Thermotoga maritima beta-fructosidases are enzymes which release beta-D-fructose from sucrose, raffinose and fructan polymers such as inulin. Surfaces of beta-fructosidases 1UYP and 1W2T from Thermotoga maritima was studied in this work. It was showed that amino acids are distributed not equally on the surfaces of the enzymes. Several clusters of charged and hydrophobic residues were detected at pH 7.0. Such clusters were detected by calculation of distances between them. It was determined that on surfaces of beta-fructosidases PDB ID: 1UYP and PDB ID: 1W2T respectively 96 and 95 % of charged amino acids and also 50 and 42 % of hydrophobic amino acids form clusters. 6 clusters of charged amino acids on surface of beta-fructosidase 1UYP and 5 clusters on surface of beta-fructosidase 1W2T was detected. Composition of such clusters is presented. Both types of beta-fructosidase have 3 clusters of hydrophobic amino acids on their surface. This facts should be considered when choosing immobilization conditions. It was showed that charged matrix is more promising to immobilization of beta-fructosidases 1UYP and 1W2T from Thermotoga maritima due to possibility of binding without significant loss of activity due to overlapping active center. Hydrophobic carriers are less promising due to probable active site overlap. Such binding may have a loss of enzyme activity as a result.

This work was supported by the Ministry of Education and Science of the Russian Federation under state order No. FZGU-2020-0044