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Chemoenzyamtic synthesis and self-assembling gelation behavior of amylose-grafted poly(γ-glutamic acid)

Authors :
Takuya Shouji
Jun-ichi Kadokawa
Kazuya Yamamoto
Source :
International Journal of Biological Macromolecules. 97:99-105
Publication Year :
2017
Publisher :
Elsevier BV, 2017.

Abstract

In this study, we investigated chmemoenzymatic synthesis of amylose-grafted poly(γ-glutamic acid) (PGA) as a new artificial saccharide-peptide conjugate composed of two biological macromolecules. Maltooligosaccharide as a primer of enzymatic polymerization by phosphorylase catalysis was first introduced on the PGA main chain by the condensation reaction using the condensing agent in NaOH aq. Thermostable phosphorylase-catalyzed enzymatic polymerization of α-d-glucose 1-phosphate (G-1-P) as a monomer was then performed from the primer chain ends of the product to obtain amylose-grafted PGAs, which formed hydrogels in reaction media depending on the G-1-P/primer feed ratios. The powder X-ray diffraction patterns of lyophilized samples (cryogels) from the hydrogels suggested that the amylose graft chains formed double helixes, which acted as cross-inking points for self-assembling hydrogelation. The scanning electron microscopic images of the cryogels showed regularly controlled porous morphologies. Moreover, pore sizes of the cryogels increased with increasing the G-1-P/primer feed ratios, whereas the degrees of substitution of primer on the PGA main chain did not obviously affect pore sizes.

Details

ISSN :
01418130
Volume :
97
Database :
OpenAIRE
Journal :
International Journal of Biological Macromolecules
Accession number :
edsair.doi.dedup.....7ae1c79226a749a3fa0ebdb331304ec7
Full Text :
https://doi.org/10.1016/j.ijbiomac.2017.01.001