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Journal of Bioinformatics©
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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 organism’s temperature and pH optimum.
Keywords: Xylanase, Thermomyces lanuginosus, family
11 xylanases, Sequence homology.
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