Expression and characterization of thermostable D-allulose 3-epimerase from Arthrobacter psychrolactophilus (Ap DAEase) with potential catalytic activity for bioconversion of D-allulose from d-fructose

Laksmi, Fina Amreta; Nirwantono, Rudi; Nuryana, Isa

doi:10.1016/j.ijbiomac.2022.06.117

Cited by 19 publications

(24 citation statements)

References 33 publications

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“…CAG317 [12], Treponema primitia ZAS-1 [24], Thermoclostridium caenicola [25], Pirellula sp. SH-Sr6A [26], Flavonifractor plautii [27], Ruminiclostridium cellulolyticum H10 [6], Arthrobacter globiformis M30 [11], Novibacillus thermophilus [10], Arthrobacter psychrolactophilus [1], and DEase Gene from the Metagenome sample (DaeM) [28].…”

Section: B D-allulose 3-epimerasementioning

confidence: 99%

“…The epimerization reaction condition usually undergoes under harsh settings, including a hightemperature conditions [1,7]. The heating procedure is beneficial for sugar production because it can foster the reaction to reach its equilibrium, reduce the substrate viscosity, and avoid microbial contamination [4].…”

Section: Introductionmentioning

confidence: 99%

“…The heating procedure is beneficial for sugar production because it can foster the reaction to reach its equilibrium, reduce the substrate viscosity, and avoid microbial contamination [4]. The problem is that there were only small numbers of bacteria known to possess promising enzymes with high thermostability and high catalytic activity [1]. Until today, there were only Desmospora sp.…”

Section: Introductionmentioning

confidence: 99%

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Genome mining of potential enzyme from Chelatococcus composti for sustainable production of D-Allulose

Nirwantono

Trinugroho

Sudigyo

et al. 2023

IOP Conf. Ser.: Earth Environ. Sci.

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A novel putative D-allulose 3-epimerase (DAEase) named CcDAE with the accession number of WP_183335203.1 was discovered in this study from Chelatococcus composti genome using in silico genome mining method. The sequence, which was retrieved from the genome of Chelatococcus composti strain CGMCC 1.15283 and became the first reported D-allulose 3-epimerase from the species. The sequence length of CcDAE was 282 aa with a molecular weight prediction of 30.504 kDa. The sequence analysis disclosed a high sequence conservation at the residues building the metal binding site and substrate binding site. The phylogenetic tree also disclosed that the closest related sequence with CcDAE was from Cereibacter spaeroides. The biochemical prediction also informed that CcDAE had an isoelectric point (pI) at pH 5.74. In addition, the novel putative enzyme was predicted to withstand a high temperature up to 65 °C and was considered as a stable protein. Therefore, the research finding suggests that CcDAE was potential for further exploration.

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Section: B D-allulose 3-epimerasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Genome mining of potential enzyme from Chelatococcus composti for sustainable production of D-Allulose

Nirwantono

Trinugroho

Sudigyo

et al. 2023

IOP Conf. Ser.: Earth Environ. Sci.

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“…Many researchers have made great efforts to improve the catalytic efficiency and thermostability of DAEases . An in vitro enzymatic process using ApDAE with excellent thermostability and activity was conducted, in which the conversion rate of d -allulose reached 27% with 500 mg/L d -fructose as a substrate . However, enzymatic conversion processes cannot compete with microbial fermentation in long-term and large-scale industrial production due to the high maintenance costs for the continuous production of expensive purified enzymes .…”

Section: Introductionmentioning

confidence: 99%

“…14 An in vitro enzymatic process using ApDAE with excellent thermostability and activity was conducted, in which the conversion rate of D-allulose reached 27% with 500 mg/L D-fructose as a substrate. 15 However, enzymatic conversion processes cannot compete with microbial fermentation in long-term and largescale industrial production due to the high maintenance costs for the continuous production of expensive purified enzymes. 16 Therefore, scalable and cost-effective cellular factories for the synthesis of D-allulose are required for industrial production.…”

Section: ■ Introductionmentioning

confidence: 99%

Fine-Tuning of Carbon Flux and Artificial Promoters in Bacillus subtilis Enables High-Level Biosynthesis of d-Allulose

Zhang

Wei

Sun

et al. 2022

J. Agric. Food Chem.

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D-Allulose is an attractive rare sugar that can be used as a low-calorie sweetener with significant health benefits. To meet the increasing market demands, it is necessary to develop an efficient and extensive microbial fermentation platform for the synthesis of D-allulose. Here, we applied a comprehensive systematic engineering strategy in Bacillus subtilis WB600 by introducing Dallulose 3-epimerase (DAEase), combined with the deactivation of fruA, levDEFG, and gmuE, to balance the metabolic network for the efficient production of D-allulose. This resulting strain initially produced 3.24 g/L of D-allulose with a yield of 0.93 g of Dallulose/g D-fructose. We further screened and obtained a suitable dual promoter combination and performed fine-tuning of its spacer region. After 64 h of fed-batch fermentation, the optimized engineered B. subtilis produced D-allulose at titers of 74.2 g/L with a yield of 0.93 g/g and a conversion rate of 27.6%. This D-allulose production strain is a promising platform for the industrial production of rare sugar.

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Semi‐rational engineering of D‐allulose 3‐epimerase for simultaneously improving the catalytic activity and thermostability based on D‐allulose biosensor

Li,

Hu,

et al. 2024

Biotechnology Journal

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BackgroundD‐Allulose is one of the most well‐known rare sugars widely used in food, cosmetics, and pharmaceutical industries. The most popular method for D‐allulose production is the conversion from D‐fructose catalyzed by D‐allulose 3‐epimerase (DAEase). To address the general problem of low catalytic efficiency and poor thermostability of wild‐type DAEase, D‐allulose biosensor was adopted in this study to develop a convenient and efficient method for high‐throughput screening of DAEase variants.ResultsThe catalytic activity and thermostability of DAEase from Caballeronia insecticola were simultaneously improved by semi‐rational molecular modification. Compared with the wild‐type enzyme, DAEaseS37N/F157Y variant exhibited 14.7% improvement in the catalytic activity and the half‐time value (t1/2) at 65°C increased from 1.60 to 27.56 h by 17.23‐fold. To our delight, the conversion rate of D‐allulose was 33.6% from 500‐g L−1 D‐fructose in 1 h by Bacillus subtilis WB800 whole cells expressing this DAEase variant. Furthermore, the practicability of cell immobilization was evaluated and more than 80% relative activity of the immobilized cells was maintained from the second to seventh cycle.ConclusionAll these results indicated that the DAEaseS37N/F157Y variant would be a potential candidate for the industrial production of D‐allulose.

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Expression and characterization of thermostable D-allulose 3-epimerase from Arthrobacter psychrolactophilus (Ap DAEase) with potential catalytic activity for bioconversion of D-allulose from d-fructose

Cited by 19 publications

References 33 publications

Genome mining of potential enzyme from Chelatococcus composti for sustainable production of D-Allulose

Genome mining of potential enzyme from Chelatococcus composti for sustainable production of D-Allulose

Fine-Tuning of Carbon Flux and Artificial Promoters in Bacillus subtilis Enables High-Level Biosynthesis of d-Allulose

Semi‐rational engineering of D‐allulose 3‐epimerase for simultaneously improving the catalytic activity and thermostability based on D‐allulose biosensor

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