462-94-2Relevant articles and documents
The use of l-lysine decarboxylase as a means to separate amino acids by electrodialysis
Teng, Yinglai,Scott, Elinor L.,Van Zeeland, Albert N. T.,Sanders, Johan P. M.
, p. 624 - 630 (2011)
Amino acids (AA's) are interesting materials as feedstocks for the chemical industry as they contain chemical functionalities similar to conventional petrochemicals. This offers the possibility to circumvent process steps, energy and reagents. AA's can be obtained by the hydrolysis of potentially inexpensive voluminous protein streams derived from biofuel production. However, isolation of the preferred AA is required in order to carry out further transformation into the desired product. Theoretically separation may be achieved using electrodialysis. To increase efficiency, specific modification to a product of industrial interest and removes charged groups of AA's with similar isoelectric points is required. Here, the reaction of l-lysine decarboxylase (LDC) was studied as a means to specifically convert l-lysine (Lys) to 1,5-pentanediamine (PDA) in the presence of l-arginine (Arg) to produce products with different charge thus allowing isolation of products by electrodialysis. Immobilization of LDC in calcium alginate enhanced the operational stability and conversion in mixtures of amino acids was highly specific. At 30 °C the presence of Arg had little effect on the activity of the enzyme although inhibition by the product PDA could be observed. Volumetric productivity was calculated and raw material and transformation costs were estimated for a potential process using a mixture of Arg and Lys. The Royal Society of Chemistry.
Advances in bio-nylon 5X: Discovery of new lysine decarboxylases for the high-level production of cadaverine
Xue, Yaju,Zhao, Yongliang,Ji, Xiuling,Yao, Jiahao,Busk, Peter Kamp,Lange, Lene,Huang, Yuhong,Zhang, Suojiang
, p. 8656 - 8668 (2020)
Cadaverine (1,5-pentanediamine) is the most important precursor for nylon PA5X, which has an extremely competitive market due to the high consumption of engineered plastics and fibers. The key enzyme lysine decarboxylase is in desperate need for industrial bio-based cadaverine production. In this study, new lysine decarboxylases have been mined by peptide pattern recognition for the high-level production of cadaverine. The predicted enzymes were expressed in E. coli and analyzed as whole-cell biocatalysts. Two outstanding recombinant enzymes from Edwardsiella tarda and Aeromonas sp. (LdcEt and LdcAer, respectively), were further purified and characterized. The optimal pH and temperature for LdcEt and LdcAer were pH 7, 55 °C and pH 6, 50 °C, respectively. These two enzymes were stable over the pH range of 5-7 during 24 h incubation. Both of them still had activity after being incubated at pH 8. LdcEt and LdcAer also have good thermostability with a half-life of 14.5 h and 20.3 h at 60 °C, respectively. The kinetic analysis showed that they have high catalytic efficiency as the kcat/Km (LdcEt: 243.28 s-1 mM-1; LdcAer: 266.86 s-1 mM-1) was the highest when compared for all the related studies. The whole cell conversion by LdcEt with 0.1% (v/v) Triton X-100 can convert 100% 2 M l-lysine HCl to cadaverine in 2 h and the cadaverine productivity was high up to 103.47 ± 4.37 g L-1 h-1. The in vitro studies further found that unpurified cell-lysates of LdcEt had relatively higher activity compared to the whole cell conversion. Meanwhile, 0.4 mg mL-1 purified LdcEt and LdcAer can efficiently produce 165.96 ± 1.41 g L-1 and 155.84 ± 4.63 g L-1 cadaverine only in 0.5 h, respectively. The high specific activity, pH, thermo-stability, and catalytic efficiency in vivo and in vitro, combined with simultaneous cell treatment with Triton X-100 and the bioconversion process, provide LdcEt with great potential in the economic and efficient production of cadaverine at the industrial scale. This journal is
Supramolecular Assays for Mapping Enzyme Activity by Displacement-Triggered Change in Hyperpolarized 129Xe Magnetization Transfer NMR Spectroscopy
Schnurr, Matthias,Sloniec-Myszk, Jagoda,D?pfert, J?rg,Schr?der, Leif,Hennig, Andreas
, p. 13444 - 13447 (2015)
Reversibly bound Xe is a sensitive NMR and MRI reporter with its resonance frequency being influenced by the chemical environment of the host. Molecular imaging of enzyme activity presents a promising approach for disease identification, but current Xe biosensing concepts are limited since substrate conversion typically has little impact on the chemical shift of Xe inside tailored cavities. Herein, we exploit the ability of the product of the enzymatic reaction to bind itself to the macrocyclic hosts CB6 and CB7 and thereby displace Xe. We demonstrate the suitability of this method to map areas of enzyme activity through changes in magnetization transfer with hyperpolarized Xe under different saturation scenarios. The supramolecular recognition properties of cucurbiturils are exploited in a modified signal-transfer approach in Xe NMR spectroscopy. Magnetic resonance imaging of enzymatic reactions was possible in this way by displacement of hyperpolarized 129Xe.
Preparation method of pentamethylene diamine
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Paragraph 0042; 0045; 0052-0057; 0064-0066, (2021/11/27)
The invention provides a preparation method of pentamethylene diamine. The method comprises the following steps: a) reacting acrylonitrile with acetaldehyde under the catalytic action of N,N-dihydroxyethyl-1,4-pentamethylene diamine to obtain 5-formyl valeronitrile; and b) carrying out one-step reaction on the product obtained in the step a) and mixed gas of ammonia gas and hydrogen under the action of a catalyst and an auxiliary agent to obtain pentamethylene diamine. Compared with the traditional method for synthesizing pentamethylene diamine by using lysine as a raw material and a biological method, the method has the advantages of simple steps and low cost, and is suitable for large-scale production of pentamethylene diamine. The use of the catalyst N,N-dihydroxyethyl-1,4-pentamethylene diamine can inhibit the self-polymerization of acetaldehyde and acrylonitrile, thereby greatly enhancing the selectivity of the target intermediate.
MODIFIED MEMBRANE PERMEABILITY
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, (2019/02/13)
Provided are microorganisms genetically modified to overexpress porin polypeptides to enhance the production of lysine and lysine derivatives by the microorganism. Also provided are methods of generating such microorganism, and methods of producing lysine and lysine derivatives using the genetically modified microorganisms.
