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Difference between revisions of "User:Anna Kulminskaya"
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| + | I’m a research scientist at the Petersburg Nuclear Physics Institute, Molecular and Radiation Biophysics Department, Russia. I received my PhD degree under supervision of Neustroev Kirill studying the exo-inulinase from Aspergillus awamori (GH32). Now I’m a leader of the Laboratory of Enzymology at the same Institute. | ||
| + | The main Research area of our team is carbohydrate enzymology and applications. We focus in understanding the way in which particular enzymes act to alter the structure of poly- or oligosaccharides found in Nature, and to harness these enzymes for practical applications. Using the tools of chemo-organic synthesis and biochemistry, our work aims to provide increased understanding of the chemical principles underlying mechanisms of action of glycoside hydrolases with transglycosylating activity. | ||
| + | We are particularly interested in the alpha-galactosidases (GH27 and 36), beta-galactosidase (GH35), beta-xylosidases (GH3), beta-xylanases, cellulose-degrading enzymes, alpha- or beta-mannosidases (GH2) and alpha-L-fucosidases. | ||
[[Category:Contributors|Kulminskaya,Anna]] | [[Category:Contributors|Kulminskaya,Anna]] | ||
Revision as of 01:13, 6 October 2010
I’m a research scientist at the Petersburg Nuclear Physics Institute, Molecular and Radiation Biophysics Department, Russia. I received my PhD degree under supervision of Neustroev Kirill studying the exo-inulinase from Aspergillus awamori (GH32). Now I’m a leader of the Laboratory of Enzymology at the same Institute.
The main Research area of our team is carbohydrate enzymology and applications. We focus in understanding the way in which particular enzymes act to alter the structure of poly- or oligosaccharides found in Nature, and to harness these enzymes for practical applications. Using the tools of chemo-organic synthesis and biochemistry, our work aims to provide increased understanding of the chemical principles underlying mechanisms of action of glycoside hydrolases with transglycosylating activity.
We are particularly interested in the alpha-galactosidases (GH27 and 36), beta-galactosidase (GH35), beta-xylosidases (GH3), beta-xylanases, cellulose-degrading enzymes, alpha- or beta-mannosidases (GH2) and alpha-L-fucosidases.