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- W2899056706 abstract "d-Allose, a rare sugar, is an ideal table-sugar substitute and has many advantageous physiological functions. l-Rhamnose isomerase (l-RI) is an important d-allose-producing enzyme, but it exhibits comparatively low catalytic activity on d-allulose. In this study, an array of hydrophobic residues located within β1−α1–loop were solely or collectively replaced with polar amino acids by site-directed mutagenesis. A group of mutants was designed to weaken the hydrophobic environment and strengthen the catalytic behavior on d-allulose. Compared with that of the wild-type enzyme, the relative activities of the V48N/G59N/I63N and V48N/G59N/I63N/F335S mutants toward d-allulose were increased by 105.6 and 134.1%, respectively. Another group of mutants was designed to enhance thermostability. Finally, the t1/2 values of mutant S81A were increased by 7.7 and 1.1 h at 70 and 80 °C, respectively. These results revealed that site-directed mutagenesis is efficient for improving thermostability and catalytic behavior toward d-allulose." @default.
- W2899056706 created "2018-11-09" @default.
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- W2899056706 date "2018-10-29" @default.
- W2899056706 modified "2023-10-17" @default.
- W2899056706 title "Improving Thermostability and Catalytic Behavior of <scp>l</scp>-Rhamnose Isomerase from <i>Caldicellulosiruptor obsidiansis</i> OB47 toward <scp>d</scp>-Allulose by Site-Directed Mutagenesis" @default.
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- W2899056706 doi "https://doi.org/10.1021/acs.jafc.8b05107" @default.
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