Novel Polyvinyl alcohoD-Degrading Enzyme and the Degradation Mechanism

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

Research output: Contribution to journalArticle

116 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 languageEnglish
Pages (from-to)7753-7761
Number of pages9
JournalMacromolecules
Volume32
Issue number23
Publication statusPublished - 1999

Fingerprint

Polyvinyls
Fructose-Bisphosphate Aldolase
Ketones
Enzymes
Apoenzymes
Degradation
Holoenzymes
Dehydrogenation
Aldehydes
Oxidoreductases
Alcohols
Proteins

ASJC Scopus subject areas

  • Materials Chemistry

Cite this

Matsumura, S., Tomizawa, N., Toki, A., Nishikawa, K., & Toshima, K. (1999). Novel Polyvinyl alcohoD-Degrading Enzyme and the Degradation Mechanism. Macromolecules, 32(23), 7753-7761.

Novel Polyvinyl alcohoD-Degrading Enzyme and the Degradation Mechanism. / Matsumura, Shuichi; Tomizawa, Noriyasu; Toki, Atsuko; Nishikawa, Kimihito; Toshima, Kazunobu.

In: Macromolecules, Vol. 32, No. 23, 1999, p. 7753-7761.

Research output: Contribution to journalArticle

Matsumura, S, Tomizawa, N, Toki, A, Nishikawa, K & Toshima, K 1999, 'Novel Polyvinyl alcohoD-Degrading Enzyme and the Degradation Mechanism', Macromolecules, vol. 32, no. 23, pp. 7753-7761.
Matsumura S, Tomizawa N, Toki A, Nishikawa K, Toshima K. Novel Polyvinyl alcohoD-Degrading Enzyme and the Degradation Mechanism. Macromolecules. 1999;32(23):7753-7761.
Matsumura, Shuichi ; Tomizawa, Noriyasu ; Toki, Atsuko ; Nishikawa, Kimihito ; Toshima, Kazunobu. / Novel Polyvinyl alcohoD-Degrading Enzyme and the Degradation Mechanism. In: Macromolecules. 1999 ; Vol. 32, No. 23. pp. 7753-7761.
@article{e82f4e2f9fab428f919f2980f29507d7,
title = "Novel Polyvinyl alcohoD-Degrading Enzyme and the Degradation Mechanism",
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 biod{\'e}gradation 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.",
author = "Shuichi Matsumura and Noriyasu Tomizawa and Atsuko Toki and Kimihito Nishikawa and Kazunobu Toshima",
year = "1999",
language = "English",
volume = "32",
pages = "7753--7761",
journal = "Macromolecules",
issn = "0024-9297",
publisher = "American Chemical Society",
number = "23",

}

TY - JOUR

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

Y1 - 1999

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.

UR - http://www.scopus.com/inward/record.url?scp=0033355907&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033355907&partnerID=8YFLogxK

M3 - Article

VL - 32

SP - 7753

EP - 7761

JO - Macromolecules

JF - Macromolecules

SN - 0024-9297

IS - 23

ER -