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Volume 11 Journal of Proteomics & Bioinformatics Open Access Computational Biology 2018
September 05-06, 2018
September 05-06, 2018 Tokyo, Japan
International Conference on
Computational Biology and Bioinformatics
J Proteomics Bioinform 2018, Volume 11
DOI: 10.4172/0974-276X-C1-113
Structural prediction and comparative studies of psychrophilic α-galactosidase from Glaciozyma antarctica
against mesophilic and thermophilic enzymes
Shuhaila Mat-Sharani
National University of Malaysia, Malaysia
α-galactosidase is an essential enzyme that catalyses’ the hydrolysis of α-1-6 linked terminal galactosyl residues from
oligosaccharides, galacto-polysaccharides and glycol-conjugates. Glaciozyma antarctica is an obligate psychrophilic yeast
with an optimal growth temperature of 12 °C and able to tolerate high temperature up to 20 °C. Since this yeast able to grow
in an extremely cold temperature the enzyme must have special characteristics in adaptation to cold. The objectives of this
study are to predict the structure and function of G. antarctica cold adapted α-galactosidase and to characterize its adaptation
strategies towards the extremely cold environment based on homology modeling and molecular dynamics. It is commonly
stated that there is a relationship between the flexibility of an enzyme and its catalytic activity at low temperature. Comparison
between the structure of G. antarctica α-galactosidase enzymes with their homologs from the mesophilic and thermophilic
fungus showed that G. antarctica α-galactosidase enzyme is more flexible because it has more loop structure with a lower
number of hydrogen and disulfide bonds.