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

Abstract

Thermostable phosphorylase-catalyzed enzymatic polymerization at 80 °C using a primer-grafted poly(γ-glutamic acid), followed by cooling at room temperature, induced the formation of microparticles.

Preparation of Amylose-Oligo[(R)-3-hydroxybutyrate] Inclusion Complex by Vine-Twining Polymerization

“…The mixture was maintained at 70 °C for 48 h; we have already confirmed that such elevated reaction temperatures in the thermostable GP-catalyzed enzymatic polymerization do not affect the chemical structure of the produced amylose [13,23]. Subsequently, to We then attempted to obtain the inclusion complex from ORHB by enzymatic production through the formation of water-soluble amylose without a double-helical assembly, called single amylose, at elevated temperatures (Scheme 1) [13]. The thermostable GPcatalyzed enzymatic polymerization of G-1-P from a maltotriose (G 3 ) primer (80:1) was conducted in the presence of ORHB (MW = 530) dispersed in an acetate buffer solvent.…”

“…The thermostable GPcatalyzed enzymatic polymerization of G-1-P from a maltotriose (G3) primer (80:1) was conducted in the presence of ORHB (MW = 530) dispersed in an acetate buffer solvent. The mixture was maintained at 70 °C for 48 h; we have already confirmed that such elevated reaction temperatures in the thermostable GP-catalyzed enzymatic polymerization do not affect the chemical structure of the produced amylose [13,23]. Subsequently, to We then attempted to obtain the inclusion complex from ORHB by enzymatic production through the formation of water-soluble amylose without a double-helical assembly, called single amylose, at elevated temperatures (Scheme 1) [13].…”

“…These results strongly suggest that under these conditions, the enzymatically produced amylose did not include ORHB, and instead favorably formed a double helix structure. We then attempted to obtain the inclusion complex from ORHB by enzymatic production through the formation of water-soluble amylose without a double-helical assembly, called single amylose, at elevated temperatures (Scheme 1) [13]. The thermostable GPcatalyzed enzymatic polymerization of G-1-P from a maltotriose (G3) primer (80:1) was conducted in the presence of ORHB (MW = 530) dispersed in an acetate buffer solvent.…”

“…GPcatalyzed enzymatic polymerization under ambient conditions, such as at 45 • C, yields an insoluble amylosic product in aqueous media through the formation of a well-known double-helical assembly [11,12]. We found that enzymatic polymerization using thermostable GP (isolated from the thermophilic bacterium Aquifex aeolicus VF5) at elevated temperatures, for example, at 70 • C, produced a water-soluble amylosic product with a single chain (called single amylose) in an equilibrium state between chain elongation and cleavage reactions (polymerization and phosphorolysis, respectively) [13]. Interestingly, when the GP-catalyzed enzymatic polymerization is conducted in the presence of appropriate hydrophobic polymers dispersed in aqueous buffer solvents, these polymers are gradually included in the helical cavity of the produced amylose chains during the propagation from the short primer toward longer α(1→4)-glucan chains, leading to the formation of amylose-polymer inclusion complexes [14][15][16][17][18].…”

“…Molecules 2021, 26, x FOR PEER REVIEW 2 of 12 amylosic product with a single chain (called single amylose) in an equilibrium state between chain elongation and cleavage reactions (polymerization and phosphorolysis, respectively) [13]. Interestingly, when the GP-catalyzed enzymatic polymerization is conducted in the presence of appropriate hydrophobic polymers dispersed in aqueous buffer solvents, these polymers are gradually included in the helical cavity of the produced amylose chains during the propagation from the short primer toward longer α(1→4)-glucan chains, leading to the formation of amylose-polymer inclusion complexes [14][15][16][17][18].…”