Mechanism of enzymatic hydrolysis of poly(butylene succinate) and poly(butylene succinate-co-L-lactate) with a lipase from Pseudomonas cepacia

Ikuo Taniguchi, Shigeyuki Nakano, Tetsuro Nakamura, Ahmed El-Salmawy, Masatoshi Miyamoto, Yoshiharu Kimura

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Enzymatic hydrolysis of poly(butylene succinate) (PBS) and poly(butylene succinate-co-L-lactate) (PBSL) has been studied by using a lipase originated from Pseudomonas cepacia. It has been found that the drawn fibers of PBSL are readily hydrolyzed by the action of the lipase, while those of PBS undergo little enzymatic hydrolysis. Since the polymer films of PBS and PBSL are readily hydrolyzed under the same conditions, the enzymatic hydrolysis should depend not only on the crystallinity but also on the molecular orientation. The molecular weight of the samples gradually decreases with incubation time, because nonspecific hydrolysis occurs on the main chains of both PBS and PBSL even in the absence of lipase. The enzymatic hydrolysis of PBS and PBSL gives 4-hydroxybutyl succinate (HBS) as the main product with traces of succinic acid and butane-1,4-diol together with L-lactic acid in the case of PBSL. In addition, the hydrolysis rate of the carboxyl end-capped PBS is much slower than that of the original or hydroxyl end-capped PBS. These results imply a hydrolysis mechanism involving the preferential exo-type chain scission from the carboxyl terminals.

Original languageEnglish
Pages (from-to)447-455
Number of pages9
JournalMacromolecular Bioscience
Volume2
Issue number9
DOIs
Publication statusPublished - Jan 1 2002

Fingerprint

Burkholderia cepacia
Enzymatic hydrolysis
Lipases
Lipase
Lactic Acid
Hydrolysis
Succinic Acid
Molecular orientation
Butane
Lactic acid
Polymer films
Molecular weight
Acids
bionole
Fibers
Hydroxyl Radical
Polymers
Molecular Weight

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

Cite this

Mechanism of enzymatic hydrolysis of poly(butylene succinate) and poly(butylene succinate-co-L-lactate) with a lipase from Pseudomonas cepacia. / Taniguchi, Ikuo; Nakano, Shigeyuki; Nakamura, Tetsuro; El-Salmawy, Ahmed; Miyamoto, Masatoshi; Kimura, Yoshiharu.

In: Macromolecular Bioscience, Vol. 2, No. 9, 01.01.2002, p. 447-455.

Research output: Contribution to journalArticle

Taniguchi, Ikuo ; Nakano, Shigeyuki ; Nakamura, Tetsuro ; El-Salmawy, Ahmed ; Miyamoto, Masatoshi ; Kimura, Yoshiharu. / Mechanism of enzymatic hydrolysis of poly(butylene succinate) and poly(butylene succinate-co-L-lactate) with a lipase from Pseudomonas cepacia. In: Macromolecular Bioscience. 2002 ; Vol. 2, No. 9. pp. 447-455.
@article{b419fe19f8d049dab627256328eb5c5f,
title = "Mechanism of enzymatic hydrolysis of poly(butylene succinate) and poly(butylene succinate-co-L-lactate) with a lipase from Pseudomonas cepacia",
abstract = "Enzymatic hydrolysis of poly(butylene succinate) (PBS) and poly(butylene succinate-co-L-lactate) (PBSL) has been studied by using a lipase originated from Pseudomonas cepacia. It has been found that the drawn fibers of PBSL are readily hydrolyzed by the action of the lipase, while those of PBS undergo little enzymatic hydrolysis. Since the polymer films of PBS and PBSL are readily hydrolyzed under the same conditions, the enzymatic hydrolysis should depend not only on the crystallinity but also on the molecular orientation. The molecular weight of the samples gradually decreases with incubation time, because nonspecific hydrolysis occurs on the main chains of both PBS and PBSL even in the absence of lipase. The enzymatic hydrolysis of PBS and PBSL gives 4-hydroxybutyl succinate (HBS) as the main product with traces of succinic acid and butane-1,4-diol together with L-lactic acid in the case of PBSL. In addition, the hydrolysis rate of the carboxyl end-capped PBS is much slower than that of the original or hydroxyl end-capped PBS. These results imply a hydrolysis mechanism involving the preferential exo-type chain scission from the carboxyl terminals.",
author = "Ikuo Taniguchi and Shigeyuki Nakano and Tetsuro Nakamura and Ahmed El-Salmawy and Masatoshi Miyamoto and Yoshiharu Kimura",
year = "2002",
month = "1",
day = "1",
doi = "10.1002/mabi.200290002",
language = "English",
volume = "2",
pages = "447--455",
journal = "Macromolecular Bioscience",
issn = "1616-5187",
publisher = "Wiley-VCH Verlag",
number = "9",

}

TY - JOUR

T1 - Mechanism of enzymatic hydrolysis of poly(butylene succinate) and poly(butylene succinate-co-L-lactate) with a lipase from Pseudomonas cepacia

AU - Taniguchi, Ikuo

AU - Nakano, Shigeyuki

AU - Nakamura, Tetsuro

AU - El-Salmawy, Ahmed

AU - Miyamoto, Masatoshi

AU - Kimura, Yoshiharu

PY - 2002/1/1

Y1 - 2002/1/1

N2 - Enzymatic hydrolysis of poly(butylene succinate) (PBS) and poly(butylene succinate-co-L-lactate) (PBSL) has been studied by using a lipase originated from Pseudomonas cepacia. It has been found that the drawn fibers of PBSL are readily hydrolyzed by the action of the lipase, while those of PBS undergo little enzymatic hydrolysis. Since the polymer films of PBS and PBSL are readily hydrolyzed under the same conditions, the enzymatic hydrolysis should depend not only on the crystallinity but also on the molecular orientation. The molecular weight of the samples gradually decreases with incubation time, because nonspecific hydrolysis occurs on the main chains of both PBS and PBSL even in the absence of lipase. The enzymatic hydrolysis of PBS and PBSL gives 4-hydroxybutyl succinate (HBS) as the main product with traces of succinic acid and butane-1,4-diol together with L-lactic acid in the case of PBSL. In addition, the hydrolysis rate of the carboxyl end-capped PBS is much slower than that of the original or hydroxyl end-capped PBS. These results imply a hydrolysis mechanism involving the preferential exo-type chain scission from the carboxyl terminals.

AB - Enzymatic hydrolysis of poly(butylene succinate) (PBS) and poly(butylene succinate-co-L-lactate) (PBSL) has been studied by using a lipase originated from Pseudomonas cepacia. It has been found that the drawn fibers of PBSL are readily hydrolyzed by the action of the lipase, while those of PBS undergo little enzymatic hydrolysis. Since the polymer films of PBS and PBSL are readily hydrolyzed under the same conditions, the enzymatic hydrolysis should depend not only on the crystallinity but also on the molecular orientation. The molecular weight of the samples gradually decreases with incubation time, because nonspecific hydrolysis occurs on the main chains of both PBS and PBSL even in the absence of lipase. The enzymatic hydrolysis of PBS and PBSL gives 4-hydroxybutyl succinate (HBS) as the main product with traces of succinic acid and butane-1,4-diol together with L-lactic acid in the case of PBSL. In addition, the hydrolysis rate of the carboxyl end-capped PBS is much slower than that of the original or hydroxyl end-capped PBS. These results imply a hydrolysis mechanism involving the preferential exo-type chain scission from the carboxyl terminals.

UR - http://www.scopus.com/inward/record.url?scp=0037557086&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037557086&partnerID=8YFLogxK

U2 - 10.1002/mabi.200290002

DO - 10.1002/mabi.200290002

M3 - Article

AN - SCOPUS:0037557086

VL - 2

SP - 447

EP - 455

JO - Macromolecular Bioscience

JF - Macromolecular Bioscience

SN - 1616-5187

IS - 9

ER -