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Kenji Soda

Researcher at Kansai University

Publications -  188
Citations -  5613

Kenji Soda is an academic researcher from Kansai University. The author has contributed to research in topics: Enzyme & Pyridoxal. The author has an hindex of 41, co-authored 188 publications receiving 5390 citations. Previous affiliations of Kenji Soda include Kyoto University.

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A Cold-Adapted Lipase of an Alaskan Psychrotroph,Pseudomonas sp. Strain B11-1: Gene Cloning and Enzyme Purification and Characterization

TL;DR: The enzyme showed a 1,3-positional specificity toward triolein and was stable between pH 6 and 9, and the optimal pH for the enzymatic hydrolysis of tributyrin was around 8.2, while the enzyme was unstable at temperatures higher than 45°C.
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Natural and edible biopolymer poly‐γ‐glutamic acid: synthesis, production, and applications

TL;DR: In this paper, a review of the production of a strain of polyγ-glutamic acid and recent developments with respect to applications in terms of Ca absorption, moisturizing properties, γ-PGA conjugation, super absorbent polymer, and so on is presented.
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A new antitumor enzyme, L-lysine alpha-oxidase from Trichoderma viride. Purification and enzymological properties.

TL;DR: L-Lysine alpha-oxidase from Trichoderma viride Y244-2 has been purified to homogeneity and several lysine analogs such as delta-hydroxylysine are oxidized efficiently.
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A poly-gamma-glutamate synthetic system of Bacillus subtilis IFO 3336: gene cloning and biochemical analysis of poly-gamma-glutamate produced by Escherichia coli clone cells.

TL;DR: Three genes encoding a poly-gamma-glutamate synthetic system of Bacillus subtilis IFO 3336 (Bacillus natto) were cloned and expressed in Escherichia coli, resulting in a higher polymer yield and co-expression of glutamate racemase gene in E. coli cells harboring pgsBCA genes increased both the polymer production and D-glUTamate content in the polymer.
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Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity.

TL;DR: There are some striking similarities between the active sites of D-AAT and the corresponding enzyme that transaminates L-amino acids, L-aspartate aminotransferase that represent convergent evolution to a common solution of the problem of enforcing transamination chemistry on the PLP cofactor.