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Articles by Roohi
Total Records ( 2 ) for Roohi
  Roohi , M.Kuddus , I.Z. Ahmad and J.M. Arif
  Cold-active α-amylases provided a large biotechnological potential and offers numerous economical and ecological benefits through energy saving process. It also minimizes undesirable chemical reactions that could occur at high temperatures. The objective of present study was to isolate novel bacterial strain for production of cold-active α-amylase. On the basis of primary screening thirty cold-active α-amylase producing bacteria were isolated from soil of Gangotri glacier, Western Himalaya, India. The isolated bacteria were subjected to enzyme production and one potential isolate (GA2) was selected for production optimization. The α-amylase production was found maximum (5870 units) at 20°C and pH 9 after 120 h incubation. Among the carbon and nitrogen sources, lactose (1%) and yeast extract (1%) was found best source, respectively. The isolate GA2 (Gangotri amylolytic) was resistant to penicillin (10 μg) among tested antibiotics and as per plasmid curing results, amylase production was a plasmid mediated characteristic. The phylogenetic analysis revealed that GA2 have highest homology with Microbacterium foliorum (99%). This was the first report on cold-active α-amylase production by M. foliorum GA2 and on the basis of 16S rRNA sequences also got an accession number HQ832574 from NCBI.
  Mohammed Kuddus , Roohi , Jamal M. Arif and Pramod W. Ramteke
  Absolutely the largest proportion of the Earth's biosphere is comprised of organisms that thrive in cold environments are known as psychrophiles and psychrotrophs. Their ability to proliferate in the cold is predicated on a capacity to synthesize cold-adapted enzymes like amylases, proteases, lipases, pectinases, cellulases, etc. that could be used in low-energy processes. Amylases have most widely been reported to occur in microorganisms, although they are also found in plants and animals. Cold-active α-amylases confer low activation energies and high activities at low temperature which are favorable properties for the production of relatively insubstantial compounds. In addition, these enzymes have an advantage under extreme low temperature conditions due to their inherent greater membrane fluidity, production of cold-acclimation proteins and the mechanism of freeze tolerance. The low temperature stability of cold-active amylases has been regarded as the most important characteristics for use in the industry because of considerable progress towards energy savings but unfortunately these enzymes have largely been overlooked. Now this situation is changing which recently fascinated the scientific community to focus in many fields, such as clinical, medicinal and analytical chemistries, as well as their widespread biotechnological applications such as food processing, additive in detergents, waste-water treatment, biopulping, environmental bioremediation in cold climates and molecular biology applications. This review addresses the present status of knowledge on the source, structure, production and molecular characteristics of cold-active α-amylases and their biotechnological applications.
 
 
 
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