Exploring a Highly D-Galactose Specific L-Arabinose Isomerase From Bifidobacterium adolescentis for D-Tagatose Production

Zhang, Guoyan; An, Yi; Parvez, Amreesh; Zabed, Hossain M.; Yun, Jimmy; Qi, Xianghui

doi:10.3389/fbioe.2020.00377

Cited by 21 publications

(13 citation statements)

References 47 publications

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“…The concentrations of D -fructose, D -allulose, D -tagatose, and D -sorbose were analyzed in HPLC equipped with a refractive index detector (RID-20A, Shimadzu, Japan). Standard HPLC analysis was carried out by using the Ca 2+ -carbohydrate column (300 × 7.7 mm) (HPLX-Ca, Agilent USA) with 20 μL sample injections (Zhang et al, 2020a ). The samples were eluted by using milli pore pure water at a flow rate of 0.6 mL/min and 84°C.…”

Section: Methodsmentioning

confidence: 99%

Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta

et al. 2020

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D-allulose, which is one of the important rare sugars, has gained significant attention in the food and pharmaceutical industries as a potential alternative to sucrose and fructose. Enzymes belonging to the D-tagatose 3-epimerase (DTEase) family can reversibly catalyze the epimerization of D-fructose at the C3 position and convert it into D-allulose by a good number of naturally occurring microorganisms. However, microbial synthesis of D-allulose is still at its immature stage in the industrial arena, mostly due to the preference of slightly acidic conditions for Izumoring reactions. Discovery of novel DTEase that works at acidic conditions is highly preferred for industrial applications. In this study, a novel DTEase, DTE-CM, capable of catalyzing D-fructose into D-allulose was applications. In this study, a novel DTEase, DTE-CM, capable of catalyzing D-fructose into D-allulose was DTE-CM on D-fructose was found to be remarkably influenced and modulated by the type of metal ions (co-factors). The DTE-CM on D-fructose was found to be remarkably influenced and modulated by the type of metal ions (co-factors). The 50°C from 0.5 to 3.5 h at a concentration of 0.1 mM. The enzyme exhibited its maximum catalytic activity on D-fructose at pH 6.0 and 50°C from 0.5 to 3.5 h at a concentration of 0.1 mM. The enzyme exhibited its maximum catalytic activity on -fructose at pH 6.0 and 50°C with a Kcat/Km value of 45 mM−1min−1. The 500 g/L D-fructose, which corresponded to 30% conversion rate. With these interesting catalytic properties, this enzyme could be a promising candidate for industrial biocatalytic applications.

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Section: Methodsmentioning

confidence: 99%

Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta

et al. 2020

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“…The products involved in the reaction such as D-allulose, D-fructose, D-tagatose, and D-sorbose were analyzed by HPLC equipped with a refractive index detector (RID-20A) (Shimadzu, Japan) [ 40 ]. More details were in the filtration of the sample with a 0.22 μm MCE filter membrane prior to the sample analysis and the HPLC system was analyzed through a Ca 2+ -carbohydrate column (Hi-Plex-Ca, Agilent, Church Stretton, Shrops, UK) with its temperature of 84 °C, with deionized water as the mobile phase, and a flow rate of 0.6 mL/min.…”

Section: Methodsmentioning

confidence: 99%

The Characterization of a Novel D-allulose 3-Epimerase from Blautia produca and Its Application in D-allulose Production

Tang

Iqbal

et al. 2022

Foods

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D-allulose is a natural rare sugar with important physiological properties that is used in food, health care items, and even the pharmaceutical industry. In the current study, a novel D-allulose 3-epimerase gene (Bp-DAE) from the probiotic strain Blautia produca was discovered for the production and characterization of an enzyme known as Bp-DAE that can epimerize D-fructose into D-allulose. Bp-DAE was strictly dependent on metals (Mn2+ and Co2+), and the addition of 1 mM of Mn2+ could enhance the half-life of Bp-DAE at 55 °C from 60 to 180 min. It exhibited optimal activity in a pH of 8 and 55 °C, and the Km values of Bp-DAE for the different substrates D-fructose and D-allulose were 235.7 and 150.7 mM, respectively. Bp-DAE was used for the transformation from 500 g/L D-fructose to 150 g/L D-allulose and exhibited a 30% of conversion yield during biotransformation. Furthermore, it was possible to employ the food-grade microbial species Bacillus subtilis for the production of D-allulose using a technique of whole-cell catalysis to circumvent the laborious process of enzyme purification and to obtain a more stable biocatalyst. This method also yields a 30% conversion yield.

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“…With this approach, the enzymatic cascade can catalyze 100% conversion of L-arabinose to L-ribulose with a production yield of 0.3 g/L in less than 7 h. Synthesis of D-tagatose from inexpensive D-galactose is another example of using oxidation−reduction instead of isomerization. For the same isomerization using L-AI 164,165 or GPI 166 (Figure 9C), the conversion is not complete and the yield can only be increased at high temperature. A two-step chemoenzymatic process using P2O was reported to oxidize Dgalactose at the C-2 position followed by catalytic hydrogenation using Pd to obtain D-tagatose.…”

Section: Production Of Lignocellulosic Biomass-derived Productsmentioning

confidence: 99%

Enzymes, In Vivo Biocatalysis, and Metabolic Engineering for Enabling a Circular Economy and Sustainability

et al. 2021

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Since the industrial revolution, the rapid growth and development of global industries have depended largely upon the utilization of coal-derived chemicals, and more recently, the utilization of petroleum-based chemicals. These developments have followed a linear economy model (produce, consume, and dispose). As the world is facing a serious threat from the climate change crisis, a more sustainable solution for manufacturing, i.e., circular economy in which waste from the same or different industries can be used as feedstocks or resources for production offers an attractive industrial/business model. In nature, biological systems, i.e., microorganisms routinely use their enzymes and metabolic pathways to convert organic and inorganic wastes to synthesize biochemicals and energy required for their growth. Therefore, an understanding of how selected enzymes convert biobased feedstocks into special (bio)chemicals serves as an important basis from which to build on for applications in biocatalysis, metabolic engineering, and synthetic biology to enable biobased processes that are greener and cleaner for the environment. This review article highlights the current state of knowledge regarding the enzymatic reactions used in converting biobased wastes (lignocellulosic biomass, sugar, phenolic acid, triglyceride, fatty acid, and glycerol) and greenhouse gases (CO 2 and CH 4 ) into value-added products and discusses the current progress made in their metabolic engineering. The commercial aspects and life cycle assessment of products from enzymatic and metabolic engineering are also discussed. Continued development in the field of metabolic engineering would offer diversified solutions which are sustainable and renewable for manufacturing valuable chemicals.

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Exploring a Highly D-Galactose Specific L-Arabinose Isomerase From Bifidobacterium adolescentis for D-Tagatose Production

Cited by 21 publications

References 47 publications

Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta

Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta

The Characterization of a Novel D-allulose 3-Epimerase from Blautia produca and Its Application in D-allulose Production

Enzymes, In Vivo Biocatalysis, and Metabolic Engineering for Enabling a Circular Economy and Sustainability

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