Production of glutaric acid from 5-aminovaleric acid using Escherichia coli whole cell bio-catalyst overexpressing GabTD from Bacillus subtilis.

Glutaric acid is one of the promising C5 platform compounds in the biochemical industry. It can be produced chemically, through the ring-opening of butyrolactone followed by hydrolysis. Alternatively, glutaric acid can be produced via lysine degradation pathways by microorganisms.

Functional Study of Lysine Decarboxylases from Klebsiella pneumoniae in Escherichia coli and Application of Whole Cell Bioconversion for Cadaverine Production.

Klebsiella pneumoniae is a gram-negative, non-motile, rod-shaped, and encapsulated bacterium in the normal flora of the intestines, mouth, skin, and food, and has decarboxylation activity, which results in generation of diamines (cadaverine, agmatine, and putrescine). However, there is no specific information on the exact mechanism of decarboxylation in K. pnuemoniae.

Whole Cell Bioconversion of Ricinoleic Acid to 12-Ketooleic Acid by Recombinant Corynebacterium glutamicum-Based Biocatalyst.

The biocatalytic efficiency of recombinant Corynebacterium glutamicum ATCC 13032 expressing the secondary alcohol dehydrogenase of Micrococcus luteus NCTC2665 was studied. Recombinant C. glutamicum converts ricinoleic acid to a product, identified by gas chromatography/mass spectrometry as 12-ketooleic acid (12-oxo-cis-9-octadecenoic acid).

Batch and fed-batch production of coenzyme Q10 in recombinant Escherichia coli containing the decaprenyl diphosphate synthase gene from Gluconobacter suboxydans.

Coenzyme Q(10) (CoQ(10)) is a quinine consisting of ten units of the isoprenoid side-chain. Because it limits the oxidative attack of free radicals to DNA and lipids, CoQ(10) has been used as an antioxidant for foods, cosmetics and pharmaceuticals. Decaprenyl diphosphate synthase (DPS) is the key enzyme for synthesis of the decaprenyl tail in CoQ(10) with isopentenyl diphosphate.

Bioelectronic device consisting of cytochrome c/poly-L-aspartic acid adsorbed hetero-Langmuir-Blodgett films.

A bioelectronic device consisting of protein-adsorbed hetero-Langmuir-Blodgett (LB) films was investigated. Four kinds of functional molecules, cytochrome c, viologen, flavin, and ferrocene, were used as a secondary electron acceptor (A2), a first electron acceptor (A1), a sensitizer (S), and an electron donor (D), respectively. To fabricate the cytochrome c adsorbed hetero-LB film, poly-L-aspartic acid was used as the bridging molecule.