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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 beginning of the development of the amino acid industry can be put at 1908 when Kikunae Ikeda identified and isolated monosodium glutamate (MSG), the sodium salt of glutamic acid, as the flavoring agent in ‘kombu’, a traditional seasoning agent used in Japan, and derived from some marine algae. The following year, the Ajinomoto Company started producing MSG by extraction from the acid hydrolysate of wheat gluten or defatted soy. Glutamic acid, lysine, and methionine are the most produced amino acids globally.Protein hydrolysis: Protein hydrolysis was the original method of amino manufacture. Hair, keratin, blood meal, and feathers are hydrolyzed using acid and the amino acid extracted. Cysteine and cystine are still produced by isolating them from chemically hydrolyzed keratin protein in hair and feathers while proline and hydroxyproline are precipitated from gelatin hydrolysates.Chemical synthesis: Glycine, L-alanine, and DL-methionine are produced by chemical synthesis. Chemical synthesis can only produce the D, L-(racemic) forms of amino acids and an additional step involving the use of an immobilized enzyme, aminoacylase, produced by Aspergillus niger is necessary to obtain the biologically active L-form. This step is expensive and therefore few amino acids are prepared by chemical synthesis. Amino acids produced by chemical synthesis are glycine and methionine which is to have the same effect as an animal feed additive whether in the L- or in the D, L-form.Microbiological methods: Microbiological methods are of three types:Semi-fermentation;Use of microbial enzymes or immobilized cells;Direct fermentation.
Estimating the proportion of bioaccessible lead (BaPb) in household dust wipe samples: a comparison of IVBA and PBET methods
Published in Journal of Environmental Science and Health, Part A, 2023
Chandima Wekumbura, Ganga M. Hettiarachchi, Christina Sobin
Glycine is an important constituent of metabolic activities[58] and is also used as a buffering agent. Glycine at low concentrations prevents pH decrease in solutions.[59] When it is used at a significantly lower pH value it has a higher opportunity to regulate that pH. Therefore, when pH 1.5 is used with glycine buffer IVBA rarely exceeds the initial solution pH ± 0.5 after one hour of extraction time as restricted by the method.[43] Both, pH 1.5 and 2.5 with glycine were buffered the pH within this limit (±0.5) in the current study. Ruby et al.[15] adopted PBET from Miller et al.[60] which was originally developed for evaluating an in vitro method for estimation of iron availability from meals. Pepsin is the major constituent in PBET, the powerful enzyme in gastric juice that digests proteins within the normal gastric juice pH 1.5–2.5 when the presence of HCl. Acidification of the samples to pH 2 or 4 is important because pepsin begins to denature itself and thus will lose its activity at pH ≥ 5.[61] In several animal feeding studies, PBET 2.5 best represented bioaccessible lead concentration as compared to PBET pH 1.5 and 2.0.[44]
Insight into intermolecular interactions and hydration properties of biologically active amino acids in aqueous solutions of cefepime: volumetric, compressibility and viscometric studies
Published in Journal of Dispersion Science and Technology, 2021
Suvarcha Chauhan, Neetika Kumari, Lalita Pathania
The drug − protein interactions are generally difficult to study because of the complex structure of protein molecules. However, to reduce the degree of complexity, it is useful to investigate the solution behavior of model compounds such as amino acids, dipeptides etc. Drug can interact with these amino acids and small peptides to change the conformation of proteins either by stabilizing or destabilizing them. The recognition of drug-amino acid/peptide interactions in aqueous solution has always been a matter of interest.[3,4] Therefore, physico-chemical investigations are carried out for amino acids/peptides in aqueous solutions of different types of drugs. Among amino acids and peptides, glycine and glycylglycine have been chosen for the present study. Glycine is the simplest possible amino acid and is biosynthesized in the body from the amino acid serine.[5] It plays an important role in the body's production of DNA, phospholipids and collagen, and in release of energy besides acting as neurotransmitter. Glycylglycine is dipeptide made up of two glycine molecules joined by peptide linkage and is used in the synthesis of more complicated peptides.
Metabolomics approach to biomarkers of dry eye disease using 1H-NMR in rats
Published in Journal of Toxicology and Environmental Health, Part A, 2021
Jung Dae Lee, Hyang Yeon Kim, Jin Ju Park, Soo Bean Oh, Hyeyoon Goo, Kyong Jin Cho, Suhkmann Kim, Kyu-Bong Kim
Glycine, a major amino acid in mammals is synthesized by serine and threonine through hepatic metabolism. Urinary glycine was increased and threonine was reduced (Figure 8). Glycine is known to be used in the treatment of metabolic disorders involving several inflammatory diseases (Wang et al. 2013). The symptoms associated with DED induced by scopolamine include elevated glycine levels, suggested that the proinflammatory cytokines TNF-α, IL-1β, and IL-6 play a role. However, Spittler et al. (1999) reported that glycine inhibited the production of proinflammatory cytokines including TNF-α, IL-1β, and IL-6. Our findings displayed different tendencies, which may be attributed to different factors.