Biochemistry & Molecular Biology Journal Open Access

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Arooma Maryam

Department of Bioinformatics and Biotechnology, Government College University, Pakistan

  • Original Research Article   
    Computational approach to study role of active site amino acids of alpha-amylases in thermostability of Pyrococcus fu-riosus and Bacillus sp.
    Author(s): Tayyaba Huma*, Ghulam Mustafa, Ayesha sethi, Arooma Maryam and Muhammad Ali

    Alpha amylase has a wide range of applications in starch processing, textile industry and its role as a detergent is also well defined. In this study rational approach of protein engineering to analyse the nature of the active site of thermostable alpha amylases via in silico computational tools was excercised. Sequential and structural analysis of alpha amylases from Pyrococcus furiosus (100ºC-105ºC), Bacillus licheniformis (90-95ºC) and Bacillus amyloliquefaciens (72ºC) was carried out. Sequential analysis of hyperthermophilic and thermophilic alpha amylases of studied organisms revealed high AT content in nucleotide sequences. Ratio of charged residues such as Asp, Glu, Arg, His and Lys were found higher as compared to neutral amino residues i.e. Asn, Ser and Thr in hyperthermostable Pyrococcus furiosus and Bacillus licheniformis alpha amylases which stay active.. View More»

    Abstract PDF