Microbial Control Using Engineered Poly-γ-glutamate-Based Materials
نویسندگان
چکیده
منابع مشابه
Microbial production and chemical transformation of poly-γ-glutamate
Poly-γ-glutamate (PGA), a novel polyamide material with industrial applications, possesses a nylon-like backbone, is structurally similar to polyacrylic acid, is biodegradable and is safe for human consumption. PGA is frequently found in the mucilage of natto, a Japanese traditional fermented food. To date, three different types of PGA, namely a homo polymer of D-glutamate (D-PGA), a homo polym...
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Poly-γ-glutamate (PGA) possesses a nylon-like backbone and polyacrylate-like carboxyl groups, and shows an extraordinary solubility in water. In this study, the effective synthesis and structural analysis of some water-insoluble PGA ion-complexes (PGAICs) using cationic surfactants, hexadecylpyridinium (HDP), dodecylpyridinium, benzalkonium and benzetonium, were examined. We demonstrated their ...
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Poly-γ-glutamic acid (γ-PGA) is a natural, biodegradable and water-soluble biopolymer of glutamic acid. This review is focused on nonrecombinant microbial production of γ-PGA via fermentation processes. In view of its commercial importance, the emphasis is on L-glutamic acid independent producers (i.e. microorganisms that do not require feeding with the relatively expensive amino acid L-glutami...
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The stability, persistence and dynamics of the peptide secondary motifs are investigated in a series of poly(γ-benzyl-L-glutamate)-b-polyalanine (PBLG-b-PAla) polypeptides through a combination of structural (X-rays, NMR) and dynamic (Dielectric Spectroscopy, NMR) probes. The unfavorable enthalpic interactions between the unlike blocks give rise to nanophase separation that results in the desta...
متن کاملPivotal Enzyme in Glutamate Metabolism of Poly-γ-Glutamate-Producing Microbes
The extremely halophilic archaeon Natrialba aegyptiaca secretes the L-homo type of poly-g-glutamate (PGA) as an extremolyte. We examined the enzymes involved in glutamate metabolism and verified the presence of L-glutamate dehydrogenases, L-aspartate aminotransferase, and L-glutamate synthase. However, neither glutamate racemase nor D-amino acid aminotransferase activity was detected, suggestin...
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ژورنال
عنوان ژورنال: Japanese Journal of Food Microbiology
سال: 2018
ISSN: 1340-8267,1882-5982
DOI: 10.5803/jsfm.35.116