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Formation of microparticles from amylose-grafted poly(γ-glutamic acid) networks obtained by thermostable phosphorylase-catalyzed enzymatic polymerization

Amylose is a natural polysaccharide with helical conformation, which spontaneously forms water-insoluble assemblies, such as double helixes and inclusion complexes, at ambient temperatures in aqueous media, whereas it is synthesized as a water-soluble single chain by thermostable phosphorylase-catal...

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Autores principales: Kadokawa, Jun-ichi, Orio, Saya, Yamamoto, Kazuya
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9064375/
https://www.ncbi.nlm.nih.gov/pubmed/35521363
http://dx.doi.org/10.1039/c9ra02999k
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author Kadokawa, Jun-ichi
Orio, Saya
Yamamoto, Kazuya
author_facet Kadokawa, Jun-ichi
Orio, Saya
Yamamoto, Kazuya
author_sort Kadokawa, Jun-ichi
collection PubMed
description Amylose is a natural polysaccharide with helical conformation, which spontaneously forms water-insoluble assemblies, such as double helixes and inclusion complexes, at ambient temperatures in aqueous media, whereas it is synthesized as a water-soluble single chain by thermostable phosphorylase-catalyzed enzymatic polymerization at elevated temperatures in aqueous buffer solvents. In this study, we investigated the enzymatic polymerization at 80 °C using a primer-grafted poly(γ-glutamic acid) (PGA) in the presence or absence of poly(l-lactic acid) (PLLA) as a guest polymer for inclusion by amylose. Consequently, the produced amylose-grafted PGAs formed microparticles by cooling the mixtures at room temperature after the enzymatic polymerization in either the presence or the absence of PLLA. The particle sizes, which were evaluated by SEM measurement, were dependent on the feed ratios of PLLA. Based on the characterization results by the powder X-ray diffraction, IR, and dynamic light scattering measurements, a mechanism for the formation of the microparticles in the present system is proposed.
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spelling pubmed-90643752022-05-04 Formation of microparticles from amylose-grafted poly(γ-glutamic acid) networks obtained by thermostable phosphorylase-catalyzed enzymatic polymerization Kadokawa, Jun-ichi Orio, Saya Yamamoto, Kazuya RSC Adv Chemistry Amylose is a natural polysaccharide with helical conformation, which spontaneously forms water-insoluble assemblies, such as double helixes and inclusion complexes, at ambient temperatures in aqueous media, whereas it is synthesized as a water-soluble single chain by thermostable phosphorylase-catalyzed enzymatic polymerization at elevated temperatures in aqueous buffer solvents. In this study, we investigated the enzymatic polymerization at 80 °C using a primer-grafted poly(γ-glutamic acid) (PGA) in the presence or absence of poly(l-lactic acid) (PLLA) as a guest polymer for inclusion by amylose. Consequently, the produced amylose-grafted PGAs formed microparticles by cooling the mixtures at room temperature after the enzymatic polymerization in either the presence or the absence of PLLA. The particle sizes, which were evaluated by SEM measurement, were dependent on the feed ratios of PLLA. Based on the characterization results by the powder X-ray diffraction, IR, and dynamic light scattering measurements, a mechanism for the formation of the microparticles in the present system is proposed. The Royal Society of Chemistry 2019-05-23 /pmc/articles/PMC9064375/ /pubmed/35521363 http://dx.doi.org/10.1039/c9ra02999k Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Kadokawa, Jun-ichi
Orio, Saya
Yamamoto, Kazuya
Formation of microparticles from amylose-grafted poly(γ-glutamic acid) networks obtained by thermostable phosphorylase-catalyzed enzymatic polymerization
title Formation of microparticles from amylose-grafted poly(γ-glutamic acid) networks obtained by thermostable phosphorylase-catalyzed enzymatic polymerization
title_full Formation of microparticles from amylose-grafted poly(γ-glutamic acid) networks obtained by thermostable phosphorylase-catalyzed enzymatic polymerization
title_fullStr Formation of microparticles from amylose-grafted poly(γ-glutamic acid) networks obtained by thermostable phosphorylase-catalyzed enzymatic polymerization
title_full_unstemmed Formation of microparticles from amylose-grafted poly(γ-glutamic acid) networks obtained by thermostable phosphorylase-catalyzed enzymatic polymerization
title_short Formation of microparticles from amylose-grafted poly(γ-glutamic acid) networks obtained by thermostable phosphorylase-catalyzed enzymatic polymerization
title_sort formation of microparticles from amylose-grafted poly(γ-glutamic acid) networks obtained by thermostable phosphorylase-catalyzed enzymatic polymerization
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9064375/
https://www.ncbi.nlm.nih.gov/pubmed/35521363
http://dx.doi.org/10.1039/c9ra02999k
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