Novel Polyvinyl alcohoD-Degrading Enzyme and the Degradation Mechanism

Shuichi Matsumura; Noriyasu Tomizawa; Atsuko Toki; Kimihito Nishikawa; Kazunobu Toshima

Novel Polyvinyl alcohoD-Degrading Enzyme and the Degradation Mechanism

Shuichi Matsumura, Noriyasu Tomizawa, Atsuko Toki, Kimihito Nishikawa, Kazunobu Toshima

Department of Applied Chemistry

Research output: Contribution to journal › Article › peer-review

130 Citations (Scopus)

Abstract

A novel poly(vinyl alcohol) (PVA) degradation pathway was demonstrated such that the hydroxy group of PVA was first dehydrogenated into the corresponding carbonyl group to form the β-hydroxy ketone moiety which was followed by the aldolase-type cleavage to produce the methyl ketone and the aldehyde terminals by the PVA-assimilating strain, Alcaligenes faecalis KK314. Both the biodégradation steps of dehydrogenation and subsequent aldolase-type cleavage were catalyzed by the same protein having 67 kDa as the holoenzyme and apoenzyme of PVA dehydrogenase, respectively.

Original language	English
Pages (from-to)	7753-7761
Number of pages	9
Journal	Macromolecules
Volume	32
Issue number	23
Publication status	Published - 1999 Dec 1

ASJC Scopus subject areas

Organic Chemistry
Polymers and Plastics
Inorganic Chemistry
Materials Chemistry

Cite this

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T1 - Novel Polyvinyl alcohoD-Degrading Enzyme and the Degradation Mechanism

AU - Matsumura, Shuichi

AU - Tomizawa, Noriyasu

AU - Toki, Atsuko

AU - Nishikawa, Kimihito

AU - Toshima, Kazunobu

PY - 1999/12/1

Y1 - 1999/12/1

N2 - A novel poly(vinyl alcohol) (PVA) degradation pathway was demonstrated such that the hydroxy group of PVA was first dehydrogenated into the corresponding carbonyl group to form the β-hydroxy ketone moiety which was followed by the aldolase-type cleavage to produce the methyl ketone and the aldehyde terminals by the PVA-assimilating strain, Alcaligenes faecalis KK314. Both the biodégradation steps of dehydrogenation and subsequent aldolase-type cleavage were catalyzed by the same protein having 67 kDa as the holoenzyme and apoenzyme of PVA dehydrogenase, respectively.

AB - A novel poly(vinyl alcohol) (PVA) degradation pathway was demonstrated such that the hydroxy group of PVA was first dehydrogenated into the corresponding carbonyl group to form the β-hydroxy ketone moiety which was followed by the aldolase-type cleavage to produce the methyl ketone and the aldehyde terminals by the PVA-assimilating strain, Alcaligenes faecalis KK314. Both the biodégradation steps of dehydrogenation and subsequent aldolase-type cleavage were catalyzed by the same protein having 67 kDa as the holoenzyme and apoenzyme of PVA dehydrogenase, respectively.

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M3 - Article

AN - SCOPUS:0033355907

SN - 0024-9297

VL - 32

SP - 7753

EP - 7761

JO - Macromolecules

JF - Macromolecules

IS - 23

ER -

Novel Polyvinyl alcohoD-Degrading Enzyme and the Degradation Mechanism

Abstract

ASJC Scopus subject areas

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