@ARTICLE{Stencel_Barbara_M._Kinetic,
 author={Stencel, Barbara M. and Jaworska, Małgorzata M.},
 volume={Accepted articles},
 journal={Chemical and Process Engineering: New Frontiers},
 pages={chitin deacetylase},
 pages={activity centre},
 pages={kinetic studies},
 howpublished={online},
 publisher={Polish Academy of Sciences Committee of Chemical and Process Engineering},
 abstract={The deacetylation process of chitin or chitosan is carried out on industrial scale by chemical reaction with concentrated NaOH or KOH solution, but an enzymatic process is also possible. Enzymatic deacetylation with chitin deacetylase (EC 3.5.1.41) is non-destructive for polymer chains, and that is why recently it has been investigated more intensively. The structure of the enzyme is important information as it helps to better understand the enzyme action. Chitin deacetylase's primary and secondary structures were presented in literature and were the basis for the mathematical modelling of the 3D tertiary structure. However, the mathematical model for the activity centre has never been confirmed experimentally. This paper presents the experimental confirmation of a computer modelling of the catalytic residues in the activity centre of extracellular chitin deacetylase from Absidia coerulea vel orchidis. Based on kinetic studies, amino acids responsible for enzyme activity were determined experimentally as aspartic acid and glutamic acid or as two aspartic acid residues.},
 type={Article},
 title={Kinetic evidence of catalytic residues in the activity centre of chitindeacetylase from Absidia coerulea vel orchidis},
 URL={http://journals.pan.pl/Content/132439/e71_CPE-00178-2024-03-Accepted%20Article.pdf},
 doi={10.24425/cpe.2024.149466},
}