Sustainable enzymatic preparation of polyaspartate using a bacterial protease

Yasuyuki Soeda, Kazunobu Toshima, Shuichi Matsumura

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Diethyl L-aspartate was polymerized by a bacterial protease from Bacillus subtilis (BS) in organic solvent at a temperature between 30 and 50 °C to yield α-linked poly(ethyl L-aspartate) having an Mw of up to 3700 and a maximum polymer yield of 85%. The best polymerization conditions were the 40 °C polymerization of diethyl L-aspartate using 30% protease BS containing 4.5 vol % water in acetonitrile for 2 days. Poly(ethyl L-aspartate) was readily depolymerized by the enzyme into the oligomeric and monomeric L-aspartate in aqueous acetonitrile. Poly(sodium aspartate) prepared by the saponification of poly(ethyl L-aspartate) was readily biodegradable by activated sludge obtained from the municipal sewage treatment plant. Also, poly(sodium aspartate) was depolymerized by the hydrolase enzyme into the monomeric aspartate. These results may indicate the sustainable chemical recycling and biorecycling of this polymer.

Original languageEnglish
Pages (from-to)196-203
Number of pages8
JournalBiomacromolecules
Volume4
Issue number2
DOIs
Publication statusPublished - 2003 Mar

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Bacilli
Acetonitrile
Aspartic Acid
Peptide Hydrolases
Enzymes
Polymerization
Sodium
Saponification
Hydrolases
Sewage treatment plants
Polymers
Organic solvents
Recycling
Sewage
Bacillus subtilis
Water
Temperature
polyaspartate

ASJC Scopus subject areas

  • Organic Chemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Polymers and Plastics
  • Materials Chemistry

Cite this

Sustainable enzymatic preparation of polyaspartate using a bacterial protease. / Soeda, Yasuyuki; Toshima, Kazunobu; Matsumura, Shuichi.

In: Biomacromolecules, Vol. 4, No. 2, 03.2003, p. 196-203.

Research output: Contribution to journalArticle

Soeda, Yasuyuki ; Toshima, Kazunobu ; Matsumura, Shuichi. / Sustainable enzymatic preparation of polyaspartate using a bacterial protease. In: Biomacromolecules. 2003 ; Vol. 4, No. 2. pp. 196-203.
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