Poly(ethylene glycol)-lipase complex that is catalytically active for alcoholysis reactions in ionic liquids

Tatsuo Maruyama, Shinichiro Nagasawa, Masahiro Goto

Research output: Contribution to journalArticle

79 Citations (Scopus)

Abstract

Lipase-catalyzed alcoholysis was investigated in three different ionic liquids. Lyophilized native lipase had a low activity in all the ionic liquids but a poly(ethylene glycol) (PEG)-lipase complex (with a molar ratio of the polymer/enzyme of 10:1) had an increased activity of over 14-fold. Of several lipases tested, PEG-lipase PS (from Pseudomonas cepacia) exhibited the highest actiyity (1.07 mmol/(hg-1 protein)) in 1-octyl-3-methylimidazolium hexafluorophosphate.

Original languageEnglish
Pages (from-to)1341-1345
Number of pages5
JournalBiotechnology Letters
Volume24
Issue number16
DOIs
Publication statusPublished - Aug 1 2002

Fingerprint

Ionic Liquids
Ethylene Glycol
Lipases
Lipase
Ionic liquids
Polyethylene glycols
Burkholderia cepacia
Polymers
Enzymes
Proteins

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Microbiology
  • Bioengineering

Cite this

Poly(ethylene glycol)-lipase complex that is catalytically active for alcoholysis reactions in ionic liquids. / Maruyama, Tatsuo; Nagasawa, Shinichiro; Goto, Masahiro.

In: Biotechnology Letters, Vol. 24, No. 16, 01.08.2002, p. 1341-1345.

Research output: Contribution to journalArticle

@article{99fd669bd43f4f72aae61fcddf641366,
title = "Poly(ethylene glycol)-lipase complex that is catalytically active for alcoholysis reactions in ionic liquids",
abstract = "Lipase-catalyzed alcoholysis was investigated in three different ionic liquids. Lyophilized native lipase had a low activity in all the ionic liquids but a poly(ethylene glycol) (PEG)-lipase complex (with a molar ratio of the polymer/enzyme of 10:1) had an increased activity of over 14-fold. Of several lipases tested, PEG-lipase PS (from Pseudomonas cepacia) exhibited the highest actiyity (1.07 mmol/(hg-1 protein)) in 1-octyl-3-methylimidazolium hexafluorophosphate.",
author = "Tatsuo Maruyama and Shinichiro Nagasawa and Masahiro Goto",
year = "2002",
month = "8",
day = "1",
doi = "10.1023/A:1019848400436",
language = "English",
volume = "24",
pages = "1341--1345",
journal = "Biotechnology Letters",
issn = "0141-5492",
publisher = "Springer Netherlands",
number = "16",

}

TY - JOUR

T1 - Poly(ethylene glycol)-lipase complex that is catalytically active for alcoholysis reactions in ionic liquids

AU - Maruyama, Tatsuo

AU - Nagasawa, Shinichiro

AU - Goto, Masahiro

PY - 2002/8/1

Y1 - 2002/8/1

N2 - Lipase-catalyzed alcoholysis was investigated in three different ionic liquids. Lyophilized native lipase had a low activity in all the ionic liquids but a poly(ethylene glycol) (PEG)-lipase complex (with a molar ratio of the polymer/enzyme of 10:1) had an increased activity of over 14-fold. Of several lipases tested, PEG-lipase PS (from Pseudomonas cepacia) exhibited the highest actiyity (1.07 mmol/(hg-1 protein)) in 1-octyl-3-methylimidazolium hexafluorophosphate.

AB - Lipase-catalyzed alcoholysis was investigated in three different ionic liquids. Lyophilized native lipase had a low activity in all the ionic liquids but a poly(ethylene glycol) (PEG)-lipase complex (with a molar ratio of the polymer/enzyme of 10:1) had an increased activity of over 14-fold. Of several lipases tested, PEG-lipase PS (from Pseudomonas cepacia) exhibited the highest actiyity (1.07 mmol/(hg-1 protein)) in 1-octyl-3-methylimidazolium hexafluorophosphate.

UR - http://www.scopus.com/inward/record.url?scp=0036670944&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036670944&partnerID=8YFLogxK

U2 - 10.1023/A:1019848400436

DO - 10.1023/A:1019848400436

M3 - Article

VL - 24

SP - 1341

EP - 1345

JO - Biotechnology Letters

JF - Biotechnology Letters

SN - 0141-5492

IS - 16

ER -