The nucleoside hydrolase is the enzyme that catalyzes nucleoside to D-ribose as well as purine or pyrimidine. Nucleoside hydrolases have been widely found in organisms except mammals. In this study, three nucleoside hydrolases (Cgl1364, Cgl1977, and Cgl2835) from Corynebacterium glutamicum ATCC 13032 were expressed and purified. The three recombinant enzymes all exhibited activities of nucleoside hydrolases, which could catalyze adenosine, cytidine, guanosine, xanthoside, inosine and uridine to D-ribose and correspond purine or pyrimidine. However, the specificity to substrates of the recombinant enzymes were different. These enzymes exhibited activities at 15-55 ℃ and pH 4-10, and the optimum temperature was 35 ℃ and the optimum pH was 7.0. Moreover, the thermal stability of Cgl1977 was higher than that of Cgl1364 and Cgl2835. The BL-cgl2835 resting cells were used as the enzyme source to hydrolyze uridine, resulting in the yield of 89.5%.This is the first work reported the function and characteristics of nucleoside hydrolases from C. glutamicum, which will provide reference for biosynthesis of D-ribose, purine, and pyrimidine.
MENG Yan
,
DING Xiaohu
,
YANG Wenjun
,
XIE Haixiao
,
WANG Junzhe
,
ZHANG Chenglin
. Enzymatic characteristics of nucleoside hydrolases from Corynebacterium glutamicum[J]. Food and Fermentation Industries, 2023
, 49(11)
: 27
-33
.
DOI: 10.13995/j.cnki.11-1802/ts.032848
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