African Journal of
Microbiology Research

  • Abbreviation: Afr. J. Microbiol. Res.
  • Language: English
  • ISSN: 1996-0808
  • DOI: 10.5897/AJMR
  • Start Year: 2007
  • Published Articles: 5215


Structural adaptation and biocatalytic prospective of microbial cold-active α-amylase

Mohammed Kuddus1*, Roohi1, Jamal M. Arif2 and Pramod W. Ramteke3      
1Protein Research Laboratory, Department of Biotechnology, Integral University, Lucknow-226026, India. 2Department of Biochemistry, University of Hail, P. O. Box 2440, Hail, Saudi Arabia. 3Department of Biological Sciences, SHIATS, Allahabad-211007, India.  
Email: [email protected]

  •  Accepted: 15 December 2011
  •  Published: 16 January 2012


Amylases have most widely been reported to occur in microorganisms, although they are also found in plants and animals. Microbial cold-active α-amylases confer high activities at low temperature that favours production of comparatively insubstantial compounds. Cold-active α-amylases have an advantage under extreme low temperature conditions due to their freeze tolerance mechanism, intrinsic greater membrane fluidity and production of cold-acclimation proteins. Due to considerable progress towards energy savings process in industries, the low temperature stability has been regarded as the most important characteristics of cold-active amylases. Cold active enzymes attract more and more attention nowadays. Comparatively little information is available on cold-active microbial α-amylases and its catalytic properties. Now the situation is changing which recently enchanted the scientific community to focus in various fields, such as analytical, medicinal and clinical chemistry, as well as their extensive industrial applications such as starch industry, food processing, additive in detergents, waste-water treatment, biopulping, textile industry, environmental bioremediation in cold climates and other molecular biology applications.


Key words: Psychrophiles, psychrotrophs, extremozymes, cold-active amylase, starch degrading enzymes.