Enzymatic Preparation of Supramolecular Networks Composed of Amylosic Inclusion Complexes with Grafted Guest Polymers. Issue 9 (26th April 2019)
- Record Type:
- Journal Article
- Title:
- Enzymatic Preparation of Supramolecular Networks Composed of Amylosic Inclusion Complexes with Grafted Guest Polymers. Issue 9 (26th April 2019)
- Main Title:
- Enzymatic Preparation of Supramolecular Networks Composed of Amylosic Inclusion Complexes with Grafted Guest Polymers
- Authors:
- Kadokawa, Jun-ichi
Tanaka, Kazuya
Yamamoto, Kazuya - Abstract:
- Abstract : In this study, we attempted to prepare supramolecular networks composed of amylosic inclusion complexes with grafted guest polymers by means of phosphorylase-catalyzed enzymatic polymerization of α-d -glucose 1-phosphate as a monomer from a maltooligosaccharide primer. When the enzymatic polymerization was examined in the presence of poly(γ-glutamic acid- graft -tetrahydrofuran) (PGA- g -PTHF), the reaction mixture totally turned into a hydrogel form. The powder X-ray diffraction measurement of a lyophilized sample of the hydrogel suggested that enzymatically elongated amyloses formed inclusion complexes with the PTHF graft chains among the PGA main-chains according to vine-twining polymerization manner to construct the supramolecular network structure. Therefore, the product formed the hydrogel with inclusion complex cross-linking as the enzymatic polymerization progressed. The vine-twining polymerization is the method for the formation of amylose-polymer inclusion complexes in the phosphorylase-catalyzed enzymatic polymerization field, which has been previously developed by us. On the other hand, the enzymatic polymerization mixture in the presence of poly(γ-glutamic acid- graft -l -lactic acid) (PGA- g -PLLA) did not induce the hydrogel formation upon the same operation. In this system, enzymatically elongated amyloses did not form inclusion complexes with the PLLA graft chains due to their bulkiness, but sorely constructed well-known double helical assemblies,Abstract : In this study, we attempted to prepare supramolecular networks composed of amylosic inclusion complexes with grafted guest polymers by means of phosphorylase-catalyzed enzymatic polymerization of α-d -glucose 1-phosphate as a monomer from a maltooligosaccharide primer. When the enzymatic polymerization was examined in the presence of poly(γ-glutamic acid- graft -tetrahydrofuran) (PGA- g -PTHF), the reaction mixture totally turned into a hydrogel form. The powder X-ray diffraction measurement of a lyophilized sample of the hydrogel suggested that enzymatically elongated amyloses formed inclusion complexes with the PTHF graft chains among the PGA main-chains according to vine-twining polymerization manner to construct the supramolecular network structure. Therefore, the product formed the hydrogel with inclusion complex cross-linking as the enzymatic polymerization progressed. The vine-twining polymerization is the method for the formation of amylose-polymer inclusion complexes in the phosphorylase-catalyzed enzymatic polymerization field, which has been previously developed by us. On the other hand, the enzymatic polymerization mixture in the presence of poly(γ-glutamic acid- graft -l -lactic acid) (PGA- g -PLLA) did not induce the hydrogel formation upon the same operation. In this system, enzymatically elongated amyloses did not form inclusion complexes with the PLLA graft chains due to their bulkiness, but sorely constructed well-known double helical assemblies, resulting in their aggregation in the reaction mixture. … (more)
- Is Part Of:
- Journal of the Electrochemical Society. Volume 166:Issue 9(2019)
- Journal:
- Journal of the Electrochemical Society
- Issue:
- Volume 166:Issue 9(2019)
- Issue Display:
- Volume 166, Issue 9 (2019)
- Year:
- 2019
- Volume:
- 166
- Issue:
- 9
- Issue Sort Value:
- 2019-0166-0009-0000
- Page Start:
- B3171
- Page End:
- B3175
- Publication Date:
- 2019-04-26
- Subjects:
- Surface Science -- Amylose -- Enzymatic polymerization -- Supramolecular network
Electrochemistry -- Periodicals
541.3705 - Journal URLs:
- https://iopscience.iop.org/journal/1945-7111?gclid=EAIaIQobChMI4Y-UmqGC7wIVFeDtCh0VQAo7EAAYASAAEgLW8_D_BwE ↗
- DOI:
- 10.1149/2.0311909jes ↗
- Languages:
- English
- ISSNs:
- 0013-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library HMNTS - ELD Digital store
- Ingest File:
- 15511.xml