A new L-arabinose isomerase with copper ion tolerance is suitable for creating protein-inorganic hybrid nanoflowers with enhanced enzyme activity and stability

被引:37
|
作者
Xu, Zheng [1 ,2 ]
Wang, Rui [1 ,2 ]
Liu, Chao [1 ,2 ]
Chi, Bo [1 ,2 ]
Gao, Jian [3 ]
Chen, Beining [4 ]
Xu, Hong [1 ,2 ]
机构
[1] State Key Lab Mat Oriented Chem Engn, Nanjing 210009, Jiangsu, Peoples R China
[2] Nanjing Tech Univ, Coll Food Sci & Light Ind, Nanjing 211816, Jiangsu, Peoples R China
[3] Yancheng Inst Technol, Yancheng, Peoples R China
[4] Univ Sheffield, Sheffield S10 2TN, S Yorkshire, England
来源
RSC ADVANCES | 2016年 / 6卷 / 37期
基金
中国国家自然科学基金;
关键词
D-TAGATOSE; PURIFICATION; CLONING; STRATEGIES;
D O I
10.1039/c5ra27035a
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Protein-inorganic hybrid nanoflowers were prepared using Cu2+, PBS buffer, and a copper ion tolerant L-arabinose isomerase that was derived from Paenibacillus polymyxa (PPAI). The expensive rare sugar L-ribulose or D-tagatose was prepared utilizing these nanoflowers with L-arabinose or D-galactose as the substrate, respectively. The PPAI hybrid nanoflowers showed better enzyme stabilities in both thermal and acidic conditions. Meanwhile, long term batch production was successful showing high stability using these hybrid nanoflowers, which achieved a conversion rate of 61.8% from L-arabinose to L-ribulose.
引用
收藏
页码:30791 / 30794
页数:4
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