China
Africa
Explore chapters and articles related to this topic
Amino Acids and Vitamin Production
Published in Debabrata Das, Soumya Pandit, Industrial Biotechnology, 2021
Glutamic acid is an alpha-amino acid which has two carboxyl group -COOH and one amino acid group. Glutamic acid can also act as an excitatory neurotransmitter and serves as the precursor for the synthesis of the inhibitory gamma-aminobutyric acid (GABA). It can exist in two optical isomers i.e. D (-) and L(+) form. The L form is the form that occurs most widely in nature whereas the D form exists in a few contexts such as in cell walls of bacteria. Glutamic acid is a non-essential amino acid (i.e. the body can synthesize it) which is used for protein synthesis as well as a flavour enhancer in various food products. Glutamic acid was the first amino acid which was discovered and manufactured by a Japanese researcher Kikunae Ikeda of the Tokyo Imperial University in the year 1908. He identified and isolated the brown crystals which were left due to evaporation of kombu broth and thus MSG or monosodium glutamate (flavour enhancer) was found. Professor Ikeda termed the flavour umami. He then patented a method of mass-producing a crystalline salt of glutamic acid, MSG. It is produced on a large scale with an estimated annual production of approximately 1.5 million tons or even more (Bender, 2012).
Microbial Biosensors
Published in Loïc J. Blum, Pierre R. Coulet, Biosensor Principles and Applications, 2019
I. Karube, M. E. SangMok Chang
Glutamic acid is produced by a fermentation process and is used as a seasoning for foods. A rapid and automatic method is required for determination of its concentration. Glutamate decarboxylase catalyzes the decarboxylation of glutamic acid, producing carbon dioxide and amine. Enzyme-based autoanalyzers can therefore be used, but the enzyme is expensive and unstable. Certain microorganisms, however, contain glutamate decarboxylase.
Production of Amino Acids by Fermentation
Published in Nduka Okafor, Benedict C. Okeke, Modern Industrial Microbiology and Biotechnology, 2017
Nduka Okafor, Benedict C. Okeke
The production of amino acids by fermentation was stimulated by the discovery of an efficient L-glutamic acid producer Corynebacterium glutamicum. Many microorganisms have been reported to produce amino acids. The four most widely reported bacteria belong to the following four genera, the typical species of which are given in parenthesis:Corynebacterium spp. (C. glutamicum; C. lilium)Brevibacterium spp. (B. divericartum: B. alanicum)Microbacterium spp. (M. flavum var. glutamicum)Arthrobacter spp. (A. globiformis; A. aminofaciens)
Kinetic process of the biosorption of Cu(II), Ni(II) and Cr(VI) by waste Pichia pastoris cells
Published in Environmental Technology, 2023
Kaiyan Zhou, Yulu Zhou, Hongbo Zhou, Haina Cheng, Gang Xu
Figure 19 shows the TEM image of Cu(II)-loaded waste P.pastoris in micrographic structure. In general, yeast cells exhibit cell-to-cell aggregation in solution due to the binding of Ca(II) to lectins [32,91,95]. The C-terminal of lectins containing the amino acid sequence glutamic acid, proline and glutamine, as the Ca(II) binding site, to form flocculations [96]. And these amino acid residues exist –NH2, -COOH and NH–C=O groups, which also generate stretching vibrations in FTIR spectrum. And besides the present SEM-EDS results about the decrease of Ca(II) content in the Cu(II) adsorption process, the phenomenon of flocculation was non-existent between Cu(II)-loaded waste P.pastoris cells in Figure 19(a). The above findings implied that Cu(II) occupied the Ca(II) binding sites in the lectins [87,95], thus removing the intercellular flocculation and thus facilitating the adsorption of heavy metals, i.e. the effect of electrostatic repulsion is weak between Cu(II) and Ca(II) on Cu(II) adsorption and is beneficial for ion exchanges [28]. In addition, as shown in Figure 19(b, c), nitrogen elements of floccule in the red circle of white area distributed more intensive, and it indicated the presence of biological macromolecules such as proteins and polysaccharides. Meanwhile Cu(II) also distributed more densely in the nitrogen-intensive region as observed. In the light of FTIR and XRD results, it can be concluded that Cu(II) bond with -NH and -OH groups of biological macromolecules, causing the phase change of waste P.pastoris.
Exogenous Hemin alleviates cadmium stress in maize by enhancing sucrose and nitrogen metabolism and regulating endogenous hormones
Published in International Journal of Phytoremediation, 2023
Meng Zhao, Yao Meng, Yong Wang, Guangyan Sun, Xiaoming Liu, Jing Li, Shi Wei, Wanrong Gu
Glutamic acid (Glu) can be used as a source of C and N for most other biosynthesis (Meng 2015; Qu et al. 2019). Exogenous substances can improve the activities of GS, GOGAT and GDH under heavy metal stress (Wang 2017). Hemin increased the activities of GS, GOGAT and GDH in maize seedlings under cadmium stress. So exogenous Hemin could enhance the assimilation of NH4+ and alleviate the toxicity of NH4+ by increasing the activity of ammonia assimilation enzyme. In this study, cadmium stress reduced activities of GS, GOGAT and GDH in leaves. The activities of GS, GOGAT and GDH of maize varieties with different cadmium resistance were different. Glutamic acid (Glu) can be used as a source of C and N for biosynthesis. Glu can be transformed into Asp and Ala by GOT and GPT pathways. In this study, the activities of GOT and GPT in Fenghe 6 were significantly lower than those in Tiannong 9. GS/GOGAT pathway was weakened and Glu content in tissues was significantly decreased under cadmium stress, which inhibited the amino transfer reaction with Glu as the substrate. The results showed that exogenous Hemin could enhance the metabolism of amino acids in plants, and then enhance the ability of tolerance to cadmium stress.
Investigation of mutations (L41F, F17M, N57E, Y99F_Y134W) effects on the TolAIII-UnaG fluorescence protein's unconjugated bilirubin (UC-BR) binding ability and thermal stability properties
Published in Preparative Biochemistry & Biotechnology, 2022
Numan Eczacioglu, Yakup Ulusu, İsa Gokce, Jeremy H. Lakey
Kumagai et al. (2013) reported that the glutamine (Q) and alanin (A) mutations in asparagine (N57) are important for bilirubin binding and also serine (S80) is located in the bilirubin binding region.[3] One of the three direct hydrogen bonds between the endo-vinyl dipyrrinone structure of UC-BR and UnaG is partially provided by the N57 side chains with average distances of 2.9 Å pyrrole ring A and 3.0 Å pyrrole ring B.[14] According to the possible configuration of UnaG, the point where the N57 and S80 are located in the loops region oppositely. Through careful analysis of the sequence, it was found that these loops formed as a result of electrostatic bridges formed between positively and negatively charged residues. Asparagine, like all other amino acids, makes the peptide bond from the amino and carboxyl groups. It can make hydrogen bonds with amino groups on the radical group. Electron donor groups in asparagine resonate with their electrons. The carboxylic acid group was formed by replacing asparagine with glutamic acid. Glutamic acid can make strong hydrogen bonds and electrostatic interaction with bilirubin thanks to carboxylic acid groups. As a result of the UnaGN57E mutation, a group able to make a much stronger hydrogen bond was added and the intermolecular interaction was increased through the hydrogen bond and the Kd value of the new mutant (N57E) was decreased.