International Journal of
Biotechnology and Molecular Biology Research

  • Abbreviation: Int. J. Biotechnol. Mol. Biol. Res.
  • Language: English
  • ISSN: 2141-2154
  • DOI: 10.5897/IJBMBR
  • Start Year: 2010
  • Published Articles: 102


Enhancing thermostability of the biocatalysts beyond their natural function via protein engineering

Shelly Goomber1, Pushpender K. Sharma1,2*, Monika Sharma1, Ranvir Singh3 and Jagdeep Kaur1
1Department of Biotechnology, Sector 14, Panjab University, Chandigarh 160014, India. 2Indian Institute of Sciences Education and Research, S.A.S. Nagar, Sector-81, Mohali, Punjab, 140306, India. 3National Centre for Human Genome Studies and Research (NCHGSR), Sector 14, Panjab University, Chandigarh 160014, India.
Email: [email protected]

  •  Accepted: 23 May 2012
  •  Published: 30 June 2012


Majority of the naturally occurring enzymes lacks essential features required during the harsh conditions of the industrial processes, because of their less stability. Protein engineering tool offers excellent opportunity to improve the biochemical properties of these biocatalysts. These techniques further help in understanding the structure and function of the proteins. Most common methods employed in protein engineering are directed evolution and rational mutagenesis. Several research groups have utilized these methods for engineering the stability/activity of diverse class of enzymes. In silico tools further plays an important role in designing better experimental strategy to engineer these proteins. The availability of vast majority of data on protein thermostability will enable one to envisage the possible factors that may contribute significantly in maintaining the protein structure and function during various physical conditions. This review discusses the common method employed in protein engineering along with various molecular/computational approaches that are being utilized for altering protein activity, along with important factors associated with these processes.

Key words: Computational database, rational, directed evolution, thermostability, hydrophobicity, three dimensional structure, configuration, biocatalysts.