Abstract
An extracellular cyclodextrin glucanotransferase (CGTase, EC 2.4.1.19) has been characterized for the first time in a strain of bacteria of the species Caldalkalibacillus mannanilyticus IB-OR17-B1. The enzyme was isolated from the culture supernatant using ultrafiltration and affinity adsorption on corn starch. The specific activity of the CGTase increased by 18 times as a result of purification with an enzyme yield of 56%. The molecular weight of the isolated enzyme was 70 kDa according to the denaturing electrophoresis in polyacrylamide gel. The CGTase of C. mannanilyticus IB-OR17-B1 demonstrated its maximum cyclizing activity at pH 8 and a temperature of 60°C, respectively, and it was stable in the pH range of 7–10 and temperatures of 70°C or less. The thermal stability of the enzyme under 70°C increased by 10–15% in the presence of 5–10 mM of calcium and magnesium salts. The cations of Ag+, Cu2+, Zn2+, Fe2+ and Fe3+ at a concentration of 5 mM inhibited CGTase activity by 90, 26, 23, 18, and 11%, respectively. Under the optimal conditions and enzyme-substrate ratio 1 U/g the isolated CGTase converted potato starch to mixture of α-, β-and γ-cyclodextrins with weight ratio 38.8 : 52.6 : 8.6 and a yield of 42% in 24 h.
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During the research, the equipment of the “Agidel” Central Common Use of the Ufa Federal Research Center of the Russian Academy of Sciences was used.
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The work was carried out within the framework of the state assignment of the Ministry of Education and Science of the Russian Federation on topic No. 220131100163-4 “Interspecific interactions in microbial communities and plant-microbial associations of natural and technogenic ecosystems (genetic, biochemical and biotechnological aspects)”.
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Milman, P.Y., Gilvanova, E.A. & Aktuganov, G.E. Cyclodextringlucanotransferase of the Alkalophilic Strain Caldalkalibacillus mannanilyticus IB-OR17-B1. Appl Biochem Microbiol 59, 570–579 (2023). https://doi.org/10.1134/S0003683823050125
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DOI: https://doi.org/10.1134/S0003683823050125