Enzymatic synthesis of novel polymer materials

 

Polymer thin film is prepared as a functional membrane on the substrate surface of a biosensor to measure the interaction between the membrane and molecules. Poly(aspartic acid), which has functional carboxyl groups, shows high biocompatibility and biodegradability. We are studying the enzymatic synthesis of poly(aspartic acid) with well-controlled structure.

 

機能性ポリアミノ酸

Schematic representation of enzymatic synthesis and degradation.

 

 

References

(1)

T. Hiraishi, Y. Hirahara, Y. Doi, M. Maeda, and S. Taguchi, “Effects of mutations in the substrate-binding domain of poly[(R)-3-hydoxybutyrate] (PHB) depolymerase from Ralstonia pickettii T1 on PHB degradation”, Appl. Environ. Microbiol., 72, 7331-7338 （2006）

(2)

Y. M. Normi, T. Hiraishi, S. Taguchi, H. Abe, K. Sudesh, N. Najimudin, Y. Doi, “Characterization and Properties of G4X Mutants of Ralstonia eutropha PHA synthase for Poly(3-hydroxybutyrate) Biosynthesis in Escherichia coli.”, Macromol. Biosci., 5, 197-206 (2005)

(3)

Y. M. Normi, T. Hiraishi, S. Taguchi, K. Sudesh, N. Najimudin, Y. Doi, “Site-directed Saturation Mutagenesis at Residue F420 and Recombination with Another Beneficial Mutation of Ralstonia eutropha PHA synthase.”, Biotechnol. Lett., 27, 705-712 (2005)

(4)

Y. Kikkawa, K. Yamashita, T. Hiraishi, M. Kanesato, Y. Doi, “Adsorption Behavior of Poly(3-hydroxybutyrate) Depolymerase on Polyester Surface Investigated by QCM and AFM.”, Biomacromolecules, 6, 2084-2090 (2005)

(5)

T. Hiraishi, Y. Kikkawa, M. Fujita, N. M. Yahaya, M. Kanesato, T. Tsuge, K. Sudesh, M. Maeda, Y. Doi, “AFM Observation of In Vitro Polymerized Poly[(R)-3-hydroxybutyrate] : Insight into Possible Mechanism of PHB Granule Formation.”, Biomacromolecules, 6, 2671-2677 (2005)

(6)

Y. Kikkawa, M. Narike, T. Hiraishi, M. Kanesato, K. Sudesh, Y. Doi, T. Tsuge, “Organization of Polyhydroxyalkanoate Synthase for In Vitro Polymerization as Revealed by Atomic Force Microscopy.”, Macromol. Biosci., 5, 929-935 (2005)

(7)

T. Hiraishi, and Y. Doi, “Enzymatic degradation of poly(aspartic acid) catalyzed by its hydrolases.”, Bio Industry, 22, 43-50 (2005)

(8)

T. Hiraishi, M. Kajiyama, I. Yamato, and Y. Doi. “Enzymatic Hydrolysis of a- and b-Oligo(L-aspartic acid)s by Poly(aspartic acid) Hydrolases-1 and 2 from Sphingomonas sp. KT-1,” Macromol. Biosci., 4, 330-339 (2004)

(9)

T. Hiraishi, M. Kajiyama, K. Tabata, H. Abe, I. Yamato, and Y. Doi, “Biochemical and Molecular Characterization of Poly(aspartic acid) Hydrolase-2 from Sphingomonas sp. KT-1.” Biomacromolecules, 4, 1285-1292 (2003)

(10)

T. Hiraishi, M. Kajiyama, K. Tabata, I. Yamato, and Y. Doi, “Genetic Analysis and Characterization of Poly(aspartic acid) Hydrolase from Sphingomonas sp. KT-1.” Biomacromolecules, 4, 80-86 (2003)

(11)

T. Hiraishi, K. Tabata, and Y. Doi, “Microbial and Enzymatic Hydrolysis of Poly(aspartic acid).” RIKEN Review, 42, 81-84 (2001)

(12)

K. Tabata, M. Kajiyama, T. Hiraishi, H. Abe, I. Yamato, and Y. Doi, “Function and characterization of poly(aspartic acid) hydrolase from Sphingomonas sp. KT-1.”, Biomacromolecules, 2, 1155-1160 (2001)

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