4-Deoxy-l-erythro-5-hexoseulose Uronate (DEH) and DEH Reductase: Key Molecule and Enzyme for the Metabolism and Utilization of Alginate

Kawai, Shigeyuki; Hashimoto, Wataru

doi:10.3390/molecules27020338

Cited by 5 publications

(3 citation statements)

References 54 publications

(145 reference statements)

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“…93 ) Details of the DEH metabolic pathway, including evolutionary and structural aspects of alginate lyases and other enzymes involved in the pathway are described elsewhere. 26 , 94 – 98 )…”

Section: Alginate Recognition and Transport Systemsmentioning

confidence: 99%

Bacteria with a mouth: Discovery and new insights into cell surface structure and macromolecule transport

Murata

Kawai

Hashimoto

2022

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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A bacterium with a “mouth”-like pit structure isolated for the first time in the history of microbiology was a Gram-negative rod, containing glycosphingolipids in the cell envelope, and named Sphingomonas sp. strain A1. The pit was dynamic, with repetitive opening and closing during growth on alginate, and directly included alginate concentrated around the pit, particularly by flagellins, an alginate-binding protein localized on the cell surface. Alginate incorporated into the periplasm was subsequently transferred to the cytoplasm by cooperative interactions of periplasmic solute-binding proteins and an ATP-binding cassette transporter in the cytoplasmic membrane. The mechanisms of assembly, functions, and interactions between the above-mentioned molecules were clarified using structural biology. The pit was transplanted into other strains of sphingomonads, and the pitted recombinant cells were effectively applied to the production of bioethanol, bioremediation for dioxin removal, and other tasks. Studies of the function of the pit shed light on the biological significance of cell surface structures and macromolecule transport in bacteria.

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Section: Alginate Recognition and Transport Systemsmentioning

confidence: 99%

Bacteria with a mouth: Discovery and new insights into cell surface structure and macromolecule transport

Murata

Kawai

Hashimoto

2022

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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“…With the understanding and exploration of marine resources, various methods are available for the degradation of alginate into alginate oligosaccharides (AOS) with a variety of significant physiological characteristics such as antioxidant ( Jiang et al, 2021 ), antitumor ( Chen et al, 2017 ), anticancer ( Fang et al, 2017 ), anti-inflammatory ( Saigusa et al, 2015 ), immune regulation ( Wang et al, 2021 ). The unsaturated monosaccharides would be converted into 4-deoxy-L-erythro-5-hexoseulose uronate (DEH), which can be used as the substrate to produce biofuel ( Kawai and Hashimoto, 2022 ). In addition, the use of algae to produce biofuel has broad development prospects, and algae biofuel is likely to become one of the most important renewable energy sources in the future ( Lee and Mooney, 2012 ).…”

Section: Introductionmentioning

confidence: 99%

Improving the thermostability of alginate lyase FlAlyA with high expression by computer-aided rational design for industrial preparation of alginate oligosaccharides

Zhang

Pan

et al. 2022

Front. Bioeng. Biotechnol.

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FlAlyA, a PL7 alginate lyase with industrial potential, is widely applied in the preparation the alginate oligosaccharide because of its high activity of degradation the alginate. However, heat inactivation still limits the industrial application of FlAlyA. To further enhance its thermostability, a group of mutants were designed, according to evaluating the B-factor value and free energy change via computer-aided calculation. 25 single-point mutants and one double-points mutant were carried out by site-directed mutagenesis. The optimal two single-point mutants H176D and H71K showed 1.20 and 0.3°C increases in the values of Tm, while 7.58 and 1.73 min increases in the values of half-life (t1/2) at 50°C, respectively, compared with that of the wild-type enzyme. Interestingly, H71K exhibits the comprehensive improvement than WT, including expression level, thermal stability and specific activity. In addition, the mechanism of these two mutants is speculated by multiple sequence alignment, structural basis and molecular dynamics simulation, which is likely to be involved in the formation of new hydrogen bonds and decrease the SASA of the mutants. These results indicate that B-factor is an efficient approach to improves the thermostability of alginate lyase composed of β-sheet unit. Furthermore, the highest yield of the mutant reached about 650 mg/L, which was nearly 36 times that of previous studies. The high expression, excellent activity and good thermal stability make FlAlyA a potential candidate for the industrial production of alginate oligosaccharides.

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“…Alginate-utilizing microorganisms express endo- and exo-type alginate lyases, degrading alginate to unsaturated uronic acid monosaccharides. Subsequently, its pyranose ring is enzymatically or non-enzymatically cleaved to produce 4-deoxy-L- erythro -5-hexoseulose uronic acid (DEH) [ 3 , 4 , 5 ]. We isolated Falsirhodobacter sp.…”

Section: Introductionmentioning

confidence: 99%

Production of 4-Deoxy-L-erythro-5-Hexoseulose Uronic Acid Using Two Free and Immobilized Alginate Lyases from Falsirhodobacter sp. Alg1

et al. 2022

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Falsirhodobacter sp. alg1 expresses two alginate lyases, AlyFRA and AlyFRB, to produce the linear monosaccharide 4-deoxy-L-erythro-5-hexoseulose uronic acid (DEH) from alginate, metabolizing it to pyruvate. In this study, we prepared recombinant AlyFRA and AlyFRB and their immobilized enzymes and investigated DEH production. Purified AlyFRA and AlyFRB reacted with sodium alginate and yielded approximately 96.8% DEH. Immobilized AlyFRA and AlyFRB were prepared using each crude enzyme solution and κ-carrageenan, and immobilized enzyme reuse in batch reactions and DEH yield were examined. Thus, DEH was produced in a relatively high yield of 79.6%, even after the immobilized enzyme was reused seven times. This method can produce DEH efficiently and at a low cost and can be used to mass produce the next generation of biofuels using brown algae.

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4-Deoxy-l-erythro-5-hexoseulose Uronate (DEH) and DEH Reductase: Key Molecule and Enzyme for the Metabolism and Utilization of Alginate

Cited by 5 publications

References 54 publications

Bacteria with a mouth: Discovery and new insights into cell surface structure and macromolecule transport

Bacteria with a mouth: Discovery and new insights into cell surface structure and macromolecule transport

Improving the thermostability of alginate lyase FlAlyA with high expression by computer-aided rational design for industrial preparation of alginate oligosaccharides

Production of 4-Deoxy-L-erythro-5-Hexoseulose Uronic Acid Using Two Free and Immobilized Alginate Lyases from Falsirhodobacter sp. Alg1

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