Purification, immobilization, evolution, and characterization of D-allulose 3-epimerase from Antarctic Microbacterium
文献类型： 外文期刊
作者： Li, Jingqi 1 ; Sun, Jingjing 1 ; Wang, Wei 1 ; Jiang, Chengcheng 1 ; Hao, Jianhua 1 ;
作者机构： 1.Chinese Acad Fishery Sci, Qingdao Marine Sci & Technol Ctr, State Key Lab Mariculture Biobreeding & Sustainabl, Yellow Sea Fisheries Res Inst,Lab Marine Drugs & B, Qingdao 266071, Peoples R China
2.Shanghai Ocean Univ, Coll Fisheries & Life Sci, Shanghai 201306, Peoples R China
3.Jiangsu Collaborat Innovat Ctr Exploitat & Utiliza, Lianyungang 222005, Peoples R China
关键词： D-allulose; Biosynthesis; Immobilized enzyme
期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.5； 五年影响因子：8.7 ）
ISSN： 0141-8130
年卷期： 2025 年 310 卷
页码：
收录情况： SCI
摘要： D-allulose is a rare, low-calorie sugar substitute with multiple physiological functions and is widely used in food and pharmaceutical industries. D-allulose is primarily produced by the catalytic conversion of D-fructose via allulose 3-epimerase (DAEase). In this study, a DAEase gene, dpema4, was isolated from an Antarctic bacterium and expressed in Escherichia coli. The recombinant DAEase was a homotetramer with an optimal temperature 60 degrees C and pH of 7.5. Its catalytic activity was not strictly dependent on metal ions, making it a safer alternative the other reported DAEases. The recombinant DAEase showed exhibited the highest activity towards D-allulose, and the bioconversion rate was 29 %. For immobilization, the cellulose-binding domain (CBD) was fused DAEase, and the fusion protein was immobilized on microcrystalline cellulose. The immobilized DAEase showed highly improved pH stability and maintained approximately 44 % of catalytic activity after 10 continuous action cycles. The single-point mutant A248H showed high thermal stability and catalytic activity at 60 degrees C, the bioconversion rate of D-fructose reached 32 %. In summary, the recombinant DAEase can serve as a good candidate enzyme for the production of D-allulose, and the establishment of a one-step purification immobilization of DAEase can facilitate its industrial application.
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