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Online Journal of Bioinformatics©
Established 1995

ISSN  1443-2250


Volume
19(3):240-246, 2018.


In silico conservation homology in xylanases from Thermomyces lanuginosus.

 

Shrivastava S, Shukla P, Poddar R.

 

Department of Biotechnology, Birla Institute of Technology, Mesra, Ranchi 835 215, India

 

ABSTRACT

 

Shrivastava S, Shukla P, Poddar R, In silico conservation homology in xylanases from Thermomyces lanuginosus, Onl J Bioinform, 19 (3): 240-246, 2018. Xylanases are diverse hydrolytic enzymes with potential applications in industries. In the present study a complete comparative analysis of DNA and amino acid sequences from the xylanase precursor from Thermomyces lanuginosus has been done with respect to other fungal xylanases. A study was made on phylogenetic trees showing genetic and morphological distance from different xylanase producing fungi. Analysis was made using multiple sequence alignment and conserved domains responsible for xylanolytic activity of the enzyme have been reported. A comparative study of structure of xylanase from Thermomyces lanuginosus with other closely related xylanase producing fungi like Aspergillus kawachii, Trichoderma harzianum was done and conserved catalytic domains were marked. As per earlier reported literature it has been found that xylanase producing gene sequences from fungi related to Thermomyces lanuginosus coded for proteins which were all structurally similar and all these structurally similar xylanases belonged to the family 11 of glycoside hydrolase. Furthermore it also supports the early literature that the structural similarity or dissimilarity of xylanase is irrespective of the organismís temperature and pH optimum.

 

Keywords: Xylanase, Thermomyces lanuginosus, family 11 xylanases, Sequence†† homology.


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