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Impact of G449 Single-Point Mutation on Glucansucrase URE 13-300 Enzyme Properties and Polysaccharide Structure.
In: Catalysts (2073-4344), Jg. 13 (2023-12-01), Heft 12, S. 1455-1470
Online
academicJournal
Zugriff:
High-molecular-weight glucansucrase (GS) URE 13-300 with two catalytic domains (CDs) synthesizes insoluble branched α-glucan. In the present work, we explore the role of the amino acid glycine 449 (G449) located in domain B of CD1 on the enzyme properties and polysaccharide structure. Glycine was substituted with lysine via site-directed mutagenesis and the mutant DNA was expressed in recombinant Escherichia coli BL21 (DE3). The obtained mutant glucansucrase U13M1 had a shifted optimum pH, from 5.3 to 6.5, and a decreased optimal temperature, from 30 to 20 °C. The modified glucan, synthesized using U13M1, retained the water-insoluble nature of the URE 13-300 glucan and also has altered linkage composition, with about 30% fewer α-(1 → 3) linked glucose residues in the main chain. This is the first mutagenesis study on glucansucrase with two catalytic domains in a non-truncated form. [ABSTRACT FROM AUTHOR]
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Titel: |
Impact of G449 Single-Point Mutation on Glucansucrase URE 13-300 Enzyme Properties and Polysaccharide Structure.
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Autor/in / Beteiligte Person: | Angelova, Stanimira ; Vasileva, Tonka ; Bivolarski, Veselin ; Iliev, Ilia |
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Zeitschrift: | Catalysts (2073-4344), Jg. 13 (2023-12-01), Heft 12, S. 1455-1470 |
Veröffentlichung: | 2023 |
Medientyp: | academicJournal |
ISSN: | 2073-4344 (print) |
DOI: | 10.3390/catal13121455 |
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