Delhi, Delhi

PhD (1983), University of Delhi, Delhi
Description of Research Expertise

Research interest: Industrial enzymes: Fermentation and Application; Protein engineering; Protein structure and function; Role of enzymes in microbial physiology

Key words: Lipase, Keratinase, Gamma-glutamyl transpeptidase, Feather recycling, Prion degradation, Chiral separation, Biotransformation

Description of Research:
Our group has been working on industrial enzymes like protease, lipase, amylase and chitinase since past thirty years. Current research is focused on keratinase, lipase and gamma-glutamyl transpeptidase. Our laboratory is continuosly engaged in isolation and identification of bacterial and yeast isolates from selective habitats through enrichment methods to select potential enzyme producers. We work towards strain improvement by taking a protein to gene aproach involving the methods of cloning, heterologous expression and developing a variety of vector-host combinations. This is followed by biochemical and biophysical studies of the proteins. In-silico structural and functional analysis including hgomology modleling, docking, etc. is conducted to solve the protein structure. Site directed mutagenesis is often employed to validate the in-silico analysis. Another key area is protein engoineering to obtain catalytically efficient enzymes. We also work on scale-up of the proteins and their industrial applications.

Major Achievements In Research -

Lab Personnel

Selected alumni from our laboratory holding key positions at national/international level

S. No.


Current Position


Rekha Gupta nee Singhal

Associate Professor, Gargi College, Delhi University


Prerna Diwan nee Ahuja

Associate Professor, Ram Lal Anand College, Delhi University


Paresh Gigras

Upstream Process Expert, Novartis, Singapore


Sapna Das-Bradoo

Assistant Professor, Northeastern State University, Oklahoma


Harapriya Mohapatra

Reader, National Institute of Science Education and Research (NISER), Bhubaneswar, Odisha


Pooja Phogat nee Rathi

Vice President, Kinapse, Delhi


Namita Gupta

Women Scientist (DST) at University of Delhi,  Ex-IP Consultant (Evalueserve)


Priya Ramnani

Post-doctoral Research Fellow, University of Reading, UK


S Suresh Kumar

Senior Lecturer, Universiti Putra Malaysia


Ekta Tiwari

Post-doctoral ResearchFellow, University of Alabama at Birmingham

Publications: Search Pubmed for publications (click here)

List of Publications in the last 5 years

  1. Syal P. and Gupta R. (2015) Cloning, Expression, and Biochemical Characterization
    of an Enantioselective Lipase, YLIP9, from Yarrowia lipolytica MSR80, Appl Biochem Biotechnol, doi 10.1007/s12010-015-1561-y
  2. *Gupta R., Kumari A., Syal P. And Singh Y. (2015) Molecular and functional diversity of yeast and fungal lipases: Their role in biotechnology and cellular physiology. Progress in Lipid Research. 57: 40-54.
  3. Arti A., Baronian K., Kunze G. and Gupta R. (2015), Extracellular expression of YlLip11 with a native signal peptide from Yarrowia lipolytica MSR80 in three different yeast hosts, Protein Express Purif, 110:138-144.
  4. Kumari A. and Gupta R. (2014), Functional characterisation of novel enantioselective lipase TALipA from Trichosporon asahii MSR54: sequence comparison revealed new signature sequence AXSXG among yeast lipases, Appl Biochem Biotechnol, doi 10.1007/s12010-014-1268-5
  5. Bindal S. and Gupta R. (2014), L-Theanine synthesis using γ-glutamyl transpeptidase from Bacillus licheniformis ER-15, J Agric Food Chem, 62(37): 9151–9159.
  6. Kumari A. and Gupta R. (2014), Functional characterization of a novel aspartic acid rich lipase, TALipC, from Trichosporon asahii MSR54: Solvent-dependent enantio inversion during esterification of 1-phenylethanol, Biotechnol Lett, 27: 121-130.
  7. Kumari A. and Gupta R. (2014), Novel strategy of using methyl esters as slow release methanol source during lipase expression by mut+ Pichia pastoris X33. PLoS ONE 9(8): e104272. doi:10.1371/journal.pone.010427
  8. Rajput R. and Gupta R. (2013), Expression of Bacillus pumilus keratinase rK27 in Bacillus subtilis: enzyme application on developing renewable flocculants from bone meal, Ann Microbiol, DOI 10.1007/s13213-013-0770-2.
  9. *Gupta R., Sharma R. and Beg Q. (2013), Revisiting microbial keratinases: Next generation proteases for sustainable biotechnology, Crit Rev Biotechnol 33(2): 216-228
  10. *Gupta R, Rajput R, Sharma R and Gupta N (2013), Biotechnological applications and prospective market of microbial keratinases, Appl Microbiol Biotechnol, 97(23) 9931-9940.
  11. Kumari A. and Gupta R. (2013), Phenylalanine to leucine point mutation in oxyanion hole improved catalytic efficiency of Lip 12 form Yarrowia lipolytica, Enzyme Microb Tech, 53: 386-390
  12. Baliyan A., Bhatia P., Gupta B., Sharma E., Kumari A. and Gupta R. (2013), Surface plasmon resonance based fiber optic sensor for the detection of triacylgylycerides using gel entrapment technique, Sensor and Actuators B, 188: 917-922
  13. Rajput R. and Gupta R. (2013), Thermostable keratinase from Bacillus pumilus KS12: Production, chitin crosslinking and degradation of Sup35NM aggregates, Biresour technol, 133: 118-126.
  14. Kumari A. and Gupta R. (2013), Heterologous expression, purification and characterization of thermostable lip11 from Yarrowia lipolytica in Pichia pastoris X33, J Prot Proteomics, 4(1): 5-10.
  15. Rajput R., Verma V.V., Chaudhary V. and Gupta R. (2013), A hydrolytic γ-glutamyl transpeptidase from thermo-acidophilic archaeon Picrophilus torridus: binding pocket mutagenesis and transpeptidation, Extremophiles, 17(1): 29-41.
  16. Sharma R., Verma V.V. and Gupta R. (2013), Functional characterization of an extracellular keratinolytic protease, Ker AP from Pseudomonas aeruginosa KS-1: A putative aminopeptidase with PA domain. J. Mol. Catal. 91: 8-16.
  17. Sharma R. and Gupta R. (2012) Coupled action of γ-glutamyl transpeptidase-glutathione and keratinase effectively degrades feather keratin and surrogate prion protein, Sup35NM. BioresourceTechnology, (Doi.org/10.1016/j.biortech.2012.06.038).
  18. Rajput R., Tiwary E., Sharma R. and Gupta R (2012) Swapping of pro-sequences between keratinases of Bacillus licheniformis and Bacillus pumilus: Altered substrate specificity and thermostability, Enzyme and Microbial Technology, 51: 131-138.
  19. Kumari A. and Gupta R. (2012) Extracellular expression and characterization of thermostable lipases, LIP8, LIP14 and LIP18, from Yarrowia lipolytica, Biotechnol Lett 34: 1733-1739.
  20. Kumari. A., Verma V.V. and Gupta R (2012) Comparative biochemical characterization and in-silico analysis of novel lipases Lip11 and Lip12 with Lip2 from Yarrowia lipolytica. World Journal of Microbiology and Biotechnology, DOI: 10.1007/s11274-012-1120-4.
  21. Rajput R. and Gupta R (2012) Enhanced production of recombinant thermostable keratinase of Bacillus pumilus KS12: Degradation of Sup35 NM . Research journal of Microbiology 6: 839-850.
  22. Kumari A. and Gupta R (2012) Purification and Biochemical Characterization of a Novel Magnesium Dependent Lipase from Trichosporon asahii MSR 54 and its Application in Biodiesel Production. Asian Journal of Biotechnology, 4: 70-82.
  23. Murty N.A.R., Tiwary E., Sharma R., Nair N., Gupta R. (2012) γ-Glutamyl transpeptidase from Bacillus pumilus KS 12: Decoupling autoprocessing from catalysis and molecular characterization of N-terminal region. Enzyme Microbial Technology 50: 159-64.
  24. Rajput R., Sharma R. and Gupta R (2011) Cloning and extracellular expression of a thermostable keratinase from Bacillus pumilus KS12 in E. coli and its industrially useful properties. Biotechnology and Applied Biochemistry, 58 (2): 109-118.
  25. Sharma R., Murty N.A.R. and Gupta R. (2011) Molecular Characterization of N-Terminal Pro-sequence of Keratinase Ker P from Pseudomonas aeruginosa: Identification of Region with Chaperone Activity. Applied Biochemistry and Biotechnology DOI10.1007/s12010-01.

    * Review Article

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