All lactose-oxidizing enzymes of Pseudomonas taetrolens, a highly efficient lactobionic acid-producing microorganism, are pyrroloquinoline quinone-dependent enzymes.

In previous and present studies, four enzymes (GCD1, GCD3, GCD4, and MQO1) have been found to act as lactose-oxidizing enzymes of Pseudomonas taetrolens. To investigate whether the four enzymes were the only lactose-oxidizing enzymes of P. taetrolens, we performed the inactivation of gcd1, gcd3, gcd4, and mqo1 genes in P.

Enhanced production of maltobionic acid by a metabolically engineered Escherichia coli incapable of maltose utilization.

To produce maltobionic acid (MBA) from maltose in Escherichia coli, we recombinantly expressed a glucose dehydrogenase gene (gdh1) from Enterobacter cloacae and a pyrroloquinoline quinone (PQQ) synthesis gene cluster (pqqFABCDEMIH) from Pseudomonas taetrolens. Although the recombinant E. coli strain (E.

Conversion of waste cooked rice into maltose by a Bacillus subtilis-derived maltogenic amylase and production of maltobionic acid from the prepared maltose using genetically modified Pseudomonas taetrolens.

In this study, we attempted to produce maltobionic acid (MBA) from waste cooked rice (WCR) using maltose as an intermediate. In our previous study, we produced maltose from WCR using a commercial maltogenic amylase (Maltogenase L). However, in the present study, we used wild-type Bacillus subtilis, which inherently produces maltogenic amylase (AmyE), instead of Maltogenase L to produce maltose from WCR.

Improving the Utilization of Food Waste: Conversion of Food Waste into Residual Food Dried Substance and Use of This Material as a Culture Nutrient for Microbial Production of Lactic Acid.

To reduce food waste (FW) disposal costs, many Koreans now convert FW into residual food dried substances (RFDS) using a house-service food drying machine and then dispose of the RFDS. To recycle RFDS, we tested whether RFDS could be used as a culture nutrient to produce value-added microbial chemicals. As a case study, we attempted to produce lactic acid (LA) by cultivating lactic acid bacteria using RFDS.

Production of lactobionic acid at high salt concentrations by Acinetobacter halotolerans isolated from seaside soil.

A lactobionic acid (LBA)-producing bacterium isolated from seaside soils was identified as Acinetobacter halotolerans and designated as strain KRICT-1. We determined whether KRICT-1 can produce LBA at high salt concentrations. The KRICT-1 strain grew on a nutrient broth (NB) agar plate with up to 7.

Efficient production of cellobionic acid using whole-cell biocatalyst of genetically modified Pseudomonas taetrolens.

Pseudomonas taetrolens has previously been shown to convert cellobiose to cellobionic acid (CBA), which can potentially be used in cosmetics, food, and pharmaceutical industries. The cellobiose-oxidizing activity of the P. taetrolens strain, which expressed the homologous quinoprotein glucose dehydrogenase (GDH), was increased by approximately 50.

Whole-cell biocatalysis using genetically modified Pseudomonas taetrolens for efficient production of maltobionic acid from pure maltose and high-maltose corn syrup.

Maltobionic acid (MBA) can be applied to various fields such as food, cosmetics, and pharmaceutical industries. In this study, whole-cell biocatalysis for MBA production was performed using recombinant Pseudomonas taetrolens homologously expressing quinoprotein glucose dehydrogenase (GDH). Various reaction parameters such as temperature, cell density, and cell harvest time, were optimized for improving MBA production.

Efficient Production of Lactobionic Acid Using Capable of Synthesizing Pyrroloquinoline Quinone.

Lactobionic acid (LBA) is an emerging chemical that has been widely utilized in food, cosmetic, and pharmaceutical industries. We sought to produce LBA using . LBA can be produced from lactose in , which is innately unable to produce LBA, by coexpressing a heterologous quinoprotein glucose dehydrogenase (GDH) and a pyrroloquinoline quinone (PQQ) synthesis gene cluster.

Efficient isolation of new lactobionic acid-producing microorganisms from environmental samples by colloidal calcium carbonate agar plate-based screening.

Lactobionic acid (LBA) has recently emerged as an important substance in various industries, such as cosmetics, foods, and pharmaceuticals. In this study, we developed a simple, efficient, and high-throughput method for screening LBA-producing microorganisms. First, an agar plate was prepared to isolate LBA-producing microorganisms by utilizing the property of LBA to solubilize colloidal calcium carbonate (CaCO), resulting in the formation of a clear halo around colonies on a nutrient broth agar plate containing CaCO.

Secretory production of an engineered cutinase in Bacillus subtilis for efficient biocatalytic depolymerization of polyethylene terephthalate.

Polyethylene terephthalate (PET) waste has caused serious environmental pollution. Recently, PET depolymerization by enzymes with PET-depolymerizing activity has received attention as a solution to recycle PET. An engineered variant of leaf-branch compost cutinase (293 amino acid), ICCG (Phe243Ile/Asp238Cys/Ser283Cys/Tyr127Gly), showed excellent depolymerizing activity toward PET at 72 °C, which was the highest depolymerizing activity and thermo-stability ever reported in previous works.

Isolation of new lactobionic acid-producing microorganisms and improvement of their production ability by heterologous expression of glucose dehydrogenase from Pseudomonas taetrolens.

Lactobionic acid (LBA) is a specialty organic acid that is widely employed in the food, cosmetic, and pharmaceutical industries. In the present study, we screened new LBA-producing bacteria from the soil of a poultry farm. Among the 700 bacterial colonies, five that exhibited LBA-producing ability were successfully isolated.

Identification of a lactose-oxidizing enzyme in Escherichia coli and improvement of lactobionic acid production by recombinant expression of a quinoprotein glucose dehydrogenase from Pseudomonas taetrolens.

Lactobionic acid (LBA), an aldonic acid prepared by oxidation of the free aldehyde group of lactose, has been broadly used in cosmetic, food, and pharmaceutical industries. Although Escherichia coli is unable to produce LBA naturally, a wild-type E. coli strain successfully produced LBA from lactose upon pyrroloquinoline quinone (PQQ) supplementation, indicating that E.

Enhancement of sophorolipids production in Candida batistae, an unexplored sophorolipids producer, by fed-batch fermentation.

Sophorolipids (SLs) from Candida batistae has a unique structure that contains ω-hydroxy fatty acids, which can be used as a building block in the polymer and fragrance industries. To improve the production of this industrially important SLs, we optimized the culture medium of C. batistae for the first time.

Valorization of waste-cooking oil into sophorolipids and application of their methyl hydroxyl branched fatty acid derivatives to produce engineering bioplastics.

Waste-cooking oil (WCO) is defined as vegetable oil that has been used to fry food at high temperatures. The annual global generation of WCO is 41-67 million tons. Without proper treatment, most WCO is abandoned in sinks and the solid residue of WCO is disposed of in landfills, resulting in serious environmental problems.

High-level production of maltobionic acid from high-maltose corn syrup by genetically engineered .

Maltobionic acid (MBA) has recently emerged as an important material in various industries. Here, we showed that quinoprotein glucose dehydrogenase (GDH) from could convert maltose into MBA by heterologously expressing this enzyme in MBA non-producing . We homologously expressed GDH in to improve intracellular maltose-oxidizing activity and MBA production.

Purification and Characterization of a Malate:Quinone Oxidoreductase from Capable of Producing Valuable Lactobionic Acid.

In this study, we successfully purified a novel lactose-oxidizing enzyme in for the first time. The purified enzyme was identified as malate:quinone oxidoreductase (MQO, EC 1.1.

Enhancement of Lactobionic Acid Productivity by Homologous Expression of Quinoprotein Glucose Dehydrogenase in .

This is the first study on improving lactobionic acid (LBA) production capacity in by genetic engineering. First, quinoprotein glucose dehydrogenase (GDH) was identified as the lactose-oxidizing enzyme of . Of the two types of GDH genes in , membrane-bound (GDH1) and soluble (GDH2), only GDH1 showed lactose-oxidizing activity.

Efficient production of lactobionic acid using genetically engineered Pseudomonas taetrolens as a whole-cell biocatalyst.

Lactobionic acid (LBA) has been widely used in the food, pharmaceutical, and cosmetic industries. Pseudomonas taetrolens is an efficient LBA-producing bacterium. To improve the LBA-production ability of P.

Efficient Itaconic acid production via protein-protein scaffold introduction between GltA, AcnA, and CadA in recombinant Escherichia coli.

Itaconic acid, which is a promising organic acid in synthetic polymers and some base-material production, has been produced by Aspergillus terreus fermentation at a high cost. The recombinant Escherichia coli that contained the cadA gene from A. terreus can produce itaconic acid but with low yield.

Manganese and cobalt recovery by surface display of metal binding peptide on various loops of OmpC in Escherichia coli.

In a cell-surface display (CSD) system, successful display of a protein or peptide is highly dependent on the anchoring motif and the position of the display in that anchoring motif. In this study, a recombinant bacterial CSD system for manganese (Mn) and cobalt (Co) recovery was developed by employing OmpC as an anchoring motif on three different external loops. A portion of Cap43 protein (TRSRSHTSEG) was employed as a manganese and cobalt binding peptide (MCBP), which was fused with OmpC at three different external loops.

Efficient Malic Acid Production in Escherichia coli Using a Synthetic Scaffold Protein Complex.

Recently, malic acid has gained attention due to its potential application in food, pharmaceutical, and medical industries. In this study, the synthetic scaffold complex strategy was employed between the two key enzymes pyruvate kinase (PykF) and malic enzyme (SfcA); SH3 ligand was attached to PykF, and the SH3 domain was attached to the C-terminus of ScfA. Synthetic scaffold systems can organize enzymes spatially and temporally to increase the local concentration of intermediates.

Enchancement of Gamma-Aminobutyric Acid Production by Co-Localization of Neurospora crassa OR74A Glutamate Decarboxylase with Escherichia coli GABA Transporter Via Synthetic Scaffold Complex.

Gamma-aminobutyric acid is a precursor of nylon-4, which is a promising heat-resistant biopolymer. GABA can be produced from the decarboxylation of glutamate by glutamate decarboxylase. In this study, a synthetic scaffold complex strategy was employed involving the Neurospora crassa glutamate decarboxylase (GadB) and GABA antiporter (GadC) to improve GABA production.