Download Amino-Acid Homopolymers Occurring in Nature by Munenori Takehara, Hideo Hirohara (auth.), Yoshimitsu Hamano PDF

By Munenori Takehara, Hideo Hirohara (auth.), Yoshimitsu Hamano (eds.)

Microorganisms are able to generating a large choice of biopolymers. Homopolymer peptides, that are made from just a unmarried kind of amino acid, are a long way much less ubiquitous. the one amino-acid homopolymers identified to take place in nature are offered during this quantity. Poly-epsilon-L-lysine is a polycationic peptide and shows antimicrobial job opposed to a large spectrum of microorganisms. it's either secure and biodegradable and is for this reason used as a foodstuff preservative in numerous nations. moreover, there was nice curiosity in scientific and different purposes of poly-lysine and its derivatives. by contrast, poly-gamma-glutamic acid is an strange anionic polypeptide. it's also water soluble, biodegradable, suitable for eating, non-toxic and non-immunogenic and will be chemically transformed to introduce quite a few medicinal drugs. those beneficial properties are very valuable for pharmaceutical and biomedical functions. Poly-glutamic acid can also be a hugely beautiful as nutrients ingredient.

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Agric Biol Chem 41:1807–1809 Shima S, Sakai H (1981a) Poly-L-lysine produced by Streptomyces. II. Taxonomy and fermentation studies. Agric Biol Chem 45:2497–2502 Shima S, Sakai H (1981b) Poly-L-lysine produced by Streptomyces. III. Chemical studies. Agric Biol Chem 45:2503–2508 Shima S, Matsuoka H, Sakai H (1982) Inactivation of bacteriophages by e-poly-L-lysine produced by Streptomyces. Agric Biol Chem 46:1917–1919 Shima S, Oshima S, Sakai H (1983) Biosynthesis of e-poly-L-lysine by washed mycelium of Streptomyces albulus No.

J Bacteriol 172:4690–4693 44 Y. Hamano Zhang JJ, Hu FM, Chen NY, Paulus H (1990) Comparison of the three aspartokinase isozymes in Bacillus subtilis Marburg and 168. J Bacteriol 172:701–708 Zhang W, Jiang W, Zhao G, Yang Y, Chiao J (1999) Sequence analysis and expression of the aspartokinase and aspartate semialdehyde dehydrogenase operon from rifamycin SV-producing Amycolatopsis mediterranei. Gene 237:413–419 Zhang WW, Jiang WH, Zhao GP, Yang YL, Chiao JS (2000) Expression in Escherichia coli, purification and kinetic analysis of the aspartokinase and aspartate semialdehyde dehydrogenase from the rifamycin SV-producing Amycolatopsis mediterranei U32.

5 Substrate Specificity of Pls . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 35 4 Concluding Remarks and Future Perspectives . . . . . . . . . . . . . . . . . . . . . . . 38 References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 42 Abstract Streptomyces albulus NBRC14147 (previously named IFO14147) is known to produce the amino-acid homopolymer antibiotic, poly-e-L-lysine (e-polyL-lysine, e-PL), consisting of 25–35 L-lysine residues with a linkage between the a-carboxyl group and the e-amino group.

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