Biochemical Properties of a Novel d-Mannose Isomerase from Pseudomonas syringae for d-Mannose Production

被引:7
|
作者
Hua, Xiaohan [1 ]
Li, Yanxiao [2 ]
Jiang, Zhengqiang [1 ]
Ma, Junwen [2 ]
Liu, Haijie [1 ]
Yan, Qiaojuan [2 ]
机构
[1] China Agr Univ, Key Lab Food Bioengn China Natl Light Ind, Coll Food Sci & Nutr Engn, 17 Qinghua Donglu, Beijing 100083, Peoples R China
[2] China Agr Univ, Beijing Adv Innovat Ctr Food Nutr & Human Hlth, Coll Engn, 17 Qinghua Donglu, Beijing 100083, Peoples R China
基金
中国国家自然科学基金;
关键词
Mannose; Mannose isomerase; Characterization; Pseudomonas syringae; Mannose production;
D O I
10.1007/s12010-021-03487-y
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
d-Mannose isomerase can reversibly catalyze d-fructose to d-mannose which has various beneficial effects. A novel d-mannose isomerase gene (PsMIaseA) from Pseudomonas syringae was cloned and expressed in Escherichia coli. The recombinant d-mannose isomerase (PsMIaseA) showed the highest amino acid sequence homogeneity of 50% with ManI from Thermobifda fusca. PsMIaseA was purified through Ni-NTA chromatography, and its specific activity was 818.6 U mg(-1). The optimal pH and temperature of PsMIaseA were pH 7.5 and 45 degrees C, respectively. The enzyme was stable within a wide pH range from 5.0 to 10.0. It could efficiently convert d-fructose to d-mannose without any metal ions. When PsMIaseA was incubated with 600 g/L d-fructose for 6 h, the space-time yield of d-mannose reached 27.2 g L-1 h(-1) with a maximum conversion ratio of 27%. Therefore, the d-mannose isomerase may be suitable for green production of d-mannose.
引用
收藏
页码:1482 / 1495
页数:14
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