Characterization of a recombinant d-allulose 3-epimerase from Agrobacterium sp. ATCC 31749 and identification of an important interfacial residue

Tseng, Wen‐Chi; Chen, Chao-Nan; Hsu, Chung-Ting; Lee, Hsu-Chieh; Fang, Hong-Yi; Wang, Mingjun; Wu, Yi-Hung; Fang, Tsuei‐Yun

doi:10.1016/j.ijbiomac.2018.02.036

Cited by 39 publications

(10 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…[15] and Caballeronia fortuita [16], d ‐allulose 3‐epimerases from Agrobacterium tumefaciens [17], Agrobacterium sp. [18], Clostridium bolteae [19], Clostridium cellulolyticum [20], Clostridium scindens [21], Clostridium sp. [22], Desmospora sp.…”

Section: Figmentioning

confidence: 99%

Crystal structure of a novel homodimeric l‐ribulose 3‐epimerase from Methylomonus sp.

et al. 2021

View full text Add to dashboard Cite

D-Allulose has potential as a low-calorie sweetener which can suppress fat accumulation. Several enzymes capable of D-allulose production have been isolated, including D-tagatose 3-epimerases. Here, we report the isolation of a novel protein from Methylomonas sp. expected to be a putative enzyme based on sequence similarity to ketose 3-epimerase. The synthesized gene encoding the deduced ketose 3-epimerase was expressed as a recombinant enzyme in Escherichia coli, and it exhibited the highest enzymatic activity toward L-ribulose, followed by D-ribulose and D-allulose. The X-ray structure analysis of L-ribulose 3-epimerase from Methylomonas sp. (MetLRE) revealed a homodimeric enzyme, the first reported structure of dimeric Lribulose 3-epimerase. The monomeric structure of MetLRE is similar to that of homotetrameric L-ribulose 3-epimerases, but the short C-terminal a-helix of MetLRE is unique and different from those of known L-ribulose 3 epimerases. The length of the C-terminal a-helix was thought to be involved in tetramerization and increasing stability; however, the addition of residues to MetLRE at the C terminus did not lead to tetramer formation. MetLRE is the first dimeric L-ribulose 3-epimerase identified to exhibit high relative activity toward D-allulose. D-Allulose (alternative name D-psicose) is a rare sugar, and its physiological functions, such as altering the blood glucose level, suppressing fat accumulation, and use as a low-calorie sweetener [1-9], have been focused on as a promising functional food ingredient. In Japan, a low-calorie syrup containing D-allulose, Rare Sugar Sweet Ò (Matsutani Chemical Industry Co., Ltd., Hyogo, Japan) [10], is commercially available and its labeling as a functional food was recently approved. In addition, the U.S. Food and Drug Administration (FDA) stated that 'it allows the low-calorie sweetener allulose to be excluded from total and added sugar counts on Nutrition and Supplement Facts labels when used as an ingredient' (FDA In Brief, April, 2019). AbbreviationsAgDAE, D-allulose 3-epimerase from Arthrobacter globiformis; AtDAE, D-allulose 3-epimerase from Agrobacterium tumefaciens; CcDAE, D-allulose 3-epimerase from Clostridium cellulolyticum; DAE, D-allulose 3-epimerase; his_MetLRE long2, his_MetLRE with nine additional residues (TAIKTIELH) at the C terminus and with three mutations (Y9I, Y37F, Y286L); his_MetLRE, N-terminal his-tagged MetLRE; his_MetLRE3, his_MetLRE with three mutations (Y9I, Y37F, and Y286L); LRE, L-ribulose 3-epimerase; MetLRE, L-ribulose 3-epimerase from Methylomonas sp.; MlLRE, L-ribulose 3-epimerase from Mesorhizobium loti; PcDTE, D-tagatose 3-epimerases from Pseudomonas cichorii.

show abstract

Section: Figmentioning

confidence: 99%

Crystal structure of a novel homodimeric l‐ribulose 3‐epimerase from Methylomonus sp.

et al. 2021

View full text Add to dashboard Cite

show abstract

“…(Mu et al, ); DAE from Treponema primitia (Zhang, Zhang, Jiang, & Mu, ), Flavonifractor plautii (Park, Kim, et al, ), Arthrobacter globiformis M30 (Yoshihara et al, ), Agrobacterium sp. ATCC 31749 (Tseng et al, ), and so on. Those enzymes have been highly expressed in Escherichia coli based on recombinant expression vector.…”

Section: Introductionmentioning

confidence: 99%

Development of food‐grade expression system for d‐allulose 3‐epimerase preparation with tandem isoenzyme genes in Corynebacterium glutamicum and its application in conversion of cane molasses to D‐allulose

Yang

Tian

Zhang

et al. 2019

Biotech & Bioengineering

View full text Add to dashboard Cite

D-Allulose 3-epimerase (DAE) has been applied to produce D-allulose, a low-calorie and functional sweetener. In this study, a new DAE from Paenibacillus senegalensis was characterized in Escherichia coli. Furthermore, we presented a tandem isoenzyme gene expression strategy to express multiple DAEs in one cell and construct foodgrade expression systems based on Corynebacterium glutamicum. Seventeen expression cassettes based on three DAE genes from different organisms were constructed.Among all recombinant strains, DAE16 harboring three DAE genes in an expression vector exhibited the highest enzyme activity with 22.7 U/mg. Whole-cell transformation of DAE16 produced 225 g/L D-allulose with a volumetric productivity of 353 g·g −1 ·hr −1 . The catalytic efficiency of strain C-DAE9 integrating total 11 DAE genes in chromosome was 16.4-fold higher than strains carrying one DAE. Fed-batch culture of C-DAE9 gave enzyme activity of 44,700 U/L. We also expressed a thermostable invertase in C. glutamicum and obtained enzyme activity of 29 U/mg. Immobilized cells expressing DAE or invertase exhibited 80% of retained activity after 30 cycles of catalytic reactions. Those immobilized cells were coupled to produce 61.2 g/L D-allulose from cane molasses in a two-step reaction process. This study provided an efficient approach for enzyme preparation and allowed access to produce D-allulose from other abundant and low-cost feedstock enriched with sucrose.

show abstract

“…C. cellulolyticum H10 DAEase Glu150 and Glu244 perform the epimerization reaction of catalysis at the C 3 position of D-fructose (Chan et al, 2012). The DTEase family enzymes have distinctly different degrees of dependency on metal ions of Mn 2+ , Co 2+ , and Mg 2+ (Tseng et al, 2018;Yang et al, 2019;Zhu et al, 2019a). A. tumefaciens DAEase and R. sphaeroides DTEase activity could be remarkably enhanced when a metal ion Mn 2+ is involved in the catalytic system (Kim H.J.…”

Section: Enzymatic Propertiesmentioning

confidence: 99%

Review on D-Allulose: In vivo Metabolism, Catalytic Mechanism, Engineering Strain Construction, Bio-Production Technology

Jiang

Xiao

Zhu

et al. 2020

Front. Bioeng. Biotechnol.

View full text Add to dashboard Cite

Rare sugar D-allulose as a substitute sweetener is produced through the isomerization of D-fructose by D-tagatose 3-epimerases (DTEases) or D-allulose 3-epimerases (DAEases). D-Allulose is a kind of low energy monosaccharide sugar naturally existing in some fruits in very small quantities. D-Allulose not only possesses high value as a food ingredient and dietary supplement, but also exhibits a variety of physiological functions serving as improving insulin resistance, antioxidant enhancement, and hypoglycemic controls, and so forth. Thus, D-allulose has an important development value as an alternative to high-energy sugars. This review provided a systematic analysis of D-allulose characters, application, enzymatic characteristics and molecular modification, engineered strain construction, and processing technologies. The existing problems and its proposed solutions for D-allulose production are also discussed. More importantly, a green and recycling process technology for D-allulose production is proposed for low waste formation, low energy consumption, and high sugar yield.

show abstract

Characterization of a recombinant d-allulose 3-epimerase from Agrobacterium sp. ATCC 31749 and identification of an important interfacial residue

Cited by 39 publications

References 36 publications

Crystal structure of a novel homodimeric l‐ribulose 3‐epimerase from Methylomonus sp.

Crystal structure of a novel homodimeric l‐ribulose 3‐epimerase from Methylomonus sp.

Development of food‐grade expression system for d‐allulose 3‐epimerase preparation with tandem isoenzyme genes in Corynebacterium glutamicum and its application in conversion of cane molasses to D‐allulose

Review on D-Allulose: In vivo Metabolism, Catalytic Mechanism, Engineering Strain Construction, Bio-Production Technology

Contact Info

Product

Resources

About